Curator Name UniProt ID NCBI Gene ID Gene Name Species Name Taxonomy ID Data Type Data Value Value Unit ChEBI Chemical Term A ChEBI Chemical ID A ChEBI Chemical Term B ChEBI Chemical ID B Secondary Source IDs Secondary Source Notes Reviewed (Y/N) Use (Y/N) Evidence Code Primary Source Secondary Source PENTACON Notes Gene Set Secondary Source Version Date Secondary Source Version PENTACON Annotation No Faith Q6E213 158835 AWAT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 549 pmol/min/mg hexadecan-1-ol CHEBI:16125 stearoyl-CoA CHEBI:15541 Y Y ECO:0000006 PubMed:15671038 Two substrates, where first substrate is [14C] labeled. Info added from publication AAP 10/31/2012 72 2000000075 Faith O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.2 mM for glutathione for the prostaglandin D synthase activity 0.2 mM glutathione CHEBI:16856 prostaglandin H2 CHEBI:15554 Y Y PubMed:10824118 PGDS activity listed as 30 umol/min/mg. However, does not explicitely state this is the Vmax. AAP 2000000170 Faith Q6E213 158835 AWAT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 524 pmol/min/mg hexadecan-1-ol CHEBI:16125 palmitoyl-CoA CHEBI:15525 Y Y ECO:0000006 PubMed:15671038 Two substrates, where first substrate is [14C] labeled. Info added from publication AAP 10/31/2012 72 2000000065 Faith Q6E213 158835 AWAT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 1125 pmol/min/mg hexadecan-1-ol CHEBI:16125 palmitoleoyl-CoA CHEBI:53152 Y Y ECO:0000006 PubMed:15671038 Two substrates, where first substrate is [14C] labeled. Info added from publication AAP 10/31/2012 72 2000000076 Faith Q6E213 158835 AWAT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 11.4 pmol/min/mg 1,2-dioleoyl-sn-glycerol CHEBI:52333 oleoyl-CoA CHEBI:15534 Y Y ECO:0000006 PubMed:15671038 Two substrates, where second substrate is [14C] labeled. Info added from publication AAP 10/31/2012 72 2000000066 Faith Q6E213 158835 AWAT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 27 pmol/min/mg Arachidyl C-20 alcohol oleoyl-CoA CHEBI:15534 Y Y ECO:0000006 PubMed:15671038 I cannot find the first substrate. The class is 'fatty alcohol'. There is also a 'arachidyl group' in ChEBI. Two substrates, where second substrate is [14C] labeled. Info added from publication Request: arachidyl alcohol AAP 10/31/2012 72 2000000067 Faith Q6E213 158835 AWAT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 1232 pmol/min/mg enzyme with [14C]cetyl-CoA as substrate 1232 pmol/min/mg hexadecan-1-ol CHEBI:16125 oleoyl-CoA CHEBI:15534 Y Y ECO:0000006 PubMed:15671038 UniProtKB Info in UniProt is incorrect. I will send an email to UniProt. Substrate 1 is [14C] labeled hexadecan-1-ol AAP 10/31/2012 72 2000000069 Faith Q6E213 158835 AWAT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 1066 pmol/min/mg hexadecan-1-ol CHEBI:16125 oleoyl-CoA CHEBI:15534 Y Y ECO:0000006 PubMed:15671038 Two substrates, where second substrate is [14C] labeled. Info added from publication AAP 10/31/2012 72 2000000070 Faith Q6E213 158835 AWAT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 665 pmol/min/mg hexadecan-1-ol CHEBI:16125 oleoyl-CoA CHEBI:15534 Y Y ECO:0000006 PubMed:15671038 Two substrates, where second substrate is [14C] labeled. Info added from publication AAP 10/31/2012 72 2000000071 Faith Q6E213 158835 AWAT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 892 pmol/min/mg Oleyl C-18:1 alcohol oleoyl-CoA CHEBI:15534 Y Y ECO:0000006 PubMed:15671038 Two substrates, where second substrate is [14C] labeled. Info added from publication Request: oleyl alcohol AAP 10/31/2012 72 2000000072 Faith Q6E213 158835 AWAT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 582 pmol/min/mg Palmitoleyl C-16:1 alcohol oleoyl-CoA CHEBI:15534 Y Y ECO:0000006 PubMed:15671038 Two substrates, where second substrate is [14C] labeled. Info added from publication Request: palmitoleyl alcohol AAP 10/31/2012 72 2000000073 Faith Q6E213 158835 AWAT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 138 pmol/min/mg stearyl alcohol CHEBI:32154 oleoyl-CoA CHEBI:15534 Y Y ECO:0000006 PubMed:15671038 Two substrates, where second substrate is [14C] labeled. Info added from publication AAP 10/31/2012 72 2000000074 Faith Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 6247 nmol/min/mg enzyme with arachidonoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates 6247 nmol/min/mg arachidonoyl-CoA CHEBI:15514 lysophosphatidylcholine 16:0 CHEBI:64563 Y Y ECO:0000311 UniProtKB Two substrates are required. The second substrate is given in Column N. LPC16:0 covers a connection of palmitoyl at either 1 or 2 in the glycero moiety. AAP 1/9/2013 82 2000000139 Faith Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 18148 nmol/min/mg enzyme with linoleoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates 18148 nmol/min/mg linoleoyl-CoA CHEBI:15530 lysophosphatidylcholine 16:0 CHEBI:64563 Y Y ECO:0000311 UniProtKB Two substrates are required. The second substrate is given in Column N. LPC16:0 covers a connection of palmitoyl at either 1 or 2 in the glycero moiety. AAP 1/9/2013 82 2000000140 Faith Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 4698 nmol/min/mg enzyme with oleoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates 4698 nmol/min/mg oleoyl-CoA CHEBI:15534 lysophosphatidylcholine 16:0 CHEBI:64563 Y Y ECO:0000311 UniProtKB Two substrates are required. The second substrate is given in Column N. LPC16:0 covers a connection of palmitoyl at either 1 or 2 in the glycero moiety. AAP 1/9/2013 82 2000000141 Faith Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 1782 nmol/min/mg enzyme with palmitoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates 1782 nmol/min/mg palmitoyl-CoA CHEBI:15525 lysophosphatidylcholine 16:0 CHEBI:64563 Y Y ECO:0000311 UniProtKB Two substrates are required. The second substrate is given in Column N. LPC16:0 covers a connection of palmitoyl at either 1 or 2 in the glycero moiety. AAP 1/9/2013 82 2000000142 Faith Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 996 nmol/min/mg enzyme with stearoyl-CoA and 1-palmitoyl-lysophosphatidylcholine as substrates 996 nmol/min/mg stearoyl-CoA CHEBI:15541 lysophosphatidylcholine 16:0 CHEBI:64563 Y Y ECO:0000311 UniProtKB Two substrates are required. The second substrate is given in Column N. LPC16:0 covers a connection of palmitoyl at either 1 or 2 in the glycero moiety. AAP 1/9/2013 82 2000000143 Faith O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.2 mM for PGH2 for the prostaglandin D synthase activity 0.2 mM prostaglandin H2 CHEBI:15554 glutathione CHEBI:16856 Y Y PubMed:10824118 PGDS activity listed as 30 umol/min/mg. However, does not explicitely state this is the Vmax. AAP 2000000171 Faith Q14032 570 BAAT Homo sapiens 9606 Comment/biophysicochemical properties/KM 1.1 mM for taurine toward choloyl-CoA 1.1 mM taurine CHEBI:15891 choloyl-CoA CHEBI:15519 Y Y ECO:0000006 PubMed:8034703 UniProtKB AAP 5/1/2013 102 2000000077 Faith Q14032 570 BAAT Homo sapiens 9606 Comment/biophysicochemical properties/KM 5.8 mM for glycine toward choloyl-CoA 5.8 mM glycine CHEBI:15428 choloyl-CoA CHEBI:15519 Y Y UniProtKB AAP 5/1/2013 102 2000000079 Rose P24752 38 ACAT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 4 uM for acteoacetyl coenzyme A 4 uM acetoacetyl-CoA CHEBI:15345 Y Y ECO:0000006 PubMed:17371050 UniProtKB AAP 11/28/2012 141 2000000001 Rose P24752 38 ACAT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 20 uM for coenzyme A 20 uM acetoacetyl-CoA CHEBI:15345 Y Y ECO:0000311 UniProtKB AAP 11/28/2012 141 2000000002 Rose P24752 38 ACAT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 8 uM for 2-methylacteoacetyl coenzyme A 8 uM acetoacetyl-CoA CHEBI:15345 Y Y ECO:0000311 UniProtKB 2-methylacteoacetyl coenzyme A not in ChEBI, send request. AAP 11/28/2012 141 2000000003 Rose P24752 38 ACAT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 508 uM for acetyl coenzyme A 508 uM acetoacetyl-CoA CHEBI:15345 Y Y ECO:0000311 UniProtKB AAP 11/28/2012 141 2000000004 Faith Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 35.8 uM for C10-acyl-CoA 35.8 uM decanoyl-CoA CHEBI:28493 Y Y ECO:0000006 PubMed:16940157 UniProtKB AAP 5/1/2013 87 2000000005 Faith Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 3.6 uM for C12-acyl-CoA 3.6 uM lauroyl-CoA CHEBI:15521 Y Y PubMed:16940157 UniProtKB AAP 5/1/2013 87 2000000006 Faith Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 2.8 uM for C14-acyl-CoA 2.8 uM myristoyl-CoA CHEBI:15532 Y Y PubMed:16940157 UniProtKB AAP 5/1/2013 87 2000000007 Faith Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 3.6 uM for C16-acyl-CoA 3.6 uM palmitoyl-CoA CHEBI:15525 Y Y PubMed:16940157 UniProtKB AAP 5/1/2013 87 2000000008 Faith Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 2.4 uM for C18-acyl-CoA 2.4 uM stearoyl-CoA CHEBI:15541 Y Y PubMed:16940157 UniProtKB AAP 5/1/2013 87 2000000009 Faith Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 2 uM for C20-acyl-CoA 2 uM icosanoyl-CoA CHEBI:15527 Y Y PubMed:16940157 UniProtKB AAP 5/1/2013 87 2000000010 Faith Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 2.4 uM for C16:1-acyl-CoA 2.4 uM hexadecenoyl-CoA CHEBI:24549 Y Y PubMed:16940157 UniProtKB AAP 5/1/2013 87 2000000011 Faith Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 4.1 uM for C18:1-acyl-CoA 4.1 uM unsaturated fatty acyl-CoA CHEBI:51006 Y Y PubMed:16940157 UniProtKB C18:1-acyl-CoA (should we assume that this is oleoyl-CoA?) AAP 5/1/2013 87 2000000012 Faith Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 2.1 uM for C18:1-trans-acyl-CoA 2.1 uM unsaturated fatty acyl-CoA CHEBI:51006 Y Y PubMed:16940157 UniProtKB C18:1-trans-acyl-CoA AAP 5/1/2013 87 2000000013 Faith Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 224 nmol/min/mg enzyme toward C10-acyl-CoA 224 nmol/min/mg decanoyl-CoA CHEBI:28493 Y Y PubMed:16940157 UniProtKB AAP 5/1/2013 87 2000000014 Faith Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 700 nmol/min/mg enzyme toward C12-acyl-CoA 700 nmol/min/mg lauroyl-CoA CHEBI:15521 Y Y PubMed:16940157 UniProtKB AAP 5/1/2013 87 2000000015 Faith Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 912 nmol/min/mg enzyme toward C14-acyl-CoA 912 nmol/min/mg myristoyl-CoA CHEBI:15532 Y Y PubMed:16940157 UniProtKB AAP 5/1/2013 87 2000000016 Faith Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 691 nmol/min/mg enzyme toward C16-acyl-CoA 691 nmol/min/mg palmitoyl-CoA CHEBI:15525 Y Y PubMed:16940157 UniProtKB AAP 5/1/2013 87 2000000017 Faith Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 597 nmol/min/mg enzyme toward C18-acyl-CoA 597 nmol/min/mg stearoyl-CoA CHEBI:15541 Y Y PubMed:16940157 UniProtKB AAP 5/1/2013 87 2000000018 Faith Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 520 nmol/min/mg enzyme toward C20-acyl-CoA 520 nmol/min/mg icosanoyl-CoA CHEBI:15527 Y Y PubMed:16940157 UniProtKB AAP 5/1/2013 87 2000000019 Faith Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 577 nmol/min/mg enzyme toward C16:1-acyl-CoA 577 nmol/min/mg hexadecenoyl-CoA CHEBI:24549 Y Y PubMed:16940157 UniProtKB AAP 5/1/2013 87 2000000020 Faith Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 258 nmol/min/mg enzyme toward C18:1-acyl-CoA 258 nmol/min/mg unsaturated fatty acyl-CoA CHEBI:51006 Y Y PubMed:16940157 UniProtKB C18:1-acyl-CoA (should we assume that this is oleoyl-CoA?) AAP 5/1/2013 87 2000000021 Faith Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 309 nmol/min/mg enzyme toward C18:1-trans-acyl-CoA 309 nmol/min/mg unsaturated fatty acyl-CoA CHEBI:51006 Y Y PubMed:16940157 UniProtKB C18:1-trans-acyl-CoA AAP 5/1/2013 87 2000000022 Faith Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM 4.9 uM for n-decanoyl-CoA 4.9 uM decanoyl-CoA CHEBI:28493 Y Y ECO:0000006 PubMed:19170545 UniProtKB n-decanoyl-CoA AAP 5/29/2013 101 2000000023 Faith Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM 26 uM for n-octanoyl-CoA 26 uM octanoyl-CoA CHEBI:15533 Y Y PubMed:19170545 UniProtKB n-octanoyl-CoA AAP 5/29/2013 101 2000000024 Faith Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM 5 uM for myristoyl-CoA 5 uM myristoyl-CoA CHEBI:15532 Y Y UniProtKB AAP 5/29/2013 101 2000000025 Faith Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM 9 uM for palmitoyl-CoA 9 uM palmitoyl-CoA CHEBI:15525 Y Y UniProtKB AAP 5/29/2013 101 2000000026 Faith Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM 9 uM for oleoyl-CoA 9 uM oleoyl-CoA CHEBI:15534 Y Y UniProtKB AAP 5/29/2013 101 2000000027 Faith Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM 10 uM for 3,4-dihydrohyphenylacetyl-CoA 10 uM phenylacetyl-CoAs CHEBI:25981 Y Y PubMed:19170545 UniProtKB Typo in UniProt will be fixed in October release. Chemical name is 3,4-dihydroxyphenylacetyl-CoA (not in ChEBI). AAP 5/29/2013 101 2000000028 Faith Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM 40 uM for 3-hydrohyphenylacetyl-CoA 40 uM phenylacetyl-CoAs CHEBI:25981 Y Y PubMed:19170545 UniProtKB Typo in UniProt will be fixed in October release. Chemical name is 3-hydroxyphenylacetyl-CoA (not in ChEBI). AAP 5/29/2013 101 2000000029 Faith Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM 20 uM for arachidonoyl-CoA 20 uM arachidonoyl-CoA CHEBI:15514 Y Y PubMed:19170545 Many substrates from this paper are not listed in UniProt. I added this one due to the scope of PENTACON. AAP 5/29/2013 101 2000000030 Faith P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 40.3 uM for C10-acyl-CoA 40.3 uM decanoyl-CoA CHEBI:28493 Y Y ECO:0000006 PubMed:16940157 UniProtKB AAP 5/29/2013 127 2000000031 Faith P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 8.9 uM for C12-acyl-CoA 8.9 uM lauroyl-CoA CHEBI:15521 Y Y PubMed:16940157 UniProtKB AAP 5/29/2013 127 2000000032 Faith P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 1.6 uM for C14-acyl-CoA 1.6 uM myristoyl-CoA CHEBI:15532 Y Y PubMed:16940157 UniProtKB AAP 5/29/2013 127 2000000033 Faith P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 2.0 uM for C16-acyl-CoA 2 uM palmitoyl-CoA CHEBI:15525 Y Y PubMed:16940157 UniProtKB AAP 5/29/2013 127 2000000034 Faith P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 2.8 uM for C18-acyl-CoA 2.8 uM stearoyl-CoA CHEBI:15541 Y Y PubMed:16940157 UniProtKB AAP 5/29/2013 127 2000000035 Faith P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 4.8 uM for C20-acyl-CoA 4.8 uM icosanoyl-CoA CHEBI:15527 Y Y PubMed:16940157 UniProtKB AAP 5/29/2013 127 2000000036 Faith P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 4.5 uM for C16:1-acyl-CoA 4.5 uM hexadecenoyl-CoA CHEBI:24549 Y Y PubMed:16940157 UniProtKB AAP 5/29/2013 127 2000000037 Faith P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 6.1 uM for C18:1-acyl-CoA 6.1 uM unsaturated fatty acyl-CoA CHEBI:51006 Y Y UniProtKB C18:1-acyl-CoA (should we assume that this is oleoyl-CoA?) AAP 5/29/2013 127 2000000038 Faith P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 4.3 uM for C18:1-trans-acyl-CoA 4.3 uM unsaturated fatty acyl-CoA CHEBI:51006 Y Y UniProtKB C18:1-trans-acyl-CoA AAP 5/29/2013 127 2000000039 Faith P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 212 nmol/min/mg enzyme toward C10-acyl-CoA 212 nmol/min/mg decanoyl-CoA CHEBI:28493 Y Y PubMed:16940157 UniProtKB AAP 5/29/2013 127 2000000040 Faith P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 681 nmol/min/mg enzyme toward C12-acyl-CoA 681 nmol/min/mg lauroyl-CoA CHEBI:15521 Y Y PubMed:16940157 UniProtKB AAP 5/29/2013 127 2000000041 Faith P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 766 nmol/min/mg enzyme toward C14-acyl-CoA 766 nmol/min/mg myristoyl-CoA CHEBI:15532 Y Y PubMed:16940157 UniProtKB AAP 5/29/2013 127 2000000042 Faith P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 656 nmol/min/mg enzyme toward C16-acyl-CoA 656 nmol/min/mg palmitoyl-CoA CHEBI:15525 Y Y PubMed:16940157 UniProtKB AAP 5/29/2013 127 2000000043 Faith P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 488 nmol/min/mg enzyme toward C18-acyl-CoA 488 nmol/min/mg stearoyl-CoA CHEBI:15541 Y Y PubMed:16940157 UniProtKB AAP 5/29/2013 127 2000000044 Faith P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 408 nmol/min/mg enzyme toward C20-acyl-CoA 408 nmol/min/mg icosanoyl-CoA CHEBI:15527 Y Y PubMed:16940157 UniProtKB AAP 5/29/2013 127 2000000045 Faith P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 661 nmol/min/mg enzyme toward C16:1-acyl-CoA 661 nmol/min/mg hexadecenoyl-CoA CHEBI:24549 Y Y PubMed:16940157 UniProtKB AAP 5/29/2013 127 2000000046 Faith P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 304 nmol/min/mg enzyme toward C18:1-acyl-CoA 304 nmol/min/mg unsaturated fatty acyl-CoA CHEBI:51006 Y Y UniProtKB C18:1-acyl-CoA (should we assume that this is oleoyl-CoA?) AAP 5/29/2013 127 2000000047 Faith P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 418 nmol/min/mg enzyme toward C18:1-trans-acyl-CoA 418 nmol/min/mg unsaturated fatty acyl-CoA CHEBI:51006 Y Y UniProtKB C18:1-trans-acyl-CoA AAP 5/29/2013 127 2000000048 Faith Q8N9L9 122970 ACOT4 Homo sapiens 9606 Comment/biophysicochemical properties/KM 14 uM for succinyl-CoA 14 uM succinyl-CoA CHEBI:15380 Y Y ECO:0000006 PubMed:16940157 UniProtKB AAP 5/1/2013 92 2000000049 Faith Q8N9L9 122970 ACOT4 Homo sapiens 9606 Comment/biophysicochemical properties/KM 147 uM for glutaryl-CoA 147 uM glutaryl-CoA CHEBI:15524 Y Y PubMed:16940157 UniProtKB AAP 5/1/2013 92 2000000050 Faith Q8N9L9 122970 ACOT4 Homo sapiens 9606 Comment/biophysicochemical properties/KM 3.4 uM for C14-acyl-CoA 3.4 uM myristoyl-CoA CHEBI:15532 Y Y PubMed:16940157 UniProtKB AAP 5/1/2013 92 2000000051 Faith Q8N9L9 122970 ACOT4 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 581 nmol/min/mg enzyme toward succinyl-CoA 581 nmol/min/mg succinyl-CoA CHEBI:15380 Y Y PubMed:16940157 UniProtKB AAP 5/1/2013 92 2000000052 Faith Q8N9L9 122970 ACOT4 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 132 nmol/min/mg enzyme toward glutaryl-CoA 132 nmol/min/mg glutaryl-CoA CHEBI:15524 Y Y PubMed:16940157 UniProtKB AAP 5/1/2013 92 2000000053 Faith Q8N9L9 122970 ACOT4 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 137 nmol/min/mg enzyme toward C14-acyl-CoA 137 nmol/min/mg myristoyl-CoA CHEBI:15532 Y Y PubMed:16940157 UniProtKB AAP 5/1/2013 92 2000000054 Katie Q9ULC5 51703 ACSL5 Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.11 uM for palmitic acid (isoform 1 at pH 7.5) 0.11 uM palmitic acid CHEBI:15756 Y Y ECO:0000006 PubMed:17681178 UniProtKB Curated by Faith. pH 7.5 AAP 11/28/2012 121 2000000055 Katie Q9ULC5 51703 ACSL5 Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.38 uM for palmitic acid (isoform 1 at pH 9.5) 0.38 uM palmitic acid CHEBI:15756 Y Y ECO:0000311 UniProtKB Curated by Faith AAP 11/28/2012 121 2000000056 Katie Q9ULC5 51703 ACSL5 Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.04 uM for palmitic acid (isoform 3 at pH 7.5) 0.04 uM palmitic acid CHEBI:15756 Y Y ECO:0000311 UniProtKB Curated by Faith AAP 11/28/2012 121 2000000057 Katie Q9ULC5 51703 ACSL5 Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.15 uM for palmitic acid (isoform 3 at pH 8.5) 0.15 uM palmitic acid CHEBI:15756 Y Y ECO:0000311 UniProtKB Curated by Faith AAP 11/28/2012 121 2000000058 Rose P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/KM 1.0 uM for androstanediol 1 uM androstane-3,17-diol CHEBI:27727 Y Y ECO:0000311 UniProtKB AAP 2/6/2013 142 2000000059 Rose P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 4.4 nmol/min/mg enzyme with androstanediol as substrate 4.4 nmol/min/mg androstane-3,17-diol CHEBI:27727 Y Y ECO:0000311 UniProtKB AAP 2/6/2013 142 2000000060 Rose P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/KM 142.1 uM for progesterone 142.1 uM progesterone CHEBI:17026 Y Y ECO:0000006 PubMed:10557352 UniProtKB AAP 2/6/2013 142 2000000061 Rose P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 20.1 nmol/min/mg enzyme with progesterone as substrate 20.1 nmol/min/mg progesterone CHEBI:17026 Y Y ECO:0000311 UniProtKB AAP 2/6/2013 142 2000000062 Rose P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/KM 2.37 uM for 5-alpha-dihydrotestosterone 2.37 uM testosterone CHEBI:17347 Y Y ECO:0000311 UniProtKB 5-alpha-dihydrotestosterone not in ChEBI, send request. AAP 2/6/2013 142 2000000063 Rose P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 1.8 nmol/min/mg enzyme with 5-alpha-dihydrotestosterone as substrate 1.8 nmol/min/mg testosterone CHEBI:17347 Y Y ECO:0000311 UniProtKB AAP 2/6/2013 142 2000000064 Faith Q14032 570 BAAT Homo sapiens 9606 Comment/biophysicochemical properties/KM 2.2 mM for 2-fluoro-beta-alanine toward choloyl-CoA 2.2 mM beta-alanine derivative CHEBI:22823 Y Y UniProtKB 2-fluoro-beta-alanine AAP 5/1/2013 102 2000000078 Faith Q14032 570 BAAT Homo sapiens 9606 Comment/biophysicochemical properties/KM 19.3 uM for arachidoyl-CoA 19.3 uM icosanoyl-CoA CHEBI:15527 Y Y UniProtKB AAP 5/1/2013 102 2000000080 Faith Q14032 570 BAAT Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 0.33 umol/min/mg enzyme with taurine as substrate for acyltransferase activity 0.33 umol/min/mg taurine CHEBI:15891 Y Y UniProtKB AAP 5/1/2013 102 2000000081 Faith Q14032 570 BAAT Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 0.19 umol/min/mg enzyme with 2-fluoro-beta-alanine as substrate for acyltransferase activity 0.19 umol/min/mg beta-alanine derivative CHEBI:22823 Y Y UniProtKB 2-fluoro-beta-alanine AAP 5/1/2013 102 2000000082 Faith Q14032 570 BAAT Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 0.77 umol/min/mg enzyme with glycine as substrate for acyltransferase activity 0.77 umol/min/mg glycine CHEBI:15428 Y Y UniProtKB AAP 5/1/2013 102 2000000083 Faith Q14032 570 BAAT Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 223 nmol/min/mg enzyme with arachidoyl-CoA as substrate for acyl-CoA thioesterase activity 223 nmol/min/mg icosanoyl-CoA CHEBI:15527 Y Y UniProtKB AAP 5/1/2013 102 2000000084 Mike P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 173 uM for daunorubicin 173 uM daunorubicin CHEBI:41977 Y Y ECO:0000311 UniProtKB AAP 11/28/2012 147 2000000085 Mike P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 22 uM for menadione 22 uM menadione CHEBI:28869 Y Y ECO:0000311 UniProtKB AAP 11/28/2012 147 2000000086 Mike P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 247 uM for NADPH 247 uM NADPH CHEBI:16474 Y Y ECO:0000311 UniProtKB AAP 11/28/2012 147 2000000087 Mike P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 309 uM for prostaglandin E2 309 uM prostaglandin E2 CHEBI:15551 Y Y ECO:0000311 UniProtKB AAP 11/28/2012 147 2000000088 Mike P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 30 uM for S-nitrosoglutathione 30 uM S-nitrosoglutathione CHEBI:50091 Y Y ECO:0000006 PubMed:18826943 PubMed:17344335 UniProtKB AAP 11/28/2012 147 2000000089 Mike O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM 25 uM for menadione (PubMed:15537833) 25 uM menadione CHEBI:28869 Y Y ECO:0000006 PubMed:15537833 UniProtKB AAP 11/28/2012 115 2000000090 Mike O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM 43 uM for menadione (PubMed:18493841) 43 uM menadione CHEBI:28869 Y Y ECO:0000006 PubMed:18493841 UniProtKB AAP 11/28/2012 115 2000000091 Mike O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM 90 uM for NADPH (PubMed:15537833) 90 uM NADPH CHEBI:16474 Y Y ECO:0000006 PubMed:15537833 UniProtKB AAP 11/28/2012 115 2000000092 Mike O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM 38 uM for NADPH (PubMed:18493841) 38 uM NADPH CHEBI:16474 Y Y ECO:0000006 PubMed:18493841 UniProtKB AAP 11/28/2012 115 2000000093 Mike P05177 1544 CYP1A2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 71 uM for 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine 71 uM 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine Y Y ECO:0000311 UniProtKB request from ChEBI:2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine AAP 11/28/2012 140 2000000094 Mike P05177 1544 CYP1A2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 26 uM for 2-amino-2,4-dimethylimidazo[4,5-f]quinoline 26 uM 2-amino-2,4-dimethylimidazo[4,5-f]quinoline Y Y ECO:0000311 UniProtKB request from ChEBI:2-amino-2,4-dimethylimidazo[4,5-f]quinoline AAP 11/28/2012 140 2000000095 Mike P05177 1544 CYP1A2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 21 uM for 2-amino-3-methylimidazo[4,5-f]quinoline 21 uM 2-amino-3-methylimidazo[4,5-f]quinoline Y Y ECO:0000311 UniProtKB request from ChEBI: 2-amino-3-methylimidazo[4,5-f]quinoline AAP 11/28/2012 140 2000000096 Mike P05177 1544 CYP1A2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 27 uM for 2-amino-3,8-dimethylimidazo[4,5-f]quinoxaline 27 uM 2-amino-3,8-dimethylimidazo[4,5-f]quinoxaline Y Y ECO:0000311 UniProtKB request from ChEBI:2-amino-3,8-dimethylimidazo[4,5-f]quinoxaline AAP 11/28/2012 140 2000000097 Mike/Rose P05177 1544 CYP1A2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 4 uM for 2-amino-6-methyldipyrido[1,2-a:3',2'-d]imidazole 4 uM 2-amino-6-methyldipyrido[1,2-a:3',2'-d]imidazole Y Y ECO:0000006 PubMed:14725854 UniProtKB request from ChEBI: 2-amino-6-methyldipyrido[1,2-a:3',2'-d]imidazole; PUBCHEMcid:49971 AAP 11/28/2012 140 2000000098 Mike P05177 1544 CYP1A2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 25 uM for phenacetin 25 uM phenacetin CHEBI:8050 Y Y ECO:0000311 UniProtKB AAP 11/28/2012 140 2000000099 Katie Q16678 1545 CYP1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 6.0 uM for 17-beta-estradiol 6 uM 17beta-estradiol CHEBI:16469 Y Y ECO:0000006 PubMed:10426814 UniProtKB Curated by Faith AAP 11/28/2012 148 2000000100 Katie Q16678 1545 CYP1B1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 14.95 nmol/min/mg enzyme for 17-beta-estradiol 4-hydroxylation 14.95 nmol/min/mg 17beta-estradiol CHEBI:16469 Y Y ECO:0000311 UniProtKB Curated by Faith 4-hydroxylation AAP 11/28/2012 148 2000000101 Katie Q16678 1545 CYP1B1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 6.9 nmol/min/mg enzyme for 17-beta-estradiol 2-hydroxylation 6.9 nmol/min/mg 17beta-estradiol CHEBI:16469 Y Y ECO:0000311 UniProtKB Curated by Faith 2-hydroxylation AAP 11/28/2012 148 2000000102 Katie Q16678 1545 CYP1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 24.0 uM for progesterone 24 uM progesterone CHEBI:17026 Y Y ECO:0000311 UniProtKB Curated by Faith AAP 11/28/2012 148 2000000103 Katie Q16678 1545 CYP1B1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 9.86 nmol/min/mg enzyme for progesterone 6-beta-hydroxylation 9.86 nmol/min/mg progesterone CHEBI:17026 Y Y ECO:0000311 UniProtKB Curated by Faith AAP 11/28/2012 148 2000000104 Katie Q16678 1545 CYP1B1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 37.80 nmol/min/mg enzyme for progesterone 16-alpha-hydroxylation 37.8 nmol/min/mg progesterone CHEBI:17026 Y Y ECO:0000311 UniProtKB Curated by Faith AAP 11/28/2012 148 2000000105 Katie/Faith Q16678 1545 CYP1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 17.0 uM for testosterone 17 uM testosterone CHEBI:17347 Y Y ECO:0000311 UniProtKB Curated by Faith AAP 11/28/2012 148 2000000106 Katie/Faith Q16678 1545 CYP1B1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 36.16 nmol/min/mg enzyme for testosterone 6-beta-hydroxylation 36.16 nmol/min/mg testosterone CHEBI:17347 Y Y ECO:0000311 UniProtKB Curated by Faith AAP 11/28/2012 148 2000000107 Rose P20813 1555 CYP2B6 Homo sapiens 9606 Comment/biophysicochemical properties/KM 360 uM for 1,4-cineole 360 uM cineole CHEBI:23243 Y Y ECO:0000006 PubMed:11695850 UniProtKB 1,4-cineole not in ChEBI, send request. AAP 11/28/2012 143 2000000108 Rose P20813 1555 CYP2B6 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 3.4 nmol/min/nmol enzyme toward 2-exo-hydroxy-1,4-cineole 3.4 nmol/min/nmol cineole CHEBI:23243 Y Y ECO:0000311 UniProtKB 2-exo-hydroxy-1,4-cineole not in ChEBI,send request. AAP 11/28/2012 143 2000000109 Faith Q7Z449 113612 CYP2U1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 2.7 uM for arachidonic acid 2.7 uM arachidonic acid CHEBI:15843 Y Y ECO:0000311 UniProtKB AAP 11/28/2012 94 2000000110 Faith Q5TCH4 284541 CYP4A22 Homo sapiens 9606 Comment/biophysicochemical properties/KM 56.7 uM for laurate 56.7 uM laurate CHEBI:18262 Y Y ECO:0000006 PubMed:10860550 UniProtKB AAP 11/28/2012 75 2000000111 Faith Q5TCH4 284541 CYP4A22 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax Vmax:15.2 umol/min/umol enzyme. 15.2 umol/min/umol laurate CHEBI:18262 Y Y ECO:0000006 PubMed:10860550 UniProtKB AAP 11/28/2012 75 2000000112 Faith P98187 11283 CYP4F8 Homo sapiens 9606 Comment/biophysicochemical properties/KM 7 uM for 9-alpha,11-alpha-epoxymethano-PGH2 (U-44069) 7 uM prostaglandin H2 CHEBI:15554 Y Y ECO:0000006 PubMed:10791960 UniProtKB Substrate used is a stable analog of PGH2. Request: 9-alpha,11-alpha-epoxymethano-PGH2 (U-44069) AAP 2/6/2013 106 2000000113 Faith P98187 11283 CYP4F8 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax The Vmax of the reaction with U-44069 as substrate is 260 pmol/min/pmol enzyme. 260 pmol/min/pmol prostaglandin H2 CHEBI:15554 Y Y ECO:0000006 PubMed:10791960 UniProtKB Substrate used is a stable analog of PGH2. Request: 9-alpha,11-alpha-epoxymethano-PGH2 (U-44069) AAP 2/6/2013 106 2000000114 Faith P98187 11283 CYP4F8 Homo sapiens 9606 Comment/biophysicochemical properties/KM 40 uM for 6,9-alpha-methylene-PGI2 40 uM prostaglandin I2 CHEBI:15552 Y Y ECO:0000006 PubMed:15789615 UniProtKB Substrate used is a stable analog of PGI2. Request: 6,9-alpha-methylene-PGI2 AAP 2/6/2013 106 2000000115 Rose P34913 2053 EPHX2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 1.1 mM for p-nitrophenyl phosphate 1.1 mM 4-nitrophenyl phosphate CHEBI:17440 Y Y ECO:0000311 UniProtKB AAP 1/9/2013 131 2000000116 Rose P34913 2053 EPHX2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 5.8 nmol/min/mg enzyme with p-nitrophenyl phosphate 5.8 nmol/min/mg 4-nitrophenyl phosphate CHEBI:17440 Y Y ECO:0000311 UniProtKB AAP 1/9/2013 131 2000000117 Rose P34913 2053 EPHX2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 338 nmol/min/mg enzyme with threo-9,10-phosphonooxy-hydroxy-octadecanoic acid 338 nmol/min/mg Y Y ECO:0000311 UniProtKB AAP 1/9/2013 131 2000000119 Katie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM 38 uM for NAD 38 uM NAD(+) CHEBI:15846 Y Y ECO:0000006 PubMed:16828555 UniProtKB Curated by Faith. I put NAD+ instead of NAD because that is how substrate is listed in the ref AAP 2/6/2013 135 2000000120 Katie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM 3.4 uM for prostaglandin E2 3.4 uM prostaglandin E2 CHEBI:15551 Y Y ECO:0000006 PubMed:16828555 UniProtKB Curated by Faith AAP 2/6/2013 135 2000000121 Mike O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 5.1 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as substrate 5.1 umol/min/mg 1-chloro-2,4-dinitrobenzene CHEBI:34718 Y Y ECO:0000311 UniProtKB AAP 2/6/2013 124 2000000122 Mike O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 44.3 umol/min/mg enzyme with 1-fluoro-2,4-dinitrobenzene as substrate 44.3 umol/min/mg 1-fluoro-2,4-dinitrobenzene CHEBI:53049 Y Y ECO:0000311 UniProtKB AAP 2/6/2013 124 2000000123 Mike/Rose O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 6.8 umol/min/mg enzyme with allyl isothiocyanate as substrate 6.8 umol/min/mg allyl isothiocyanate Y Y ECO:0000311 UniProtKB request from ChEBI: allyl isothiocyanate; PUBCHEMcid:5971 AAP 2/6/2013 124 2000000124 Mike O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 6.3 umol/min/mg enzyme with benzyl isothiocyanate as substrate 6.3 umol/min/mg benzyl isothiocyanate CHEBI:17484 Y Y ECO:0000311 UniProtKB AAP 2/6/2013 124 2000000125 Mike/Rose O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 0.05 umol/min/mg enzyme with cumene hydroperoxide as substrate 0.05 umol/min/mg cumene hydroperoxide Y Y ECO:0000311 UniProtKB request from ChEBI: cumene hydroperoxide; PUBCHEMcid:6629 AAP 2/6/2013 124 2000000126 Mike O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 8.6 umol/min/mg enzyme with 1-bromo-2,4-dinitrobenzene as substrate 8.6 umol/min/mg dinitrobenzene CHEBI:51396 Y Y ECO:0000311 UniProtKB request from ChEBI AAP 2/6/2013 124 2000000127 Mike O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 10.7 umol/min/mg enzyme with 1-iodo-2,4-dinitrobenzene as substrate 10.7 umol/min/mg dinitrobenzene CHEBI:51396 Y Y ECO:0000311 UniProtKB request from ChEBI AAP 2/6/2013 124 2000000128 Mike O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/KM 8 mM for glutathione for the glutathione-conjugating activity 8 mM glutathione CHEBI:16856 Y Y ECO:0000006 PubMed:11672424 PubMed:12627223 PubMed:15113825 UniProtKB AAP 2/6/2013 124 2000000129 Mike O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.6 mM for glutathione for the prostaglandin D synthase activity in the presence of EDTA 0.6 mM glutathione CHEBI:16856 Y Y ECO:0000311 UniProtKB AAP 2/6/2013 124 2000000130 Mike O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.14 mM for glutathione for the prostaglandin D synthase activity in the presence of magnesium ions 0.14 mM glutathione CHEBI:16856 Y Y ECO:0000311 UniProtKB AAP 2/6/2013 124 2000000131 Mike P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.4 mM for HDL(2) 0.4 mM high-density lipoprotein CHEBI:39025 Y Y ECO:0000311 UniProtKB request from ChEBI AAP 11/28/2012 141 2000000132 Mike P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.10 mM for HDL(3) 0.1 mM high-density lipoprotein CHEBI:39025 Y Y ECO:0000311 UniProtKB request from ChEBI AAP 11/28/2012 141 2000000133 Mike P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 8.3 mmol/min/mg enzyme with LDL as substrate 8.3 mmol/min/mg high-density lipoprotein CHEBI:39025 Y Y ECO:0000311 UniProtKB AAP 11/28/2012 141 2000000134 Mike P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 0.58 mmol/min/mg enzyme with HDL(2) as substrate 0.58 mmol/min/mg high-density lipoprotein CHEBI:39025 Y Y ECO:0000311 UniProtKB request from ChEBI AAP 11/28/2012 141 2000000135 Mike P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 2.0 mmol/min/mg enzyme with HDL(3) as substrate 2 mmol/min/mg high-density lipoprotein CHEBI:39025 Y Y ECO:0000311 UniProtKB request from ChEBI AAP 11/28/2012 141 2000000136 Mike P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.97 mM for LDL 0.97 mM low-density lipoprotein CHEBI:39026 Y Y ECO:0000006 PubMed:10329423 UniProtKB AAP 11/28/2012 141 2000000137 Faith Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/KM 71.56 uM for arachidonoyl-CoA 71.56 uM arachidonoyl-CoA CHEBI:15514 Y Y ECO:0000311 UniProtKB AAP 1/9/2013 82 2000000144 Faith Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/KM 201.4 uM for linoleoyl-CoA 201.4 uM linoleoyl-CoA CHEBI:15530 Y Y ECO:0000311 UniProtKB AAP 1/9/2013 82 2000000145 Faith Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/KM 72.19 uM for 1-palmitoyl-lysophosphatidylcholine 72.19 uM lysophosphatidylcholine 16:0 CHEBI:64563 Y Y ECO:0000311 UniProtKB LPC16:0 covers a connection of palmitoyl at either 1 or 2 in the glycero moiety. AAP 1/9/2013 82 2000000146 Faith Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/KM 72.68 uM for oleoyl-CoA 72.68 uM oleoyl-CoA CHEBI:15534 Y Y ECO:0000311 UniProtKB AAP 1/9/2013 82 2000000147 Faith Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/KM 41.29 uM for palmitoyl-CoA 41.29 uM palmitoyl-CoA CHEBI:15525 Y Y ECO:0000006 PubMed:18195019 UniProtKB AAP 1/9/2013 82 2000000148 Faith Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/KM 36.65 uM for stearoyl-CoA 36.65 uM stearoyl-CoA CHEBI:15541 Y Y ECO:0000311 UniProtKB AAP 1/9/2013 82 2000000149 Rose P47712 5321 PLA2G4A Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 2.7 umol/min/mg enzyme for the phospholipase A2 reaction 2.7 umol/min/mg Y Y ECO:0000006 PubMed:8083230 UniProtKB AAP 11/28/2012 140 2000000150 Rose P47712 5321 PLA2G4A Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 4.6 umol/min/mg enzyme for the lysophosphatase reaction 4.6 umol/min/mg Y Y ECO:0000311 UniProtKB AAP 11/28/2012 140 2000000151 Mike P0C869 PLA2G4B Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 2.1 nmol/min/ug enzyme with 1-16:0-2-[14C]20:4-PC as substrate (isoform 5) 2.1 nmol/min/ug 1-O-palmitoyl-2-O-arachidonoyl-sn-glycero-3-phosphocholine CHEBI:60378 Y Y ECO:0000311 UniProtKB isoform 5 AAP 11/28/2012 45 2000000152 Mike P0C869 PLA2G4B Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 3.6 pmol/min/ug enzyme with cAMP as substrate (isoform 4) 3.6 pmol/min/ug 3',5'-cyclic AMP CHEBI:17489 Y Y ECO:0000311 UniProtKB AAP 11/28/2012 45 2000000153 Mike P0C869 PLA2G4B Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 0.6 nmol/min/ug enzyme with 1-16:0-2-[14C]20:4-PE as substrate (isoform 5) 0.6 nmol/min/ug dialkylglycerophosphoethanolamine CHEBI:37814 Y Y ECO:0000311 UniProtKB request from ChEBI: 1-16:0-2-[14C]20:4-PE AAP 11/28/2012 45 2000000154 Mike P0C869 PLA2G4B Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 0.8 nmol/min/ug enzyme with 1-16:0-2-[14C]20:4-PE as substrate (isoform 3) 0.8 nmol/min/ug dialkylglycerophosphoethanolamine CHEBI:37814 Y Y ECO:0000311 UniProtKB request from ChEBI: 1-16:0-2-[14C]20:4-PE AAP 11/28/2012 45 2000000155 Mike P0C869 PLA2G4B Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 0.3 nmol/min/ug enzyme with 1-16:0-2-[14C]18:2-PE as substrate (isoform 3) 0.3 nmol/min/ug dialkylglycerophosphoethanolamine CHEBI:37814 Y Y ECO:0000311 UniProtKB request from ChEBI: 1-16:0-2-[14C]18:2-PE AAP 11/28/2012 45 2000000156 Mike P0C869 PLA2G4B Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 140 nmol/min/ug enzyme with 1-[14C]16:0-2-lyso-PC as substrate (isoform 5) 140 nmol/min/ug lysophosphatidylcholine 16:0 CHEBI:64563 Y Y ECO:0000311 UniProtKB request from ChEBI: 1-[14C]16:0-2-lyso-PC AAP 11/28/2012 45 2000000157 Mike P0C869 PLA2G4B Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 1.6 nmol/min/ug enzyme with 1-[14C]16:0-2-lyso-PC as substrate (isoform 3) 1.6 nmol/min/ug lysophosphatidylcholine 16:0 CHEBI:64563 Y Y ECO:0000311 UniProtKB request from ChEBI: 1-[14C]16:0-2-lyso-PC AAP 11/28/2012 45 2000000158 Mike P0C869 PLA2G4B Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 7.9 pmol/min/mg enzyme (isoform 5) 7.9 pmol/min/mg Y Y ECO:0000006 PubMed:10085124 UniProtKB substrate unclear AAP 11/28/2012 45 2000000159 Faith Q9UP65 8605 PLA2G4C Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 218 pmol/min/mg enzyme 218 pmol/min/mg 1-O-palmitoyl-2-O-arachidonoyl-sn-glycero-3-phosphocholine CHEBI:60378 Y Y ECO:0000006 PubMed:10085124 UniProtKB Curated by Faith. Article states that enzyme assay carried out as previously in two cited articles. One article used 1-palmitoyl-2-[14C]arachidonoyl-sn-glycero-3-phosphocholine and other [14C]arachidonoyl phosphatidylcholine. I could note phosphatidylcholine, but there are more specific options (diacylPC or specificacylPC AAP 11/28/2012 93 2000000160 Faith Q15185 10728 PTGES3 Homo sapiens 9606 Comment/biophysicochemical properties/KM 14 uM for PGH2 14 uM prostaglandin H2 CHEBI:15554 Y Y ECO:0000006 PubMed:10922363 UniProtKB AAP 2/6/2013 125 2000000161 Faith Q15185 10728 PTGES3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 190 nmol/min/mg enzyme toward PGH2 190 nmol/min/mg prostaglandin H2 CHEBI:15554 Y Y ECO:0000006 PubMed:10922363 UniProtKB AAP 2/6/2013 125 2000000162 Rose P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 16.2 uM for arachidonate (in absence of sodium nitroprusside NO donor) 16.2 uM arachidonate CHEBI:32395 Y Y ECO:0000006 PubMed:16373578 UniProtKB AAP 2/6/2013 143 2000000163 Rose P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 17.0 uM for arachidonate (in presence of sodium nitroprusside NO donor) 17 uM arachidonate CHEBI:32395 Y Y ECO:0000311 UniProtKB AAP 2/6/2013 143 2000000164 Rose P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 81.3 nmol/min/mg enzyme (in absence of sodium nitroprusside NO donor) 81.3 nmol/min/mg Y Y ECO:0000311 UniProtKB AAP 2/6/2013 143 2000000165 Rose P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 132 nmol/min/mg enzyme (in absence of sodium nitroprusside NO donor) 132 nmol/min/mg Y Y ECO:0000311 UniProtKB AAP 2/6/2013 143 2000000166 Faith P53816 11145 PLA2G16 Homo sapiens 9606 Comment/biophysicochemical properties/KM 300 uM for dipalmitoyl-PC 300 uM 1,2-di-O-palmitoyl-sn-glycero-3-phosphocholine CHEBI:40265 Y Y ECO:0000006 PubMed:19615464 UniProtKB AAP 5/29/2013 109 2000000167 Faith P53816 11145 PLA2G16 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 2.57 umol/min/mg enzyme with dipalmitoyl-PC as substrate 2.57 umol/min/mg 1,2-di-O-palmitoyl-sn-glycero-3-phosphocholine CHEBI:40265 Y Y PubMed:19615464 UniProtKB AAP 5/29/2013 109 2000000168 Faith P53816 11145 PLA2G16 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 267 nmol/min/mg enzyme with dipalmitoyl-PE as substrate 267 nmol/min/mg 1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine CHEBI:73127 Y Y UniProtKB AAP 5/29/2013 109 2000000169 Faith P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 4.5 uM for arachidonate 4.5 uM arachidonate CHEBI:32395 Y Y PubMed:7947975 also contains IC50 values for various NSAIDs AAP 2000000172 Faith P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 5.1 uM for arachidonate 5.1 uM arachidonate CHEBI:32395 Y Y PubMed:7947975 also contains IC50 values for various NSAIDs AAP 2000000173 Faith P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 10.2 uM for [3H]arachidonic acid 10.2 uM arachidonic acid CHEBI:15843 Y Y PubMed:9139685 [3H]arachidonic acid AAP 2000000174 Faith P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 10.0 uM for [3H]arachidonic acid 10 uM arachidonic acid CHEBI:15843 Y Y PubMed:9139685 [3H]arachidonic acid AAP 2000000175 Faith P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.9 uM for arachidonic acid 0.9 uM arachidonic acid CHEBI:15843 Y Y PubMed:7979387 AAP 2000000176 Faith P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 1.1 uM for arachidonic acid 1.1 uM arachidonic acid CHEBI:15843 Y Y PubMed:12433707 AAP 2000000177 Faith P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 1.7 uM for arachidonate 1.7 uM arachidonate CHEBI:32395 Y Y PubMed:16770009 AAP 2000000178 Faith P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 9.2 uM for arachidonic acid 9.2 uM arachidonic acid CHEBI:15843 Y Y PubMed:19218248 AAP 2000000179 Faith P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 9 uM for arachidonic acid 9 uM arachidonic acid CHEBI:15843 Y Y PubMed:11602656 AAP 2000000180 Faith P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 14.7 uM for arachidonic acid 14.7 uM arachidonic acid CHEBI:15843 Y Y PubMed:9172778 AAP 2000000181 Faith Q16647 5740 PTGIS Homo sapiens 9606 Comment/biophysicochemical properties/KM 30 uM for PGH2 30 uM prostaglandin H2 CHEBI:15554 Y Y PubMed:15115769 AAP 2000000182 Faith Q16647 5740 PTGIS Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 15 umol/min/mg enzyme with PGH2 as substrate 15 umol/min/mg prostaglandin H2 CHEBI:15554 Y Y PubMed:15115769 AAP 2000000183Jodi Jodi O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.2 {glutathione} <31> 0.2 mM glutathione CHEBI:16856 5.3.99.2 Y Y ECO:0000033 Pubmed:11672424 BRENDA <31> Jowsey, I.R.; Thomson, A.M.; Flanagan, J.U.; Murdock, P.R.; Moore,G.B.T.; Meyer, D.J.; Murphy, G.J.; Smith, S.A.; Hayes, J.D.: Mammalianclass Sigma glutathione S-transferases: catalytic properties andtissue-specific expression of human and rat GSH-dependent prostaglandinD2 synthases. Biochem. J. (2001) 359, 507-516. {Pubmed:11672424} AAP 12/7/2011 1111 2000000185 Jodi O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 3.2 {1-chloro-2,4-dinitrobenzene} <31> 3.2 mM 1-chloro-2,4-dinitrobenzene CHEBI:34718 5.3.99.2 Y Y ECO:0000033 Pubmed:11672424 BRENDA <31> Jowsey, I.R.; Thomson, A.M.; Flanagan, J.U.; Murdock, P.R.; Moore,G.B.T.; Meyer, D.J.; Murphy, G.J.; Smith, S.A.; Hayes, J.D.: Mammalianclass Sigma glutathione S-transferases: catalytic properties andtissue-specific expression of human and rat GSH-dependent prostaglandinD2 synthases. Biochem. J. (2001) 359, 507-516. {Pubmed:11672424} AAP 12/7/2011 1111 2000000186 Chandra O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.1 {(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate} (#2# in the presence of 0.3 mM dodecylmaltoside <14>) <14> 0.01 mM prostaglandin H2 CHEBI:15554 5.3.99.3 #2# in the presence of 0.3 mM dodecylmaltoside <14> Y Y ECO:0000006 Pubmed:12460774 BRENDA <14> Ouellet, M.; Falgueyret, J.P.; Ear, P.H.; Pen, A.; Mancini, J.A.;Riendeau, D.; David Percival, M.: Purification and characterization ofrecombinant microsomal prostaglandin E synthase-1. Protein Expr. Purif.(2002) 26, 489-495. {Pubmed:12460774}; PENTACON Notes: corrected value AAP 12/7/2011 1111 2000000187 Chandra O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.1 {(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate} (#2# in the presence of 0.3 mM dodecylmaltoside <14>) <14> 0.01 mM prostaglandin H2 CHEBI:15554 5.3.99.3 #2# in the presence of 0.3 mM dodecylmaltoside <14> Y Y ECO:0000006 Pubmed:12460774 BRENDA <14> Ouellet, M.; Falgueyret, J.P.; Ear, P.H.; Pen, A.; Mancini, J.A.;Riendeau, D.; David Percival, M.: Purification and characterization ofrecombinant microsomal prostaglandin E synthase-1. Protein Expr. Purif.(2002) 26, 489-495. {Pubmed:12460774}; PENTACON Notes: corrected value AAP 12/7/2011 1111 2000000188 Chandra O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.014 {(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate} <14> 0.014 mM prostaglandin H2 CHEBI:15554 5.3.99.3 Y Y ECO:0000006 Pubmed:12460774 BRENDA <14> Ouellet, M.; Falgueyret, J.P.; Ear, P.H.; Pen, A.; Mancini, J.A.;Riendeau, D.; David Percival, M.: Purification and characterization ofrecombinant microsomal prostaglandin E synthase-1. Protein Expr. Purif.(2002) 26, 489-495. {Pubmed:12460774} AAP 12/7/2011 1111 2000000189 Chandra O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #12# 0.75 {glutathione} <14> 0.75 mM glutathione CHEBI:16856 5.3.99.3 Y Y ECO:0000006 Pubmed:12460774 BRENDA <14> Ouellet, M.; Falgueyret, J.P.; Ear, P.H.; Pen, A.; Mancini, J.A.;Riendeau, D.; David Percival, M.: Purification and characterization ofrecombinant microsomal prostaglandin E synthase-1. Protein Expr. Purif.(2002) 26, 489-495. {Pubmed:12460774} AAP 12/7/2011 1111 2000000190 Chandra O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.6 {glutathione} (#2# in the presence of 0.3 mM dodecylmaltoside<14>) <14> 0.6 mM glutathione CHEBI:16856 5.3.99.3 #2# in the presence of 0.3 mM dodecylmaltoside<14> Y Y ECO:0000006 Pubmed:12460774 BRENDA <14> Ouellet, M.; Falgueyret, J.P.; Ear, P.H.; Pen, A.; Mancini, J.A.;Riendeau, D.; David Percival, M.: Purification and characterization ofrecombinant microsomal prostaglandin E synthase-1. Protein Expr. Purif.(2002) 26, 489-495. {Pubmed:12460774} AAP 12/7/2011 1111 2000000191 Chandra O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 5.5 umol/min/mg no detergent and 2.5mM GSH. 5.5 umol/min/mg glutathione CHEBI:16856 prostaglandin H2 CHEBI:15554 Y Y ECO:0000006 Pubmed:12460774 PENTACON Added by PENTACON; PENTACON Notes: no detergent AAP 2000000192 Chandra O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 5.5 umol/min/mg no detergent and 20μM PGH2 5.5 umol/min/mg glutathione CHEBI:16856 prostaglandin H2 CHEBI:15554 Y Y ECO:0000006 Pubmed:12460774 PENTACON Added by PENTACON; PENTACON Notes: no detergent AAP 2000000193 Chandra O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 38.6 umol/min/mg in the presence of 0.3 mM dodecylmaltoside and 20μM PGH2 38.6 umol/min/mg glutathione CHEBI:16856 prostaglandin H2 CHEBI:15554 Y Y ECO:0000006 Pubmed:12460774 PENTACON Added by PENTACON; PENTACON Notes: in the presence of 0.3 mM dodecylmaltoside AAP 2000000194 Chandra O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 46 umol/min/mg in the presence of 0.3 mM dodecylmaltoside and 2.5mM GSH. 46 umol/min/mg glutathione CHEBI:16856 prostaglandin H2 CHEBI:15554 Y Y ECO:0000006 Pubmed:12460774 PENTACON Added by PENTACON; PENTACON Notes: in the presence of 0.3 mM dodecylmaltoside AAP 2000000195 Christie O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.71 {glutathione} <12> 0.71 mM glutathione CHEBI:16856 5.3.99.3 Y Y ECO:0000006 Pubmed:12672824 BRENDA <12> Thoren, S.; Weinander, R.; Saha, S.; Jegerschoeld, C.; Pettersson,P.L.; Samuelsson, B.; Hebert, H.; Hamberg, M.; Morgenstern, R.;Jakobsson, P.J.: Human microsomal prostaglandin E synthase-1:purification, functional characterization, and projection structuredetermination. J. Biol. Chem. (2003) 278, 22199-22209. {Pubmed:12672824} AAP 12/7/2011 1111 2000000196 Christie O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.16 {prostaglandin G2} <12,25> 0.16 mM prostaglandin G2 CHEBI:27647 5.3.99.3 Y Y ECO:0000006 Pubmed:12672824 BRENDA <12> Thoren, S.; Weinander, R.; Saha, S.; Jegerschoeld, C.; Pettersson,P.L.; Samuelsson, B.; Hebert, H.; Hamberg, M.; Morgenstern, R.;Jakobsson, P.J.: Human microsomal prostaglandin E synthase-1:purification, functional characterization, and projection structuredetermination. J. Biol. Chem. (2003) 278, 22199-22209. {Pubmed:12672824} AAP 12/7/2011 1111 2000000197 Christie/Rose O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.16 {(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate} <12> 0.16 mM prostaglandin H2 CHEBI:15554 5.3.99.3 Y Y ECO:0000006 Pubmed:12672824 BRENDA <12> Thoren, S.; Weinander, R.; Saha, S.; Jegerschoeld, C.; Pettersson,P.L.; Samuelsson, B.; Hebert, H.; Hamberg, M.; Morgenstern, R.;Jakobsson, P.J.: Human microsomal prostaglandin E synthase-1:purification, functional characterization, and projection structuredetermination. J. Biol. Chem. (2003) 278, 22199-22209. {Pubmed:12672824} AAP 12/7/2011 1111 2000000198 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 1.3 {H2O2} (#3# pH 8.0, 23°C, wild-type enzyme <45>) <45> 1.3 mM H2O2 CHEBI:16240 1.14.99.1 #3# pH 8.0, 23°C, wild-type enzyme <45> Y Y ECO:0000006 Pubmed:14625295 BRENDA <45> Bambai, B.; Rogge, C.E.; Stec, B.; Kulmacz, R.J.: Role of Asn-382and Thr-383 in activation and inactivation of human prostaglandin Hsynthase cyclooxygenase catalysis. J. Biol. Chem. (2004) 279,4084-4092. {Pubmed:14625295} (c) AAP 12/7/2011 1111 2000000199 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 5.5 {H2O2} (#3# pH 8.0, 23°C, mutant enzyme N382L <45>) <45> 5.5 mM H2O2 CHEBI:16240 1.14.99.1 #3# pH 8.0, 23°C, mutant enzyme N382L <45> Y Y ECO:0000006 Pubmed:14625295 BRENDA <45> Bambai, B.; Rogge, C.E.; Stec, B.; Kulmacz, R.J.: Role of Asn-382and Thr-383 in activation and inactivation of human prostaglandin Hsynthase cyclooxygenase catalysis. J. Biol. Chem. (2004) 279,4084-4092. {Pubmed:14625295} (c) AAP 12/7/2011 1111 2000000200 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.08 {Guaiacol} (#3# pH 8.0, 23°C, wild-type enzyme <45>) <45> 0.08 mM Guaiacol CHEBI:28591 1.14.99.1 #3# pH 8.0, 23°C, wild-type enzyme <45> Y Y ECO:0000006 Pubmed:14625295 BRENDA <45> Bambai, B.; Rogge, C.E.; Stec, B.; Kulmacz, R.J.: Role of Asn-382and Thr-383 in activation and inactivation of human prostaglandin Hsynthase cyclooxygenase catalysis. J. Biol. Chem. (2004) 279,4084-4092. {Pubmed:14625295} (c) AAP 12/7/2011 1111 2000000201 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.29 {Guaiacol} (#3# pH 8.0, 23°C, mutant enzyme N382L <45>) <45> 0.29 mM Guaiacol CHEBI:28591 1.14.99.1 #3# pH 8.0, 23°C, mutant enzyme N382L <45> Y Y ECO:0000006 Pubmed:14625295 BRENDA <45> Bambai, B.; Rogge, C.E.; Stec, B.; Kulmacz, R.J.: Role of Asn-382and Thr-383 in activation and inactivation of human prostaglandin Hsynthase cyclooxygenase catalysis. J. Biol. Chem. (2004) 279,4084-4092. {Pubmed:14625295} (c) AAP 12/7/2011 1111 2000000202 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0021 {arachidonate} (#3# native enzyme <43>; #3# pH 7.2, 30°C,mutant enzyme N382L <45>; #3# pH 7.2, 30°C, PGHS-2 wild-type enzyme<45>) <43,45> 0.0021 mM arachidonate CHEBI:32395 1.14.99.1 #3# native enzyme <43>; #3# pH 7.2, 30°C,mutant enzyme N382L <45>; #3# pH 7.2, 30°C, PGHS-2 wild-type enzyme<45> Y Y ECO:0000006 Pubmed:14625295 BRENDA <45> Bambai, B.; Rogge, C.E.; Stec, B.; Kulmacz, R.J.: Role of Asn-382and Thr-383 in activation and inactivation of human prostaglandin Hsynthase cyclooxygenase catalysis. J. Biol. Chem. (2004) 279,4084-4092. {Pubmed:14625295} (c) AAP 12/7/2011 1111 2000000203 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0022 {arachidonate} (#3# pH 7.2, 30°C, mutant enzyme N383D<45>) <45> 0.0022 mM arachidonate CHEBI:32395 1.14.99.1 #3# pH 7.2, 30°C, mutant enzyme N383D<45> Y Y ECO:0000006 Pubmed:14625295 BRENDA <45> Bambai, B.; Rogge, C.E.; Stec, B.; Kulmacz, R.J.: Role of Asn-382and Thr-383 in activation and inactivation of human prostaglandin Hsynthase cyclooxygenase catalysis. J. Biol. Chem. (2004) 279,4084-4092. {Pubmed:14625295} (c); PENTACON Notes: Mutant: N383D mutant is really T383D AAP 12/7/2011 1111 2000000204 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0029 {arachidonate} (#3# pH 7.2, 30°C, mutant enzyme N382D<45>) <45> 0.0029 mM arachidonate CHEBI:32395 1.14.99.1 #3# pH 7.2, 30°C, mutant enzyme N382D<45> Y Y ECO:0000006 Pubmed:14625295 BRENDA <45> Bambai, B.; Rogge, C.E.; Stec, B.; Kulmacz, R.J.: Role of Asn-382and Thr-383 in activation and inactivation of human prostaglandin Hsynthase cyclooxygenase catalysis. J. Biol. Chem. (2004) 279,4084-4092. {Pubmed:14625295} (c) AAP 12/7/2011 1111 2000000205 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0041 {arachidonate} (#3# pH 7.2, 30°C, mutant enzyme N382A<45>) <45> 0.0041 mM arachidonate CHEBI:32395 1.14.99.1 #3# pH 7.2, 30°C, mutant enzyme N382A<45> Y Y ECO:0000006 Pubmed:14625295 BRENDA <45> Bambai, B.; Rogge, C.E.; Stec, B.; Kulmacz, R.J.: Role of Asn-382and Thr-383 in activation and inactivation of human prostaglandin Hsynthase cyclooxygenase catalysis. J. Biol. Chem. (2004) 279,4084-4092. {Pubmed:14625295} (c) AAP 12/7/2011 1111 2000000206 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0083 {N,N,N',N'-tetramethyl-p-phenylenediamine} (#3# pH 7.2,30°C, mutant enzyme N383H <45>) <45> 0.0083 mM N,N,N',N'-tetramethyl-p-phenylenediamine 1.14.99.1 #3# pH 7.2,30°C, mutant enzyme N383H <45> Y Y ECO:0000006 Pubmed:14625295 BRENDA <45> Bambai, B.; Rogge, C.E.; Stec, B.; Kulmacz, R.J.: Role of Asn-382and Thr-383 in activation and inactivation of human prostaglandin Hsynthase cyclooxygenase catalysis. J. Biol. Chem. (2004) 279,4084-4092. {Pubmed:14625295} (c); PENTACON Notes: Request ChEBI ID: N,N,N',N'-tetramethyl-p-phenylenediamine; Mutant: N383H mutant is really T383H AAP 12/7/2011 1111 2000000207 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.01 {N,N,N',N'-tetramethyl-p-phenylenediamine} (#3# pH 7.2,30°C, mutant enzyme N383D <45>) <45> 0.01 mM N,N,N',N'-tetramethyl-p-phenylenediamine 1.14.99.1 #3# pH 7.2,30°C, mutant enzyme N383D <45> Y Y ECO:0000006 Pubmed:14625295 BRENDA <45> Bambai, B.; Rogge, C.E.; Stec, B.; Kulmacz, R.J.: Role of Asn-382and Thr-383 in activation and inactivation of human prostaglandin Hsynthase cyclooxygenase catalysis. J. Biol. Chem. (2004) 279,4084-4092. {Pubmed:14625295} (c); PENTACON Notes: Request ChEBI ID: N,N,N',N'-tetramethyl-p-phenylenediamine; Mutant: N383D mutant is really T383D AAP 12/7/2011 1111 2000000208 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0156 {N,N,N',N'-tetramethyl-p-phenylenediamine} (#3# pH 7.2,30°C, mutant enzyme N382D <45>) <45> 0.0156 mM N,N,N',N'-tetramethyl-p-phenylenediamine 1.14.99.1 #3# pH 7.2,30°C, mutant enzyme N382D <45> Y Y ECO:0000006 Pubmed:14625295 BRENDA <45> Bambai, B.; Rogge, C.E.; Stec, B.; Kulmacz, R.J.: Role of Asn-382and Thr-383 in activation and inactivation of human prostaglandin Hsynthase cyclooxygenase catalysis. J. Biol. Chem. (2004) 279,4084-4092. {Pubmed:14625295} (c); PENTACON Notes: Request ChEBI ID: N,N,N',N'-tetramethyl-p-phenylenediamine AAP 12/7/2011 1111 2000000209 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0163 {N,N,N',N'-tetramethyl-p-phenylenediamine} (#3# pH 7.2,30°C, PGHS-2 wild-type enzyme <45>) <45> 0.0163 mM N,N,N',N'-tetramethyl-p-phenylenediamine 1.14.99.1 #3# pH 7.2,30°C, PGHS-2 wild-type enzyme <45> Y Y ECO:0000006 Pubmed:14625295 BRENDA <45> Bambai, B.; Rogge, C.E.; Stec, B.; Kulmacz, R.J.: Role of Asn-382and Thr-383 in activation and inactivation of human prostaglandin Hsynthase cyclooxygenase catalysis. J. Biol. Chem. (2004) 279,4084-4092. {Pubmed:14625295} (c); PENTACON Notes: Request ChEBI ID: N,N,N',N'-tetramethyl-p-phenylenediamine AAP 12/7/2011 1111 2000000210 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0854 {N,N,N',N'-tetramethyl-p-phenylenediamine} (#3# pH 7.2,30°C, mutant enzyme N382L <45>) <45> 0.0854 mM N,N,N',N'-tetramethyl-p-phenylenediamine 1.14.99.1 #3# pH 7.2,30°C, mutant enzyme N382L <45> Y Y ECO:0000006 Pubmed:14625295 BRENDA <45> Bambai, B.; Rogge, C.E.; Stec, B.; Kulmacz, R.J.: Role of Asn-382and Thr-383 in activation and inactivation of human prostaglandin Hsynthase cyclooxygenase catalysis. J. Biol. Chem. (2004) 279,4084-4092. {Pubmed:14625295} (c); PENTACON Notes: Request ChEBI ID: N,N,N',N'-tetramethyl-p-phenylenediamine AAP 12/7/2011 1111 2000000211 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0021 {arachidonate} (#3# native enzyme <43>) <43> 0.0021 mM arachidonate CHEBI:32395 1.14.99.1 #3# native enzyme <43> Y Y ECO:0000006 Pubmed:14769032 BRENDA <43> Rogge, C.E.; Liu, W.; Wu, G.; Wang, L.H.; Kulmacz, R.J.; Tsai,A.L.: Identification of Tyr504 as an alternative tyrosyl radical sitein human prostaglandin H synthase-2. Biochemistry (2004) 43, 1560-1568.{Pubmed:14769032} (c) AAP 12/7/2011 1111 2000000212 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0032 {arachidonate} (#3# mutant enzyme Y148F <43>) <43> 0.0032 mM arachidonate CHEBI:32395 1.14.99.1 #3# mutant enzyme Y148F <43> Y Y ECO:0000006 Pubmed:14769032 BRENDA <43> Rogge, C.E.; Liu, W.; Wu, G.; Wang, L.H.; Kulmacz, R.J.; Tsai,A.L.: Identification of Tyr504 as an alternative tyrosyl radical sitein human prostaglandin H synthase-2. Biochemistry (2004) 43, 1560-1568.{Pubmed:14769032} (c); PENTACON Notes: Mutant: Y148F AAP 12/7/2011 1111 2000000213 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0036 {arachidonate} (#3# mutant enzyme Y404F <43>) <43> 0.0036 mM arachidonate CHEBI:32395 1.14.99.1 #3# mutant enzyme Y404F <43> Y Y ECO:0000006 Pubmed:14769032 BRENDA <43> Rogge, C.E.; Liu, W.; Wu, G.; Wang, L.H.; Kulmacz, R.J.; Tsai,A.L.: Identification of Tyr504 as an alternative tyrosyl radical sitein human prostaglandin H synthase-2. Biochemistry (2004) 43, 1560-1568.{Pubmed:14769032} (c); PENTACON Notes: Mutant: Y404F AAP 12/7/2011 1111 2000000214 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0038 {arachidonate} (#3# mutant enzyme Y348F <43>) <43> 0.0038 mM arachidonate CHEBI:32395 1.14.99.1 #3# mutant enzyme Y348F <43> Y Y ECO:0000006 Pubmed:14769032 BRENDA <43> Rogge, C.E.; Liu, W.; Wu, G.; Wang, L.H.; Kulmacz, R.J.; Tsai,A.L.: Identification of Tyr504 as an alternative tyrosyl radical sitein human prostaglandin H synthase-2. Biochemistry (2004) 43, 1560-1568.{Pubmed:14769032} (c); PENTACON Notes: Mutant: Y348F AAP 12/7/2011 1111 2000000215 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0042 {arachidonate} (#3# mutant enzyme Y504F <43>) <43> 0.0042 mM arachidonate CHEBI:32395 1.14.99.1 #3# mutant enzyme Y504F <43> Y Y ECO:0000006 Pubmed:14769032 BRENDA <43> Rogge, C.E.; Liu, W.; Wu, G.; Wang, L.H.; Kulmacz, R.J.; Tsai,A.L.: Identification of Tyr504 as an alternative tyrosyl radical sitein human prostaglandin H synthase-2. Biochemistry (2004) 43, 1560-1568.{Pubmed:14769032} (c); PENTACON Notes: Mutant: Y504F AAP 12/7/2011 1111 2000000216 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0043 {arachidonate} (#3# mutant enzyme Y148F/Y348F/Y404F/Y504F<43>) <43> 0.0043 mM arachidonate CHEBI:32395 1.14.99.1 #3# mutant enzyme Y148F/Y348F/Y404F/Y504F<43> Y Y ECO:0000006 Pubmed:14769032 BRENDA <43> Rogge, C.E.; Liu, W.; Wu, G.; Wang, L.H.; Kulmacz, R.J.; Tsai,A.L.: Identification of Tyr504 as an alternative tyrosyl radical sitein human prostaglandin H synthase-2. Biochemistry (2004) 43, 1560-1568.{Pubmed:14769032} (c); PENTACON Notes: Mutant: Y148F/Y348F/Y404F/Y504F AAP 12/7/2011 1111 2000000217 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.02 {trans-5-phenyl-4-pentenyl-1-hydroperoxide} (#3# mutantenzyme Y148F <43>) <43> 0.02 mM trans-5-phenyl-4-pentenyl-1-hydroperoxide 1.14.99.1 #3# mutantenzyme Y148F <43> Y Y ECO:0000006 Pubmed:14769032 BRENDA <43> Rogge, C.E.; Liu, W.; Wu, G.; Wang, L.H.; Kulmacz, R.J.; Tsai,A.L.: Identification of Tyr504 as an alternative tyrosyl radical sitein human prostaglandin H synthase-2. Biochemistry (2004) 43, 1560-1568.{Pubmed:14769032} (c); PENTACON Notes: Mutant: Y148F; Request ChEBI ID: trans-5-phenyl-4-pentenyl-1-hydroperoxide, PubChem ID: CID 6438577 AAP 12/7/2011 1111 2000000218 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.061 {trans-5-phenyl-4-pentenyl-1-hydroperoxide} (#3# mutantenzyme Y404F <43>) <43> 0.061 mM trans-5-phenyl-4-pentenyl-1-hydroperoxide 1.14.99.1 #3# mutantenzyme Y404F <43> Y Y ECO:0000006 Pubmed:14769032 BRENDA <43> Rogge, C.E.; Liu, W.; Wu, G.; Wang, L.H.; Kulmacz, R.J.; Tsai,A.L.: Identification of Tyr504 as an alternative tyrosyl radical sitein human prostaglandin H synthase-2. Biochemistry (2004) 43, 1560-1568.{Pubmed:14769032} (c); PENTACON Notes: Request ChEBI ID: trans-5-phenyl-4-pentenyl-1-hydroperoxide, PubChem ID: CID 6438577 AAP 12/7/2011 1111 2000000219 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.072 {trans-5-phenyl-4-pentenyl-1-hydroperoxide} (#3# mutantenzyme Y348F <43>) <43> 0.072 mM trans-5-phenyl-4-pentenyl-1-hydroperoxide 1.14.99.1 #3# mutantenzyme Y348F <43> Y Y ECO:0000006 Pubmed:14769032 BRENDA <43> Rogge, C.E.; Liu, W.; Wu, G.; Wang, L.H.; Kulmacz, R.J.; Tsai,A.L.: Identification of Tyr504 as an alternative tyrosyl radical sitein human prostaglandin H synthase-2. Biochemistry (2004) 43, 1560-1568.{Pubmed:14769032} (c); PENTACON Notes: Mutant:Y348F; Request ChEBI ID: trans-5-phenyl-4-pentenyl-1-hydroperoxide, PubChem ID: CID 6438577 AAP 12/7/2011 1111 2000000220 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.103 {trans-5-phenyl-4-pentenyl-1-hydroperoxide} (#3# mutantenzyme Y148F/Y348F/Y385F/Y404F/Y504F <43>) <43> 0.103 mM trans-5-phenyl-4-pentenyl-1-hydroperoxide 1.14.99.1 #3# mutantenzyme Y148F/Y348F/Y385F/Y404F/Y504F <43> Y Y ECO:0000006 Pubmed:14769032 BRENDA <43> Rogge, C.E.; Liu, W.; Wu, G.; Wang, L.H.; Kulmacz, R.J.; Tsai,A.L.: Identification of Tyr504 as an alternative tyrosyl radical sitein human prostaglandin H synthase-2. Biochemistry (2004) 43, 1560-1568.{Pubmed:14769032} (c); PENTACON Notes: Mutant:Y148F/Y348F/Y385F/Y404F/Y504F; Request ChEBI ID: trans-5-phenyl-4-pentenyl-1-hydroperoxide, PubChem ID: CID 6438577 AAP 12/7/2011 1111 2000000221 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.138 {trans-5-phenyl-4-pentenyl-1-hydroperoxide} (#3# nativeenzyme <43>) <43> 0.138 mM trans-5-phenyl-4-pentenyl-1-hydroperoxide 1.14.99.1 #3# nativeenzyme <43> Y Y ECO:0000006 Pubmed:14769032 BRENDA <43> Rogge, C.E.; Liu, W.; Wu, G.; Wang, L.H.; Kulmacz, R.J.; Tsai,A.L.: Identification of Tyr504 as an alternative tyrosyl radical sitein human prostaglandin H synthase-2. Biochemistry (2004) 43, 1560-1568.{Pubmed:14769032} (c); PENTACON Notes: Request ChEBI ID: trans-5-phenyl-4-pentenyl-1-hydroperoxide, PubChem ID: CID 6438577 AAP 12/7/2011 1111 2000000222 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.339 {trans-5-phenyl-4-pentenyl-1-hydroperoxide} (#3# mutantenzyme Y385F <43>) <43> 0.339 mM trans-5-phenyl-4-pentenyl-1-hydroperoxide 1.14.99.1 #3# mutantenzyme Y385F <43> Y Y ECO:0000006 Pubmed:14769032 BRENDA <43> Rogge, C.E.; Liu, W.; Wu, G.; Wang, L.H.; Kulmacz, R.J.; Tsai,A.L.: Identification of Tyr504 as an alternative tyrosyl radical sitein human prostaglandin H synthase-2. Biochemistry (2004) 43, 1560-1568.{Pubmed:14769032} (c); PENTACON Notes: Mutant: Y385F; Request ChEBI ID: trans-5-phenyl-4-pentenyl-1-hydroperoxide, PubChem ID: CID 6438577 AAP 12/7/2011 1111 2000000223 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.37 {trans-5-phenyl-4-pentenyl-1-hydroperoxide} (#3# mutantenzyme Y148F/Y348F/Y404F/Y504F <43>) <43> 0.37 mM trans-5-phenyl-4-pentenyl-1-hydroperoxide 1.14.99.1 #3# mutantenzyme Y148F/Y348F/Y404F/Y504F <43> Y Y ECO:0000006 Pubmed:14769032 BRENDA <43> Rogge, C.E.; Liu, W.; Wu, G.; Wang, L.H.; Kulmacz, R.J.; Tsai,A.L.: Identification of Tyr504 as an alternative tyrosyl radical sitein human prostaglandin H synthase-2. Biochemistry (2004) 43, 1560-1568.{Pubmed:14769032} (c); PENTACON Notes: Mutant: Y148F/Y348F/Y404F/Y504F; Request ChEBI ID: trans-5-phenyl-4-pentenyl-1-hydroperoxide, PubChem ID: CID 6438577 AAP 12/7/2011 1111 2000000224 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.437 {trans-5-phenyl-4-pentenyl-1-hydroperoxide} (#3# mutantenzyme Y504F <43>) <43> 0.437 mM trans-5-phenyl-4-pentenyl-1-hydroperoxide 1.14.99.1 #3# mutantenzyme Y504F <43> Y Y ECO:0000006 Pubmed:14769032 BRENDA <43> Rogge, C.E.; Liu, W.; Wu, G.; Wang, L.H.; Kulmacz, R.J.; Tsai,A.L.: Identification of Tyr504 as an alternative tyrosyl radical sitein human prostaglandin H synthase-2. Biochemistry (2004) 43, 1560-1568.{Pubmed:14769032} (c); PENTACON Notes: Mutant: Y504F; Request ChEBI ID: trans-5-phenyl-4-pentenyl-1-hydroperoxide, PubChem ID: CID 6438577 AAP 12/7/2011 1111 2000000225 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.24 {prostaglandin E2} (#6# form CR2 <16>) <16> 0.24 mM prostaglandin E2 CHEBI:15551 1.1.1.184 #6# form CR2 <16> Y Y ECO:0000006 Pubmed:1540623 BRENDA <16> Inazu, N.; Ruepp, B.; Wirth, H.; Wermuth, B.: Carbonyl reductasefrom human testis: purification and comparison with carbonyl reductasefrom human brain and rat testis. Biochim. Biophys. Acta (1992) 1116,50-56. {Pubmed:1540623}; PENTACON Notes: Tissue: Testis AAP 12/7/2011 1111 2000000226 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.15 {5alpha-androstane-3,17-dione} (#6# form CR2 <16>) <16> 0.15 mM 5alpha-androstane-3,17-dione CHEBI:15994 1.1.1.184 #6# form CR2 <16> Y Y ECO:0000006 Pubmed:1540623 BRENDA <16> Inazu, N.; Ruepp, B.; Wirth, H.; Wermuth, B.: Carbonyl reductasefrom human testis: purification and comparison with carbonyl reductasefrom human brain and rat testis. Biochim. Biophys. Acta (1992) 1116,50-56. {Pubmed:1540623}; PENTACON Notes: Tissue: Testis AAP 12/7/2011 1111 2000000227 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.14-0.21 {Prostaglandin B2} (#6# Km depending on enzyme form<16>) <16> mM Prostaglandin B2 CHEBI:28099 1.1.1.184 #6# Km depending on enzyme form<16> Y Y ECO:0000006 Pubmed:1540623 BRENDA <16> Inazu, N.; Ruepp, B.; Wirth, H.; Wermuth, B.: Carbonyl reductasefrom human testis: purification and comparison with carbonyl reductasefrom human brain and rat testis. Biochim. Biophys. Acta (1992) 1116,50-56. {Pubmed:1540623}; PENTACON Notes: Tissue: Testis AAP 12/7/2011 1111 2000000228 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1.3-2.5 {4-Nitroacetophenone} (#6# Km depending on enzyme form<16>) <16> mM 4-Nitroacetophenone CHEBI:28735 1.1.1.184 #6# Km depending on enzyme form<16> Y Y ECO:0000006 Pubmed:1540623 BRENDA <16> Inazu, N.; Ruepp, B.; Wirth, H.; Wermuth, B.: Carbonyl reductasefrom human testis: purification and comparison with carbonyl reductasefrom human brain and rat testis. Biochim. Biophys. Acta (1992) 1116,50-56. {Pubmed:1540623}; PENTACON Notes: Tissue: Testis AAP 12/7/2011 1111 2000000229 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.05-0.07 {menadione} (#6# Km depending on enzyme form <16>) <16> mM menadione CHEBI:28869 1.1.1.184 #6# Km depending on enzyme form <16> Y Y ECO:0000006 Pubmed:1540623 BRENDA <16> Inazu, N.; Ruepp, B.; Wirth, H.; Wermuth, B.: Carbonyl reductasefrom human testis: purification and comparison with carbonyl reductasefrom human brain and rat testis. Biochim. Biophys. Acta (1992) 1116,50-56.{Pubmed:1540623}; PENTACON Notes: Tissue: Testis AAP 12/7/2011 1111 2000000230 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1.3-1.6 {4-Nitrobenzaldehyde} (#6# Km depending on enzyme form<16>) <16> mM 4-Nitrobenzaldehyde CHEBI:66926 1.1.1.184 #6# Km depending on enzyme form<16> Y Y ECO:0000006 Pubmed:1540623 BRENDA <16> Inazu, N.; Ruepp, B.; Wirth, H.; Wermuth, B.: Carbonyl reductasefrom human testis: purification and comparison with carbonyl reductasefrom human brain and rat testis. Biochim. Biophys. Acta (1992) 1116,50-56. {Pubmed:1540623}; PENTACON Notes: Tissue: Testis AAP 12/7/2011 1111 2000000231 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.31-0.45 {4-benzoylpyridine} (#6# Km depending on enzyme form<16>) <16> mM 4-benzoylpyridine 1.1.1.184 #6# Km depending on enzyme form<16> Y Y ECO:0000006 Pubmed:1540623 BRENDA <16> Inazu, N.; Ruepp, B.; Wirth, H.; Wermuth, B.: Carbonyl reductasefrom human testis: purification and comparison with carbonyl reductasefrom human brain and rat testis. Biochim. Biophys. Acta (1992) 1116,50-56. {Pubmed:1540623}; PENTACON Notes: Tissue: Testis; Request ChEBI ID: 4-benzoylpyridine, PubChem ID: CID 26731 AAP 12/7/2011 1111 2000000232 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.38-0.65 {4-carboxybenzaldehde} (#6# Km depending on enzyme form<16>) <16> mM 4-carboxybenzaldehde 1.1.1.184 #6# Km depending on enzyme form<16> Y Y ECO:0000006 Pubmed:1540623 BRENDA <16> Inazu, N.; Ruepp, B.; Wirth, H.; Wermuth, B.: Carbonyl reductasefrom human testis: purification and comparison with carbonyl reductasefrom human brain and rat testis. Biochim. Biophys. Acta (1992) 1116,50-56. {Pubmed:1540623}; PENTACON Notes: Tissue: Testis; Request ChEBI ID: 4-Carboxybenzaldehyde, Pubchem ID: CID 12088 AAP 12/7/2011 1111 2000000233 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.49-2 {pyridine-4-carboxaldehyde} (#6# Km depending on enzymeform <16>) <16> mM pyridine-4-carboxaldehyde 1.1.1.184 #6# Km depending on enzymeform <16> Y Y ECO:0000006 Pubmed:1540623 BRENDA <16> Inazu, N.; Ruepp, B.; Wirth, H.; Wermuth, B.: Carbonyl reductasefrom human testis: purification and comparison with carbonyl reductasefrom human brain and rat testis. Biochim. Biophys. Acta (1992) 1116,50-56. {Pubmed:1540623}; PENTACON Notes: Tissue: Testis; Request ChEBI ID: Pyridine4-carboxaldehyde, PubChem ID: CID 13389 AAP 12/7/2011 1111 2000000234 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.34 {prostaglandin E2} (#6# form CR8 <16>) <16> 0.34 mM prostaglandin E2 CHEBI:15551 Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Brain AAP 2000000235 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.08 {5alpha-androstane-3,17-dione} (#6# form CR8 <16>) <16> 0.08 mM 5alpha-androstane-3,17-dione CHEBI:15994 Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Brain AAP 2000000236 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.03 {5alpha-androstan-17beta-ol-3-one} (#6# form CR8 <16>) <16> 0.03 mM 5alpha-androstan-17beta-ol-3-one CHEBI:16330 Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Brain AAP 2000000237 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.05 {5alpha-androstan-17beta-ol-3-one} (#6# form CR2 <16>) <16> 0.05 mM 5alpha-androstan-17beta-ol-3-one CHEBI:16330 Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Testis AAP 2000000238 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.33 {prostaglandin B2} (#6# form CR8 <16>) <16> 0.33 mM prostaglandin B2 CHEBI:28099 Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Brain AAP 2000000239 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.39 {prostaglandin B2} (#6# form CR2 <16>) <16> 0.39 mM prostaglandin B2 CHEBI:28099 Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Testis AAP 2000000240 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.16-0.51 {Prostaglandin B2} (#6# Km depending on enzyme form<16>) <16> mM Prostaglandin B2 CHEBI:28099 Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Brain AAP 2000000241 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1.9 {4-nitroacetophenone} (#6# form CR8 <16>) <16> 1.9 mM 4-nitroacetophenone CHEBI:28735 Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Brain AAP 2000000242 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 2.5 {4-nitroacetophenone} (#6# form CR2 <16>) <16> 2.5 mM 4-nitroacetophenone CHEBI:28735 Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Testis AAP 2000000243 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1.9-2.7 {4-Nitroacetophenone} (#6# Km depending on enzyme form<16>) <16> mM 4-Nitroacetophenone CHEBI:28735 Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Brain AAP 2000000244 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.07 {menadione} (#6# form CR2 <16>) <16> 0.07 mM menadione CHEBI:28869 Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Testis AAP 2000000245 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.07 {menadione} (#6# form CR8 <16>) <16> 0.07 mM menadione CHEBI:28869 Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Brain AAP 2000000246 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.05-0.07 {menadione} (#6# Km depending on enzyme form <16>) <16> mM menadione CHEBI:28869 Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Brain AAP 2000000247 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1.5 {4-nitrobenzaldehyde} (#6# form CR2 <16>) <16> 1.5 mM 4-nitrobenzaldehyde CHEBI:66926 Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Testis AAP 2000000248 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 2.0 {4-nitrobenzaldehyde} (#6# form CR8 <16>) <16> 2 mM 4-nitrobenzaldehyde CHEBI:66926 Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Brain AAP 2000000249 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1.9-2.1 {4-Nitrobenzaldehyde} (#6# Km depending on enzyme form<16>) <16> mM 4-Nitrobenzaldehyde CHEBI:66926 Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Brain AAP 2000000250 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.31 {4-benzoylpyridine} (#6# form CR2 <16>) <16> 0.31 mM 4-benzoylpyridine Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Testis; Request ChEBI ID: 4-benzoylpyridine, PubChem ID: CID 26731 AAP 2000000251 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.32 {4-benzoylpyridine} (#6# form CR8 <16>) <16> 0.32 mM 4-benzoylpyridine Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Brain; Request ChEBI ID: 4-benzoylpyridine, PubChem ID: CID 26731 AAP 2000000252 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.32-0.44 {4-benzoylpyridine} (#6# Km depending on enzyme form<16>) <16> mM 4-benzoylpyridine Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Brain; Request ChEBI ID: 4-benzoylpyridine, PubChem ID: CID 26731 AAP 2000000253 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.54-1.37 {4-carboxybenzaldehde} (#6# Km depending on enzyme form<16>) <16> mM 4-carboxybenzaldehde Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Brain; Request ChEBI ID: 4-Carboxybenzaldehyde, Pubchem ID: CID 12088 AAP 2000000254 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.4 {4-Carboxybenzaldehyde} (#6# form CR2 <16>) <16> 0.4 mM 4-Carboxybenzaldehyde Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Testis; Request ChEBI ID: 4-Carboxybenzaldehyde, Pubchem ID: CID 12088 AAP 2000000255 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1.37 {4-Carboxybenzaldehyde} (#6# form CR8 <16>) <16> 1.37 mM 4-Carboxybenzaldehyde Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Brain; Request ChEBI ID: 4-Carboxybenzaldehyde, Pubchem ID: CID 12088 AAP 2000000256 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1.2-2.8 {pyridine-4-carboxaldehyde} (#6# Km depending on enzymeform <16>) <16> mM pyridine-4-carboxaldehyde Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Brain; Request ChEBI ID: Pyridine4-carboxaldehyde, PubChem ID: CID 13389 AAP 2000000257 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.49 {Pyridine4-carboxaldehyde} (#6# form CR2 <16>) <16> 0.49 mM Pyridine4-carboxaldehyde Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Testis; Request ChEBI ID: Pyridine4-carboxaldehyde, PubChem ID: CID 13389 AAP 2000000258 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1.2 {Pyridine4-carboxaldehyde} (#6# form CR8 <16>) <16> 1.2 mM Pyridine4-carboxaldehyde Y Y ECO:0000006 Pubmed:1540623 PENTACON Added by PENTACON; PENTACON Notes: Tissue: Brain; Request ChEBI ID: Pyridine4-carboxaldehyde, PubChem ID: CID 13389 AAP 2000000259 Jodi P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0097 {1-palmitoyl-2-(5-oxovaleryl)sn-glycero-3-phosphocholine} (#4# pH 6.0, 30°C <46>) <46> 0.0097 mM 1-palmitoyl-2-(5-oxovaleryl)sn-glycero-3-phosphocholine 1.1.1.21 #4# pH 6.0, 30°C <46> Y Y ECO:0000006 Pubmed:15465833 BRENDA <46> Srivastava, S.; Spite, M.; Trent, J.O.; West, M.B.; Ahmed, Y.;Bhatnagar, A.: Aldose reductase-catalyzed reduction of aldehydephospholipids. J. Biol. Chem. (2004) 279, 53395-53406. {Pubmed:15465833}; PENTACON Notes: Request ChEBI ID: 1-palmitoyl-2-(5-oxovaleryl)sn-glycero-3-phosphocholine AAP 12/7/2011 1111 2000000260 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.025 {menadione} (#6# pH 7.4, 37°C, recombinant enzyme <33>) <33> 0.025 mM menadione CHEBI:28869 1.1.1.184 #6# pH 7.4, 37°C, recombinant enzyme <33> Y Y ECO:0000006 Pubmed:15476404 BRENDA <33> Doorn, J.A.; Maser, E.; Blum, A.; Claffey, D.J.; Petersen, D.R.:Human carbonyl reductase catalyzes reduction of 4-oxonon-2-enal.Biochemistry (2004) 43, 13106-13114. {Pubmed:15476404} AAP 12/7/2011 1111 2000000261 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.345 {4-oxonon-2-enal} (#6# pH 7.4, 37°C, recombinant enzyme<33>) <33> 0.345 mM 4-oxonon-2-enal CHEBI:58972 1.1.1.184 #6# pH 7.4, 37°C, recombinant enzyme<33> Y Y ECO:0000006 Pubmed:15476404 BRENDA <33> Doorn, J.A.; Maser, E.; Blum, A.; Claffey, D.J.; Petersen, D.R.:Human carbonyl reductase catalyzes reduction of 4-oxonon-2-enal.Biochemistry (2004) 43, 13106-13114. {Pubmed:15476404} AAP 12/7/2011 1111 2000000262 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.329 {glutathione-4-oxonon-2-enal} (#6# pH 7.4, 37°C,recombinant enzyme <33>) <33> 0.329 mM glutathione-4-oxonon-2-enal 1.1.1.184 #6# pH 7.4, 37°C,recombinant enzyme <33> Y Y ECO:0000006 Pubmed:15476404 BRENDA <33> Doorn, J.A.; Maser, E.; Blum, A.; Claffey, D.J.; Petersen, D.R.:Human carbonyl reductase catalyzes reduction of 4-oxonon-2-enal.Biochemistry (2004) 43, 13106-13114. {Pubmed:15476404} ; PENTACON Notes: Request ChEBI ID: glutathione-4-oxonon-2-enal AAP 12/7/2011 1111 2000000263 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #6# 8200 {menadione} (#6# pH 7.4, 37°C, recombinant enzyme <33>) <33> 8200 nmol/min/mg menadione CHEBI:28869 Y Y ECO:0000006 Pubmed:15476404 PENTACON Added by PENTACON; PENTACON Notes: pH 7.4, 37°C AAP 2000000264 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #6# 7330 {4-oxonon-2-enal} (#6# pH 7.4, 37°C, recombinant enzyme<33>) <33> 7330 nmol/min/mg 4-oxonon-2-enal CHEBI:58972 Y Y ECO:0000006 Pubmed:15476404 PENTACON Added by PENTACON; PENTACON Notes: pH 7.4, 37°C AAP 2000000265 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #6# 214 {glutathione-4-oxonon-2-enal} (#6# pH 7.4, 37°C,recombinant enzyme <33>) <33> 214 nmol/min/mg glutathione-4-oxonon-2-enal Y Y ECO:0000006 Pubmed:15476404 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: glutathione-4-oxonon-2-enal; pH 7.4, 37°C AAP 2000000266 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.085 {NADPH} (#6# pH 7.4, 37°C, recombinant isozyme CBR M244<50>) <50> 0.085 mM NADPH CHEBI:16474 1.1.1.184 #6# pH 7.4, 37°C, recombinant isozyme CBR M244<50> Y Y ECO:0000006 Pubmed:15537833 BRENDA <50> Lakhman, S.S.; Ghosh, D.; Blanco, J.G.: Functional significance ofa natural allelic variant of human carbonyl reductase 3 (CBR3). DrugMetab. Dispos. (2005) 33, 254-257. {Pubmed:15537833}; PENTACON Notes: Isoform: M244 AAP 12/7/2011 1111 2000000267 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.0905 {NADPH} (#6# pH 7.4, 37°C, recombinant isozyme CBR V244<50>) <50> 0.0905 mM NADPH CHEBI:16474 1.1.1.184 #6# pH 7.4, 37°C, recombinant isozyme CBR V244<50> Y Y ECO:0000006 Pubmed:15537833 BRENDA <50> Lakhman, S.S.; Ghosh, D.; Blanco, J.G.: Functional significance ofa natural allelic variant of human carbonyl reductase 3 (CBR3). DrugMetab. Dispos. (2005) 33, 254-257. {Pubmed:15537833} AAP 12/7/2011 1111 2000000268 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.0229 {menadione} (#6# pH 7.4, 37°C, recombinant isozyme CBRM244 <50>) <50> 0.0229 mM menadione CHEBI:28869 1.1.1.184 #6# pH 7.4, 37°C, recombinant isozyme CBRM244 <50> Y Y ECO:0000006 Pubmed:15537833 BRENDA <50> Lakhman, S.S.; Ghosh, D.; Blanco, J.G.: Functional significance ofa natural allelic variant of human carbonyl reductase 3 (CBR3). DrugMetab. Dispos. (2005) 33, 254-257. {Pubmed:15537833}; PENTACON Notes: Isoform: M244 AAP 12/7/2011 1111 2000000269 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.0246 {menadione} (#6# pH 7.4, 37°C, recombinant isozyme CBRV244 <50>) <50> 0.0246 mM menadione CHEBI:28869 1.1.1.184 #6# pH 7.4, 37°C, recombinant isozyme CBRV244 <50> Y Y ECO:0000006 Pubmed:15537833 BRENDA <50> Lakhman, S.S.; Ghosh, D.; Blanco, J.G.: Functional significance ofa natural allelic variant of human carbonyl reductase 3 (CBR3). DrugMetab. Dispos. (2005) 33, 254-257. {Pubmed:15537833} AAP 12/7/2011 1111 2000000270 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #6# 32400 {NADPH} (#6# pH 7.4, 37°C, recombinant isozyme CBR V244<50>) <50> 32400 nmol/min/mg NADPH CHEBI:16474 Y Y ECO:0000006 Pubmed:15537833 PENTACON Added by PENTACON; PENTACON Notes: pH 7.4, 37°C AAP 2000000271 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #6# 53000 {NADPH} (#6# pH 7.4, 37°C, recombinant isozyme CBR M244<50>) <50> 53000 nmol/min/mg NADPH CHEBI:16474 Y Y ECO:0000006 Pubmed:15537833 PENTACON Added by PENTACON; PENTACON Notes: Isoform: M244; pH 7.4, 37°C AAP 2000000272 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #6# 19600 {menadione} (#6# pH 7.4, 37°C, recombinant isozyme CBRV244 <50>) <50> 19600 nmol/min/mg menadione CHEBI:28869 Y Y ECO:0000006 Pubmed:15537833 PENTACON Added by PENTACON; PENTACON Notes: pH 7.4, 37°C AAP 2000000273 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #6# 40600 {menadione} (#6# pH 7.4, 37°C, recombinant isozyme CBRM244 <50>) <50> 40600 nmol/min/mg menadione CHEBI:28869 Y Y ECO:0000006 Pubmed:15537833 PENTACON Added by PENTACON; PENTACON Notes: Isoform: M244; pH 7.4, 37°C AAP 2000000274 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.02 {DL-glyceraldehyde} (#4# pH 7.0, 25°C, recombinant wild-typeenzyme <59>) <19,59> 0.02 mM glyceraldehyde CHEBI:5445 1.1.1.21 #4# pH 7.0, 25°C, recombinant wild-typeenzyme <59> Y Y ECO:0000006 Pubmed:15769597 BRENDA <59> Bohren, K.M.; Brownlee, J.M.; Milne, A.C.; Gabbay, K.H.; Harrison,D.H.: The structure of Apo R268A human aldose reductase: Hinges andlatches that control the kinetic mechanism. Biochim. Biophys. Acta(2005) 1748, 201-212. {Pubmed:15769597} AAP 12/7/2011 1111 2000000275 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4,8# 0.03 {DL-glyceraldehyde} (#4# pH 7.0, 25°C, recombinant mutantS226A <59>) <12,59> 0.03 mM glyceraldehyde CHEBI:5445 1.1.1.21 #4# pH 7.0, 25°C, recombinant mutantS226A <59> Y Y ECO:0000006 Pubmed:15769597 BRENDA <59> Bohren, K.M.; Brownlee, J.M.; Milne, A.C.; Gabbay, K.H.; Harrison,D.H.: The structure of Apo R268A human aldose reductase: Hinges andlatches that control the kinetic mechanism. Biochim. Biophys. Acta(2005) 1748, 201-212. {Pubmed:15769597}; PENTACON Notes: Mutant: S226A AAP 12/7/2011 1111 2000000276 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.05 {DL-glyceraldehyde} (#4# pH 7.0, 25°C, recombinant mutantR268A <59>) <59> 0.05 mM glyceraldehyde CHEBI:5445 1.1.1.21 #4# pH 7.0, 25°C, recombinant mutantR268A <59> Y Y ECO:0000006 Pubmed:15769597 BRENDA <59> Bohren, K.M.; Brownlee, J.M.; Milne, A.C.; Gabbay, K.H.; Harrison,D.H.: The structure of Apo R268A human aldose reductase: Hinges andlatches that control the kinetic mechanism. Biochim. Biophys. Acta(2005) 1748, 201-212. {Pubmed:15769597}; PENTACON Notes: Mutant: R268A AAP 12/7/2011 1111 2000000277 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.11 {DL-glyceraldehyde} (#4# pH 7.0, 25°C, recombinant mutantS210A <59>) <59> 0.11 mM glyceraldehyde CHEBI:5445 1.1.1.21 #4# pH 7.0, 25°C, recombinant mutantS210A <59> Y Y ECO:0000006 Pubmed:15769597 BRENDA <59> Bohren, K.M.; Brownlee, J.M.; Milne, A.C.; Gabbay, K.H.; Harrison,D.H.: The structure of Apo R268A human aldose reductase: Hinges andlatches that control the kinetic mechanism. Biochim. Biophys. Acta(2005) 1748, 201-212. {Pubmed:15769597}; PENTACON Notes: Mutant: S210A AAP 12/7/2011 1111 2000000278 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.13 {DL-glyceraldehyde} (#4# pH 7.0, 25°C, recombinant mutantS214A <59>) <59> 0.13 mM glyceraldehyde CHEBI:5445 1.1.1.21 #4# pH 7.0, 25°C, recombinant mutantS214A <59> Y Y ECO:0000006 Pubmed:15769597 BRENDA <59> Bohren, K.M.; Brownlee, J.M.; Milne, A.C.; Gabbay, K.H.; Harrison,D.H.: The structure of Apo R268A human aldose reductase: Hinges andlatches that control the kinetic mechanism. Biochim. Biophys. Acta(2005) 1748, 201-212. {Pubmed:15769597}; PENTACON Notes: Mutant: S214A AAP 12/7/2011 1111 2000000279 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.42 {DL-glyceraldehyde} (#4# pH 7.0, 25°C, recombinant mutantG213S <59>) <59> 0.42 mM glyceraldehyde CHEBI:5445 1.1.1.21 #4# pH 7.0, 25°C, recombinant mutantG213S <59> Y Y ECO:0000006 Pubmed:15769597 BRENDA <59> Bohren, K.M.; Brownlee, J.M.; Milne, A.C.; Gabbay, K.H.; Harrison,D.H.: The structure of Apo R268A human aldose reductase: Hinges andlatches that control the kinetic mechanism. Biochim. Biophys. Acta(2005) 1748, 201-212. {Pubmed:15769597}; PENTACON Notes: Mutant: G213S AAP 12/7/2011 1111 2000000280 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.5 {DL-glyceraldehyde} (#4# pH 7.0, 25°C, recombinant mutantDELTA214-219 <59>) <59> 0.5 mM glyceraldehyde CHEBI:5445 1.1.1.21 #4# pH 7.0, 25°C, recombinant mutantDELTA214-219 <59> Y Y ECO:0000006 Pubmed:15769597 BRENDA <59> Bohren, K.M.; Brownlee, J.M.; Milne, A.C.; Gabbay, K.H.; Harrison,D.H.: The structure of Apo R268A human aldose reductase: Hinges andlatches that control the kinetic mechanism. Biochim. Biophys. Acta(2005) 1748, 201-212. {Pubmed:15769597}; PENTACON Notes: Mutant: DELTA214-219 AAP 12/7/2011 1111 2000000281 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.6 {DL-glyceraldehyde} (#4# pH 7.0, 25°C, recombinant mutantC298A <59>) <59> 0.6 mM glyceraldehyde CHEBI:5445 1.1.1.21 #4# pH 7.0, 25°C, recombinant mutantC298A <59> Y Y ECO:0000006 Pubmed:15769597 BRENDA <59> Bohren, K.M.; Brownlee, J.M.; Milne, A.C.; Gabbay, K.H.; Harrison,D.H.: The structure of Apo R268A human aldose reductase: Hinges andlatches that control the kinetic mechanism. Biochim. Biophys. Acta(2005) 1748, 201-212. {Pubmed:15769597}; PENTACON Notes: Mutant: C298A AAP 12/7/2011 1111 2000000282 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 3.7 {DL-glyceraldehyde} (#4# pH 7.0, 25°C, recombinant mutantG213P <59>) <59> 3.7 mM glyceraldehyde CHEBI:5445 1.1.1.21 #4# pH 7.0, 25°C, recombinant mutantG213P <59> Y Y ECO:0000006 Pubmed:15769597 BRENDA <59> Bohren, K.M.; Brownlee, J.M.; Milne, A.C.; Gabbay, K.H.; Harrison,D.H.: The structure of Apo R268A human aldose reductase: Hinges andlatches that control the kinetic mechanism. Biochim. Biophys. Acta(2005) 1748, 201-212. {Pubmed:15769597}; PENTACON Notes: Mutant: G213P AAP 12/7/2011 1111 2000000283 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.02 {DL-glyceraldehyde} (#4# pH 7.0, 25°C, recombinant mutant R293A <59>; #4# pH7.0, 25°C, recombinant mutant W219A <59>; #4# pH 7.0, 25°C,recombinant mutant W219E <59>) <19,59> 0.02 mM glyceraldehyde CHEBI:5445 1.1.1.21 #4# pH 7.0, 25°C, recombinant mutant R293A <59>; #4# pH7.0, 25°C, recombinant mutant W219A <59>; #4# pH 7.0, 25°C,recombinant mutant W219E <59> Y Y ECO:0000006 Pubmed:15769597 BRENDA <59> Bohren, K.M.; Brownlee, J.M.; Milne, A.C.; Gabbay, K.H.; Harrison,D.H.: The structure of Apo R268A human aldose reductase: Hinges andlatches that control the kinetic mechanism. Biochim. Biophys. Acta(2005) 1748, 201-212. {Pubmed:15769597}; PENTACON Notes: Mutant: recombinant mutant R293A, recombinant mutant W219A, recombinant mutant W219E AAP 12/7/2011 1111 2000000284 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 2.1 {D-Xylose} mutant R293A 2.1 mM D-Xylose CHEBI:65327 Y Y ECO:0000006 Pubmed:15769597 PENTACON Added by PENTACON; PENTACON Notes: Mutant: R293A AAP 2000000285 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 5.6 {D-Xylose} mutant W219E 5.6 mM D-Xylose CHEBI:65327 Y Y ECO:0000006 Pubmed:15769597 PENTACON Added by PENTACON; PENTACON Notes: Mutant: W219E AAP 2000000286 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 6.0 {D-Xylose} wild-type 6 mM D-Xylose CHEBI:65327 Y Y ECO:0000006 Pubmed:15769597 PENTACON Added by PENTACON AAP 2000000287 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 8.0 {D-Xylose} mutant R268A 8 mM D-Xylose CHEBI:65327 Y Y ECO:0000006 Pubmed:15769597 PENTACON Added by PENTACON; PENTACON Notes: Mutant: R268A AAP 2000000288 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 9.2 {D-Xylose} mutant W219A 9.2 mM D-Xylose CHEBI:65327 Y Y ECO:0000006 Pubmed:15769597 PENTACON Added by PENTACON; PENTACON Notes: Mutant: W219A AAP 2000000289 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 11 {D-Xylose} mutant S226A 11 mM D-Xylose CHEBI:65327 Y Y ECO:0000006 Pubmed:15769597 PENTACON Added by PENTACON; PENTACON Notes: Mutant: S226A AAP 2000000290 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 48 {D-Xylose} mutant S214A 48 mM D-Xylose CHEBI:65327 Y Y ECO:0000006 Pubmed:15769597 PENTACON Added by PENTACON; PENTACON Notes: Mutant: S214A AAP 2000000291 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 58 {D-Xylose} mutant S210A 58 mM D-Xylose CHEBI:65327 Y Y ECO:0000006 Pubmed:15769597 PENTACON Added by PENTACON; PENTACON Notes: Mutant: S210A AAP 2000000292 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 260 {D-Xylose} mutant G213S 260 mM D-Xylose CHEBI:65327 Y Y ECO:0000006 Pubmed:15769597 PENTACON Added by PENTACON; PENTACON Notes: Mutant: G213S AAP 2000000293 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 270 {D-Xylose} mutant DELTA214-219 270 mM D-Xylose CHEBI:65327 Y Y ECO:0000006 Pubmed:15769597 PENTACON Added by PENTACON; PENTACON Notes: Mutant: DELTA214-219 AAP 2000000294 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 400 {D-Xylose} mutant C298A 400 mM D-Xylose CHEBI:65327 Y Y ECO:0000006 Pubmed:15769597 PENTACON Added by PENTACON; PENTACON Notes: Mutant: C298A AAP 2000000295 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 5000 {D-Xylose} mutant G213P 5000 mM D-Xylose CHEBI:65327 Y Y ECO:0000006 Pubmed:15769597 PENTACON Added by PENTACON; PENTACON Notes: Mutant: G213P AAP 2000000296 Jodi O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.16 {prostaglandin H2} <25> 0.16 mM prostaglandin H2 CHEBI:15554 5.3.99.3 Y Y ECO:0000006 Pubmed:16399384 BRENDA <25> Pettersson, P.L.; Thoren, S.; Jakobsson, P.J.: Human microsomalprostaglandin E synthase 1: a member of the MAPEG protein superfamily.Methods Enzymol. (2005) 401, 147-161. {Pubmed:16399384} AAP 12/7/2011 1111 2000000297 Jodi O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.16 {prostaglandin G2} <12,25> 0.16 mM prostaglandin G2 CHEBI:27647 5.3.99.3 Y Y ECO:0000006 Pubmed:16399384 BRENDA <25> Pettersson, P.L.; Thoren, S.; Jakobsson, P.J.: Human microsomalprostaglandin E synthase 1: a member of the MAPEG protein superfamily.Methods Enzymol. (2005) 401, 147-161. {Pubmed:16399384} AAP 12/7/2011 1111 2000000298 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0021 {arachidonic acid} (#3# wild-type, cyclooxygenase activity<51>) <51> 0.0021 mM arachidonic acid CHEBI:15843 1.14.99.1 #3# wild-type, cyclooxygenase activity<51> Y Y ECO:0000006 Pubmed:16401081 BRENDA <51> Rogge, C.E.; Ho, B.; Liu, W.; Kulmacz, R.J.; Tsai, A.L.: Role ofTyr348 in Tyr385 radical dynamics and cyclooxygenase inhibitorinteractions in prostaglandin H synthase-2. Biochemistry (2006) 45,523-532. {Pubmed:16401081} AAP 12/7/2011 1111 2000000299 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0034 {arachidonic acid} (#3# mutant Y348F/Y504F, cyclooxygenaseactivity <51>) <51> 0.0034 mM arachidonic acid CHEBI:15843 1.14.99.1 #3# mutant Y348F/Y504F, cyclooxygenaseactivity <51> Y Y ECO:0000006 Pubmed:16401081 BRENDA <51> Rogge, C.E.; Ho, B.; Liu, W.; Kulmacz, R.J.; Tsai, A.L.: Role ofTyr348 in Tyr385 radical dynamics and cyclooxygenase inhibitorinteractions in prostaglandin H synthase-2. Biochemistry (2006) 45,523-532. {Pubmed:16401081}; PENTACON Notes: Mutant: mutant Y348F/Y504F AAP 12/7/2011 1111 2000000300 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0038 {arachidonic acid} (#3# mutant Y348F, cyclooxygenaseactivity <51>) <51> 0.0038 mM arachidonic acid CHEBI:15843 1.14.99.1 #3# mutant Y348F, cyclooxygenaseactivity <51> Y Y ECO:0000006 Pubmed:16401081 BRENDA <51> Rogge, C.E.; Ho, B.; Liu, W.; Kulmacz, R.J.; Tsai, A.L.: Role ofTyr348 in Tyr385 radical dynamics and cyclooxygenase inhibitorinteractions in prostaglandin H synthase-2. Biochemistry (2006) 45,523-532. {Pubmed:16401081}; PENTACON Notes: Mutant: mutant Y348F AAP 12/7/2011 1111 2000000301 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0042 {arachidonic acid} (#3# mutant Y504F, cyclooxygenaseactivity <51>) <51> 0.0042 mM arachidonic acid CHEBI:15843 1.14.99.1 #3# mutant Y504F, cyclooxygenaseactivity <51> Y Y ECO:0000006 Pubmed:16401081 BRENDA <51> Rogge, C.E.; Ho, B.; Liu, W.; Kulmacz, R.J.; Tsai, A.L.: Role ofTyr348 in Tyr385 radical dynamics and cyclooxygenase inhibitorinteractions in prostaglandin H synthase-2. Biochemistry (2006) 45,523-532. {Pubmed:16401081}; PENTACON Notes: Mutant: mutant Y504F AAP 12/7/2011 1111 2000000302 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #3# 0.00068 {nimesulide} (#3# wildtype <51>) <51> 0.00068 mM nimesulide CHEBI:44445 arachidonate CHEBI:32395 Y Y ECO:0000006 Pubmed:16401081 PENTACON Added by PENTACON AAP 2000000303 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# .138 {PPHP} (#3# wildtype, peroxidase activity <51>) <51> 0.138 mM PPHP Y Y ECO:0000006 Pubmed:16401081 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: 5-phenylpent-4-enyl-1-hydroperoxide, Pubchem ID: CID 6438577 AAP 2000000304 Jenn O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.13 {prostaglandin H2} (#2#wild-type, 0°C, pH 7.2 <38>) <38> 0.13 mM prostaglandin H2 CHEBI:15554 5.3.99.3 #2#wild-type, 0°C, pH 7.2 <38> Y Y ECO:0000006 Pubmed:16439136 BRENDA <38> Huang, X.; Yan, W.; Gao, D.; Tong, M.; Tai, H.H.; Zhan, C.G.:Structural and functional characterization of human microsomalprostaglandin E synthase-1 by computational modeling and site-directedmutagenesis. Bioorg. Med. Chem. (2006) 14, 3553-3562. {Pubmed:16439136} AAP 12/7/2011 1111 2000000305 Jenn O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.734 {prostaglandin H2} (#2#mutant Q134E, 0°C, pH 7.2 <38>) <38> 0.734 mM prostaglandin H2 CHEBI:15554 5.3.99.3 #2#mutant Q134E, 0°C, pH 7.2 <38> Y Y ECO:0000006 Pubmed:16439136 BRENDA <38> Huang, X.; Yan, W.; Gao, D.; Tong, M.; Tai, H.H.; Zhan, C.G.:Structural and functional characterization of human microsomalprostaglandin E synthase-1 by computational modeling and site-directedmutagenesis. Bioorg. Med. Chem. (2006) 14, 3553-3562. {Pubmed:16439136}; PENTACON Notes: Mutant: mutant Q134E AAP 12/7/2011 1111 2000000306 Jenn O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 1.61 {prostaglandin H2} (#2#mutant Q36E, 0°C, pH 7.2 <38>) <38> 1.61 mM prostaglandin H2 CHEBI:15554 5.3.99.3 #2#mutant Q36E, 0°C, pH 7.2 <38> Y Y ECO:0000006 Pubmed:16439136 BRENDA <38> Huang, X.; Yan, W.; Gao, D.; Tong, M.; Tai, H.H.; Zhan, C.G.:Structural and functional characterization of human microsomalprostaglandin E synthase-1 by computational modeling and site-directedmutagenesis. Bioorg. Med. Chem. (2006) 14, 3553-3562. {Pubmed:16439136}; PENTACON Notes: Mutant: mutant Q36E AAP 12/7/2011 1111 2000000307 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #16# 0.002 {cis-8,11,14-eicosatrienoic acid} <57> 0.002 mM cis-8,11,14-eicosatrienoic acid CHEBI:53486 1.14.99.1 Y Y ECO:0000006 Pubmed:16770009 BRENDA <57> Liu, W.; Cao, D.; Oh, S.F.; Serhan, C.N.; Kulmacz, R.J.: Divergentcyclooxygenase responses to fatty acid structure and peroxide level infish and mammalian prostaglandin H synthases. FASEB J. (2006) 20,1097-1108. {Pubmed:16770009} AAP 12/7/2011 1111 2000000308 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #14# 0.0017 {cis-5,8,11,14-eicosatetraenoic acid} <57> 0.0017 mM cis-5,8,11,14-eicosatetraenoic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:16770009 PENTACON Added by PENTACON AAP 2000000309 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #14# 0.0031 {alpha-linolenic acid} <57> 0.0031 mM alpha-linolenic acid CHEBI:27432 Y Y ECO:0000006 Pubmed:16770009 PENTACON Added by PENTACON AAP 2000000310 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #14# 0.0011 {cis-4,7,10,13,16,19-docosahexaenoic acid} <57> 0.0011 mM cis-4,7,10,13,16,19-docosahexaenoic acid CHEBI:28125 Y Y ECO:0000006 Pubmed:16770009 PENTACON Added by PENTACON AAP 2000000311 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #14# 0.0012 {cis-5,8,11,14,17-eicosapentaenoic acid} <57> 0.0012 mM cis-5,8,11,14,17-eicosapentaenoic acid CHEBI:28364 Y Y ECO:0000006 Pubmed:16770009 PENTACON Added by PENTACON AAP 2000000312 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #14# 0.0048 {gamma-linolenic acid} <57> 0.0048 mM gamma-linolenic acid CHEBI:28661 Y Y ECO:0000006 Pubmed:16770009 PENTACON Added by PENTACON AAP 2000000313 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #14# 0.0027 {cis-7,10,13,16-docosatetraenoic acid} <57> 0.0027 mM cis-7,10,13,16-docosatetraenoic acid CHEBI:53487 Y Y ECO:0000006 Pubmed:16770009 PENTACON Added by PENTACON AAP 2000000314 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #14# 0.0052 {cis-11,14-eicosadienoic acid} <57> 0.0052 mM cis-11,14-eicosadienoic acid CHEBI:73731 Y Y ECO:0000006 Pubmed:16770009 PENTACON Added by PENTACON AAP 2000000315 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.309 {prostaglandin E2} (#6# wild-type, 37°C, pH 7.4 <61>) <61> 0.309 mM prostaglandin E2 CHEBI:15551 1.1.1.184 #6# wild-type, 37°C, pH 7.4 <61> Y Y ECO:0000006 Pubmed:17344335 BRENDA <61> Gonzalez-Covarrubias, V.; Ghosh, D.; Lakhman, S.S.; Pendyala, L.;Blanco, J.G.: A functional genetic polymorphism on human carbonylreductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH bindingaffinity. Drug Metab. Dispos. (2007) 35, 973-980. {Pubmed:17344335} AAP 12/7/2011 1111 2000000316 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.32 {prostaglandin E2} (#6# mutant V88I, 37°C, pH 7.4 <61>) <61> 0.32 mM prostaglandin E2 CHEBI:15551 1.1.1.184 #6# mutant V88I, 37°C, pH 7.4 <61> Y Y ECO:0000006 Pubmed:17344335 BRENDA <61> Gonzalez-Covarrubias, V.; Ghosh, D.; Lakhman, S.S.; Pendyala, L.;Blanco, J.G.: A functional genetic polymorphism on human carbonylreductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH bindingaffinity. Drug Metab. Dispos. (2007) 35, 973-980. {Pubmed:17344335}; PENTACON Notes: Mutant: mutant V88I AAP 12/7/2011 1111 2000000317 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.247 {NADPH} (#6# wild-type, 37°C, pH 7.4 <61>) <61> 0.247 mM NADPH CHEBI:16474 1.1.1.184 #6# wild-type, 37°C, pH 7.4 <61> Y Y ECO:0000006 Pubmed:17344335 BRENDA <61> Gonzalez-Covarrubias, V.; Ghosh, D.; Lakhman, S.S.; Pendyala, L.;Blanco, J.G.: A functional genetic polymorphism on human carbonylreductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH bindingaffinity. Drug Metab. Dispos. (2007) 35, 973-980. {Pubmed:17344335} AAP 12/7/2011 1111 2000000318 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.343 {NADPH} (#6# mutant V88I, 37°C, pH 7.4 <61>) <61> 0.343 mM NADPH CHEBI:16474 1.1.1.184 #6# mutant V88I, 37°C, pH 7.4 <61> Y Y ECO:0000006 Pubmed:17344335 BRENDA <61> Gonzalez-Covarrubias, V.; Ghosh, D.; Lakhman, S.S.; Pendyala, L.;Blanco, J.G.: A functional genetic polymorphism on human carbonylreductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH bindingaffinity. Drug Metab. Dispos. (2007) 35, 973-980. {Pubmed:17344335} ; PENTACON Notes: Mutant: mutant V88I AAP 12/7/2011 1111 2000000319 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.042 {menadione} (#6# wild-type, 37°C, pH 7.4 <61>) <61> 0.042 mM menadione CHEBI:28869 1.1.1.184 #6# wild-type, 37°C, pH 7.4 <61> Y Y ECO:0000006 Pubmed:17344335 BRENDA <61> Gonzalez-Covarrubias, V.; Ghosh, D.; Lakhman, S.S.; Pendyala, L.;Blanco, J.G.: A functional genetic polymorphism on human carbonylreductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH bindingaffinity. Drug Metab. Dispos. (2007) 35, 973-980. {Pubmed:17344335} AAP 12/7/2011 1111 2000000320 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.055 {menadione} (#6# mutant V88I, 37°C, pH 7.4 <61>) <61> 0.055 mM menadione CHEBI:28869 1.1.1.184 #6# mutant V88I, 37°C, pH 7.4 <61> Y Y ECO:0000006 Pubmed:17344335 BRENDA <61> Gonzalez-Covarrubias, V.; Ghosh, D.; Lakhman, S.S.; Pendyala, L.;Blanco, J.G.: A functional genetic polymorphism on human carbonylreductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH bindingaffinity. Drug Metab. Dispos. (2007) 35, 973-980. {Pubmed:17344335}; PENTACON Notes: Mutant: mutant V88I AAP 12/7/2011 1111 2000000321 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.14 {daunorubicin} (#6# mutant V88I, 37°C, pH 7.4 <61>) <61> 0.14 mM daunorubicin CHEBI:41977 1.1.1.184 #6# mutant V88I, 37°C, pH 7.4 <61> Y Y ECO:0000006 Pubmed:17344335 BRENDA <61> Gonzalez-Covarrubias, V.; Ghosh, D.; Lakhman, S.S.; Pendyala, L.;Blanco, J.G.: A functional genetic polymorphism on human carbonylreductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH bindingaffinity. Drug Metab. Dispos. (2007) 35, 973-980. {Pubmed:17344335}; PENTACON Notes: Mutant: mutant V88I AAP 12/7/2011 1111 2000000322 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.173 {daunorubicin} (#6# wild-type, 37°C, pH 7.4 <61>) <61> 0.173 mM daunorubicin CHEBI:41977 1.1.1.184 #6# wild-type, 37°C, pH 7.4 <61> Y Y ECO:0000006 Pubmed:17344335 BRENDA <61> Gonzalez-Covarrubias, V.; Ghosh, D.; Lakhman, S.S.; Pendyala, L.;Blanco, J.G.: A functional genetic polymorphism on human carbonylreductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH bindingaffinity. Drug Metab. Dispos. (2007) 35, 973-980. {Pubmed:17344335} AAP 12/7/2011 1111 2000000323 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #6# 35 {prostaglandin E2} (#6# mutant V88I, 37°C, pH 7.4 <61>) <61> 35 nmol/min/mg prostaglandin E2 CHEBI:15551 Y Y ECO:0000006 Pubmed:17344335 PENTACON Added by PENTACON; PENTACON Notes: Mutant: mutant V88I; pH 7.4, 37°C AAP 2000000324 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #6# 53 {prostaglandin E2} (#6# wild-type, 37°C, pH 7.4 <61>) <61> 53 nmol/min/mg prostaglandin E2 CHEBI:15551 Y Y ECO:0000006 Pubmed:17344335 PENTACON Added by PENTACON; PENTACON Notes: pH 7.4, 37°C AAP 2000000325 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #6# 295 {NADPH} (#6# mutant V88I, 37°C, pH 7.4 <61>) <61> 295 nmol/min/mg NADPH CHEBI:16474 Y Y ECO:0000006 Pubmed:17344335 PENTACON Added by PENTACON; PENTACON Notes: Mutant: mutant V88I; pH 7.4, 37°C AAP 2000000326 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #6# 356 {NADPH} (#6# wild-type, 37°C, pH 7.4 <61>) <61> 356 nmol/min/mg NADPH CHEBI:16474 Y Y ECO:0000006 Pubmed:17344335 PENTACON Added by PENTACON; PENTACON Notes: pH 7.4, 37°C AAP 2000000327 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #6# 168 {menadione} (#6# mutant V88I, 37°C, pH 7.4 <61>) <61> 168 nmol/min/mg menadione CHEBI:28869 Y Y ECO:0000006 Pubmed:17344335 PENTACON Added by PENTACON; PENTACON Notes: Mutant: mutant V88I; pH 7.4, 37°C AAP 2000000328 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #6# 220 {menadione} (#6# wild-type, 37°C, pH 7.4 <61>) <61> 220 nmol/min/mg menadione CHEBI:28869 Y Y ECO:0000006 Pubmed:17344335 PENTACON Added by PENTACON; PENTACON Notes: pH 7.4, 37°C AAP 2000000329 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #6# 121 {daunorubicin} (#6# mutant V88I, 37°C, pH 7.4 <61>) <61> 121 nmol/min/mg daunorubicin CHEBI:41977 Y Y ECO:0000006 Pubmed:17344335 PENTACON Added by PENTACON; PENTACON Notes: Mutant: mutant V88I; pH 7.4, 37°C AAP 2000000330 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #6# 181 {daunorubicin} (#6# wild-type, 37°C, pH 7.4 <61>) <61> 181 nmol/min/mg daunorubicin CHEBI:41977 Y Y ECO:0000006 Pubmed:17344335 PENTACON Added by PENTACON; PENTACON Notes: pH 7.4, 37°C AAP 2000000331 Jenn P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.0066 {DELTA4-andostene-3,17-dione} (#2# pH 7.0, 37°C <39>) <39> 0.0066 mM DELTA4-andostene-3,17-dione CHEBI:16422 1.1.1.188 #2# pH 7.0, 37°C <39> Y Y ECO:0000006 Pubmed:17950253 BRENDA <39> Byrns, M.C.; Steckelbroeck, S.; Penning, T.M.: An indomethacinanalogue, N-(4-chlorobenzoyl)-melatonin, is a selective inhibitor ofaldo-keto reductase 1C3 (type 2 3alpha-HSD, type 5 17beta-HSD, andprostaglandin F synthase), a potential target for the treatment ofhormone dependent and hormone independent malignancies. Biochem.Pharmacol. (2008) 75, 484-493. {Pubmed:17950253} AAP 12/7/2011 1111 2000000332 Jenn P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.0015 {9,10-Phenanthrenequinone} (#2# pH 7.0, 37°C <39>) <39> 0.0015 mM 9,10-Phenanthrenequinone CHEBI:37454 1.1.1.188 #2# pH 7.0, 37°C <39> Y Y ECO:0000006 Pubmed:17950253 BRENDA <39> Byrns, M.C.; Steckelbroeck, S.; Penning, T.M.: An indomethacinanalogue, N-(4-chlorobenzoyl)-melatonin, is a selective inhibitor ofaldo-keto reductase 1C3 (type 2 3alpha-HSD, type 5 17beta-HSD, andprostaglandin F synthase), a potential target for the treatment ofhormone dependent and hormone independent malignancies. Biochem.Pharmacol. (2008) 75, 484-493. {Pubmed:17950253} AAP 12/7/2011 1111 2000000333 Jenn P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #2# 0.04 {Zomepirac} (#2# pH 7.0, 37°C <39>) <39> 0.04 mM Zomepirac CHEBI:35859 9,10-Phenanthrenequinone CHEBI:37454 Y Y ECO:0000006 Pubmed:17950253 PENTACON Added by PENTACON; PENTACON Notes: pH 7.0, 37°C AAP 2000000334 Jenn P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #2# 0.0023 {indomethacin} (#2# pH 7.0, 37°C <39>) <39> 0.0023 mM indometacin CHEBI:49662 9,10-Phenanthrenequinone CHEBI:37454 Y Y ECO:0000006 Pubmed:17950253 PENTACON Added by PENTACON; PENTACON Notes: pH 7.0, 37°C AAP 2000000335 Jenn P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #2# 0.0078 {Flurbiprofen} (#2# pH 7.0, 37°C <39>) <39> 0.0078 mM Flurbiprofen CHEBI:5130 9,10-Phenanthrenequinone CHEBI:37454 Y Y ECO:0000006 Pubmed:17950253 PENTACON Added by PENTACON; PENTACON Notes: pH 7.0, 37°C AAP 2000000336 Jenn P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #2# 0.0099 {Ibuprofen} (#2# pH 7.0, 37°C <39>) <39> 0.0099 mM Ibuprofen CHEBI:5855 9,10-Phenanthrenequinone CHEBI:37454 Y Y ECO:0000006 Pubmed:17950253 PENTACON Added by PENTACON; PENTACON Notes: pH 7.0, 37°C AAP 2000000337 Jenn P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #2# 0.007 {Meclofenamic Acid} (#2# pH 7.0, 37°C <39>) <39> 0.007 mM Meclofenamic Acid CHEBI:6710 9,10-Phenanthrenequinone CHEBI:37454 Y Y ECO:0000006 Pubmed:17950253 PENTACON Added by PENTACON; PENTACON Notes: pH 7.0, 37°C AAP 2000000338 Jenn P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #2# 0.0014 {Naproxen} (#2# pH 7.0, 37°C <39>) <39> 0.0014 mM Naproxen CHEBI:7476 9,10-Phenanthrenequinone CHEBI:37454 Y Y ECO:0000006 Pubmed:17950253 PENTACON Added by PENTACON; PENTACON Notes: pH 7.0, 37°C AAP 2000000339 Jenn P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #2# 0.0034 {sulindac} (#2# pH 7.0, 37°C <39>) <39> 0.0034 mM Sulindac CHEBI:9352 9,10-Phenanthrenequinone CHEBI:37454 Y Y ECO:0000006 Pubmed:17950253 PENTACON Added by PENTACON; PENTACON Notes: pH 7.0, 37°C AAP 2000000340 Jenn P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #2# 0.052 {N-(4-aminobenzyl)-6-methoxy-3-indole acetic acid} (#2# pH 7.0, 37°C <39>) <39> 0.052 mM N-(4-aminobenzyl)-6-methoxy-3-indole acetic acid 9,10-Phenanthrenequinone CHEBI:37454 Y Y ECO:0000006 Pubmed:17950253 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: N-(4-aminobenzyl)-6-methoxy-3-indole acetic acid; PENTACON Notes: Added by PENTACON; PENTACON Notes: pH 7.0, 37°C AAP 2000000341 Jodi O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #27# 0.13 {4-Nitrobenzaldehyde} (#27# pH 6.5, 25°C <65>) <65> 0.13 mM 4-Nitrobenzaldehyde CHEBI:66926 1.1.1.184 #27# pH 6.5, 25°C <65> Y Y ECO:0000006 Pubmed:18493841 BRENDA <65> Miura, T.; Nishinaka, T.; Terada, T.: Different functions betweenhuman monomeric carbonyl reductase 3 and carbonyl reductase 1. Mol.Cell. Biochem. (2008) 315, 113-121. {Pubmed:18493841} AAP 12/7/2011 1111 2000000342 Jodi O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #27# 0.3 {4-benzoylpyridine} (#27# pH 6.5, 25°C <65>) <65> 0.3 mM 4-benzoylpyridine 1.1.1.184 #27# pH 6.5, 25°C <65> Y Y ECO:0000006 Pubmed:18493841 BRENDA <65> Miura, T.; Nishinaka, T.; Terada, T.: Different functions betweenhuman monomeric carbonyl reductase 3 and carbonyl reductase 1. Mol.Cell. Biochem. (2008) 315, 113-121. {Pubmed:18493841}; PENTACON Notes: Request ChEBI ID: 4-benzoylpyridine, PubChem ID: CID 26731 AAP 12/7/2011 1111 2000000343 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.0852 {daunorubicin} (#6# pH 7.4, 37°C <60>) <60> 0.0852 mM daunorubicin CHEBI:41977 1.1.1.184 #6# pH 7.4, 37°C <60> Y Y ECO:0000006 Pubmed:18579125 BRENDA <60> Carlquist, M.; Frejd, T.; Gorwa-Grauslund, M.F.: Flavonoids asinhibitors of human carbonyl reductase 1. Chem. Biol. Interact. (2008)174, 98-108. {Pubmed:18579125} AAP 12/7/2011 1111 2000000344 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 3.490 {daunorubicin} 3490 nmol/min/mg daunorubicin CHEBI:41977 Y Y ECO:0000006 Pubmed:18579125 PENTACON Added by PENTACON AAP 2000000345 Jenn P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #25# 0.129 {Doxorubicin} (#25# purified enzyme <76>) <76> 0.129 mM Doxorubicin CHEBI:28748 Y Y ECO:0000006 Pubmed:18635746 PENTACON Added by PENTACON AAP 2000000346 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #25# 20.6 {Doxorubicin} (#25# purified enzyme <76>) <76> 20.6 nmol/min/mg Doxorubicin CHEBI:28748 Y Y ECO:0000006 Pubmed:18635746 PENTACON Added by PENTACON AAP 2000000347 Jenn P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #25# 183.5 {Doxorubicin} (#25# purified enzyme <76>) <76> 183.5 nmol/min/mg Doxorubicin CHEBI:28748 Y Y ECO:0000006 Pubmed:18635746 PENTACON Added by PENTACON AAP 2000000348 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #25# 0.167 {Doxorubicin} (#25# purified enzyme <76>) <76> 0.167 mM Doxorubicin CHEBI:28748 1.1.1.184 #25# purified enzyme <76> Y Y ECO:0000006 Pubmed:18635746 BRENDA <76> Kassner, N.; Huse, K.; Martin, H.J.; Goedtel-Armbrust, U.;Metzger, A.; Meineke, I.; Brockmoeller, J.; Klein, K.; Zanger, U.M.;Maser, E.; Wojnowski, L.: Carbonyl reductase 1 is a predominantdoxorubicin reductase in the human liver. Drug Metab. Dispos. (2008)36, 2113-2120. {Pubmed:18635746} AAP 12/7/2011 1111 2000000349 Jodi P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #11# 0.0019 {prostaglandin H2} <47> 0.0019 mM prostaglandin H2 CHEBI:15554 1.1.1.188 Y Y ECO:0000006 Pubmed:19010934 BRENDA <47> Kabututu, Z.; Manin, M.; Pointud, J.C.; Maruyama, T.; Nagata, N.;Lambert, S.; Lefrancois-Martinez, A.M.; Martinez, A.; Urade, Y.:Prostaglandin F2alpha synthase activities of aldo-keto reductase 1B1,1B3 and 1B7. J. Biochem. (2009) 145, 161-168. {Pubmed:19010934} AAP 12/7/2011 1111 2000000350 Jodi P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #15# 0.018 {prostaglandin H2} <47> 0.018 mM prostaglandin H2 CHEBI:15554 1.1.1.188 Y Y ECO:0000006 Pubmed:19010934 BRENDA <47> Kabututu, Z.; Manin, M.; Pointud, J.C.; Maruyama, T.; Nagata, N.;Lambert, S.; Lefrancois-Martinez, A.M.; Martinez, A.; Urade, Y.:Prostaglandin F2alpha synthase activities of aldo-keto reductase 1B1,1B3 and 1B7. J. Biochem. (2009) 145, 161-168. {Pubmed:19010934} AAP 12/7/2011 1111 2000000351 Jodi P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #11# 0.0057 {NADPH} <47> 0.0057 mM NADPH CHEBI:16474 1.1.1.188 Y Y ECO:0000006 Pubmed:19010934 BRENDA <47> Kabututu, Z.; Manin, M.; Pointud, J.C.; Maruyama, T.; Nagata, N.;Lambert, S.; Lefrancois-Martinez, A.M.; Martinez, A.; Urade, Y.:Prostaglandin F2alpha synthase activities of aldo-keto reductase 1B1,1B3 and 1B7. J. Biochem. (2009) 145, 161-168. {Pubmed:19010934} AAP 12/7/2011 1111 2000000352 Jodi P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #15# 3.9 {prostaglandin H2} <47> 3.9 nmol/min/mg prostaglandin H2 CHEBI:15554 Y Y ECO:0000006 Pubmed:19010934 PENTACON Added by PENTACON AAP 2000000353 Jodi P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #15# 26 {prostaglandin H2} <47> 26 nmol/min/mg prostaglandin H2 CHEBI:15554 Y Y ECO:0000006 Pubmed:19010934 PENTACON Added by PENTACON AAP 2000000354 Jodi P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #11# 0.009 {4-nitrobenzaldehyde} <47> 0.009 mM 4-nitrobenzaldehyde CHEBI:66926 Y Y ECO:0000006 Pubmed:19010934 PENTACON Added by PENTACON AAP 2000000355 Jodi P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #11# 37.1 {4-nitrobenzaldehyde} <47> 37.1 nmol/min/mg 4-nitrobenzaldehyde CHEBI:66926 Y Y ECO:0000006 Pubmed:19010934 PENTACON Added by PENTACON AAP 2000000356 Jodi P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #11# 0.012 {4-nitrobenzaldehyde} <47> 0.012 mM 4-nitrobenzaldehyde CHEBI:66926 Y Y ECO:0000006 Pubmed:19010934 PENTACON Added by PENTACON AAP 2000000357 Jodi P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #11# 408.3 {4-nitrobenzaldehyde} <47> 408.3 nmol/min/mg 4-nitrobenzaldehyde CHEBI:66926 Y Y ECO:0000006 Pubmed:19010934 PENTACON Added by PENTACON AAP 2000000358 Jenn O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.0024 {(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate} <55> 0.0024 mM prostaglandin H2 CHEBI:15554 5.3.99.3 Y Y ECO:0000006 Pubmed:19017494 BRENDA <55> Kim, W.I.; Choi, K.A.; Do, H.S.; Yu, Y.G.: Expression andpurification of human mPGES-1 in E. coli and identification ofinhibitory compounds from a drug-library. BMB Rep. (2008) 41, 808-813.{Pubmed:19017494} AAP 12/7/2011 1111 2000000359 Jenn O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #2# 0.0024 {(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate} <55> 0.23 mM dyphylline CHEBI:4728 prostaglandin H2 CHEBI:15554 Y Y ECO:0000006 Pubmed:19017494 PENTACON Added by PENTACON AAP 2000000360 Jenn O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #2# 0.0024 {(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate} <55> 0.11 mM oxacillin CHEBI:7809 prostaglandin H2 CHEBI:15554 Y Y ECO:0000006 Pubmed:19017494 PENTACON Added by PENTACON AAP 2000000361 Jenn O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #2# 0.0024 {(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate} <55> 3.5 nmol/min/mg prostaglandin H2 CHEBI:15554 Y Y ECO:0000006 Pubmed:19017494 PENTACON Added by PENTACON AAP 2000000362 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 49.3 {D-galactose} <2> 49.3 mM D-galactose CHEBI:12936 1.1.1.21 Y Y ECO:0000006 Pubmed:1901806 BRENDA <2> Tanimoto, T.; Ohta, M.; Tanaka, A.; Ikemoto, I.; Machida, T.:Purification and characterization of human testis aldose and aldehydereductase. Int. J. Biochem. (1991) 23, 421-428. {Pubmed:1901806} AAP 12/7/2011 1111 2000000363 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 5.05 {D-glucuronate} <2> 5.05 mM D-glucuronate CHEBI:15748 1.1.1.21 Y Y ECO:0000006 Pubmed:1901806 BRENDA <2> Tanimoto, T.; Ohta, M.; Tanaka, A.; Ikemoto, I.; Machida, T.:Purification and characterization of human testis aldose and aldehydereductase. Int. J. Biochem. (1991) 23, 421-428. {Pubmed:1901806} AAP 12/7/2011 1111 2000000364 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0032 {NADPH} <2> 0.0032 mM NADPH CHEBI:16474 1.1.1.21 Y Y ECO:0000006 Pubmed:1901806 BRENDA <2> Tanimoto, T.; Ohta, M.; Tanaka, A.; Ikemoto, I.; Machida, T.:Purification and characterization of human testis aldose and aldehydereductase. Int. J. Biochem. (1991) 23, 421-428. {Pubmed:1901806} AAP 12/7/2011 1111 2000000365 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.25 {NADH} <2> 0.25 mM NADH CHEBI:16908 1.1.1.21 Y Y ECO:0000006 Pubmed:1901806 BRENDA <2> Tanimoto, T.; Ohta, M.; Tanaka, A.; Ikemoto, I.; Machida, T.:Purification and characterization of human testis aldose and aldehydereductase. Int. J. Biochem. (1991) 23, 421-428. {Pubmed:1901806} AAP 12/7/2011 1111 2000000366 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 57.3 {D-glucose} <2> 57.3 mM D-glucose CHEBI:17634 1.1.1.21 Y Y ECO:0000006 Pubmed:1901806 BRENDA <2> Tanimoto, T.; Ohta, M.; Tanaka, A.; Ikemoto, I.; Machida, T.:Purification and characterization of human testis aldose and aldehydereductase. Int. J. Biochem. (1991) 23, 421-428. {Pubmed:1901806} AAP 12/7/2011 1111 2000000367 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.026 {DL-glyceraldehyde} <2,6> 0.026 mM glyceraldehyde CHEBI:5445 1.1.1.21 Y Y ECO:0000006 Pubmed:1901806 BRENDA <2> Tanimoto, T.; Ohta, M.; Tanaka, A.; Ikemoto, I.; Machida, T.:Purification and characterization of human testis aldose and aldehydereductase. Int. J. Biochem. (1991) 23, 421-428. {Pubmed:1901806} AAP 12/7/2011 1111 2000000368 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 6.2 {D-xylose} <2> 6.2 mM D-xylose CHEBI:65327 1.1.1.21 Y Y ECO:0000006 Pubmed:1901806 BRENDA <2> Tanimoto, T.; Ohta, M.; Tanaka, A.; Ikemoto, I.; Machida, T.:Purification and characterization of human testis aldose and aldehydereductase. Int. J. Biochem. (1991) 23, 421-428. {Pubmed:1901806} AAP 12/7/2011 1111 2000000369 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 43.3 {D-galactose} (#4# recombinant from baculovirus system inSpodoptera frugiperda cells <26>) <26> 43.3 mM D-galactose CHEBI:12936 1.1.1.21 #4# recombinant from baculovirus system inSpodoptera frugiperda cells <26> Y Y ECO:0000006 Pubmed:1905957 BRENDA <26> Nishimura, C.; Yamaoka, T.; Mizutani, M.; Yamashita, K.; Akera,T.; Tanimoto, T.: Purification and characterization of the recombinanthuman aldose reductase expressed in baculovirus system. Biochim.Biophys. Acta (1991) 1078, 171-178. {Pubmed:1905957} AAP 12/7/2011 1111 2000000370 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 3.53 {D-glucuronate} (#4# recombinant from baculovirus system inSpodoptera frugiperda cells <26>) <26> 3.53 mM D-glucuronate CHEBI:15748 1.1.1.21 #4# recombinant from baculovirus system inSpodoptera frugiperda cells <26> Y Y ECO:0000006 Pubmed:1905957 BRENDA <26> Nishimura, C.; Yamaoka, T.; Mizutani, M.; Yamashita, K.; Akera,T.; Tanimoto, T.: Purification and characterization of the recombinanthuman aldose reductase expressed in baculovirus system. Biochim.Biophys. Acta (1991) 1078, 171-178. {Pubmed:1905957} AAP 12/7/2011 1111 2000000371 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.004 {NADPH} (#4# recombinant from baculovirus system inSpodoptera frugiperda cells <26>) <26> 0.004 mM NADPH CHEBI:16474 1.1.1.21 #4# recombinant from baculovirus system inSpodoptera frugiperda cells <26> Y Y ECO:0000006 Pubmed:1905957 BRENDA <26> Nishimura, C.; Yamaoka, T.; Mizutani, M.; Yamashita, K.; Akera,T.; Tanimoto, T.: Purification and characterization of the recombinanthuman aldose reductase expressed in baculovirus system. Biochim.Biophys. Acta (1991) 1078, 171-178. {Pubmed:1905957} AAP 12/7/2011 1111 2000000372 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 98.1 {D-glucose} (#4# recombinant from E. coli <25>; #4#recombinant from baculovirus system in Spodoptera frugiperda cells<26>) <25,26> 98.1 mM D-glucose CHEBI:17634 1.1.1.21 #4# recombinant from E. coli <25>; #4#recombinant from baculovirus system in Spodoptera frugiperda cells<26> Y Y ECO:0000006 Pubmed:1905957 BRENDA <26> Nishimura, C.; Yamaoka, T.; Mizutani, M.; Yamashita, K.; Akera,T.; Tanimoto, T.: Purification and characterization of the recombinanthuman aldose reductase expressed in baculovirus system. Biochim.Biophys. Acta (1991) 1078, 171-178. {Pubmed:1905957} AAP 12/7/2011 1111 2000000373 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.018 {Glyceraldehyde} (#4# recombinant from baculovirus systemwith Spodoptera frugiperda cells <26>) <6,26> 0.018 mM glyceraldehyde CHEBI:5445 1.1.1.21 #4# recombinant from baculovirus systemwith Spodoptera frugiperda cells <26> Y Y ECO:0000006 Pubmed:1905957 BRENDA <26> Nishimura, C.; Yamaoka, T.; Mizutani, M.; Yamashita, K.; Akera,T.; Tanimoto, T.: Purification and characterization of the recombinanthuman aldose reductase expressed in baculovirus system. Biochim.Biophys. Acta (1991) 1078, 171-178. {Pubmed:1905957} AAP 12/7/2011 1111 2000000374 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 5.04 {D-xylose} (#4# recombinant fron baculovirus system inSpodoptera frugiperda cells <26>) <26> 5.04 mM D-xylose CHEBI:65327 1.1.1.21 #4# recombinant fron baculovirus system inSpodoptera frugiperda cells <26> Y Y ECO:0000006 Pubmed:1905957 BRENDA <26> Nishimura, C.; Yamaoka, T.; Mizutani, M.; Yamashita, K.; Akera,T.; Tanimoto, T.: Purification and characterization of the recombinanthuman aldose reductase expressed in baculovirus system. Biochim.Biophys. Acta (1991) 1078, 171-178. {Pubmed:1905957} AAP 12/7/2011 1111 2000000375 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #4# 0.00032 {sorbinil} (#4# recombinant from baculovirus system inSpodoptera frugiperda cells <26>) <26> 0.00032 mM sorbinil CHEBI:102029 NADPH CHEBI:16474 Y Y ECO:0000006 Pubmed:1905957 PENTACON Added by PENTACON AAP 2000000376 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #4# 0.00055 {sorbinil} (#4# purified from human testis <26>) <26> 0.00055 mM sorbinil CHEBI:102029 NADPH CHEBI:16474 Y Y ECO:0000006 Pubmed:1905957 PENTACON Added by PENTACON AAP 2000000377 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #4# 0.000018 {tolrestat} (#4# recombinant from baculovirus system inSpodoptera frugiperda cells <26>) <26> 0.000018 mM tolrestat CHEBI:48549 NADPH CHEBI:16474 Y Y ECO:0000006 Pubmed:1905957 PENTACON Added by PENTACON AAP 2000000378 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #4# 0.000018 {tolrestat} (#4# purified from human testis <26>) <26> 0.00002 mM tolrestat CHEBI:48549 NADPH CHEBI:16474 Y Y ECO:0000006 Pubmed:1905957 PENTACON Added by PENTACON AAP 2000000379 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #4# 0.00026 {epalrestat} (#4# purified from human testis <26>) <26> 0.000021 mM epalrestat NADPH CHEBI:16474 Y Y ECO:0000006 Pubmed:1905957 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: epalrestat, Chembl ID: CHEMBL56337 AAP 2000000380 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #4# 0.00026 {epalrestat} (#4# recombinant from baculovirus system inSpodoptera frugiperda cells <26>) <26> 0.00026 mM epalrestat NADPH CHEBI:16474 Y Y ECO:0000006 Pubmed:1905957 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: epalrestat, Chembl ID: CHEMBL56337 AAP 2000000381 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #4# 0.000014 {imirestat} (#4# recombinant from baculovirus system inSpodoptera frugiperda cells <26>) <26> 0.000014 mM imirestat NADPH CHEBI:16474 Y Y ECO:0000006 Pubmed:1905957 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: imirestat, Pubchem ID: CID 65673 AAP 2000000382 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #4# 0.000014 {imirestat} (#4# purified from human testis <26>) <26> 0.000015 mM imirestat NADPH CHEBI:16474 Y Y ECO:0000006 Pubmed:1905957 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: imirestat, Pubchem ID: CID 65673 AAP 2000000383 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #4# 0.0002 {M79175} (#4# recombinant from baculovirus system inSpodoptera frugiperda cells <26>) <26> 0.0002 mM M 79175 NADPH CHEBI:16474 Y Y ECO:0000006 Pubmed:1905957 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: M 79175, Pubchem ID: CID 115090 AAP 2000000384 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #4# 0.0002 {M79175} (#4# purified from human testis <26>) <26> 0.00044 mM M 79175 NADPH CHEBI:16474 Y Y ECO:0000006 Pubmed:1905957 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: M 79175, Pubchem ID: CID 115090 AAP 2000000385 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #4# 0.000011 {statil} (#4# purified from human testis <26>) <26> 0.000007 mM statil NADPH CHEBI:16474 Y Y ECO:0000006 Pubmed:1905957 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: statil Chembl ID: CHEMBL7679 AAP 2000000386 Jenn P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #4# 0.000011 {statil} (#4# recombinant from baculovirus system inSpodoptera frugiperda cells <26>) <26> 0.00032 mM statil NADPH CHEBI:16474 Y Y ECO:0000006 Pubmed:1905957 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: statil, Chembl ID: CHEMBL7679 AAP 2000000387 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #25# 0.0078 {isatin} (#25# wild-type CBR1 <75>) <75> 0.0078 mM isatin CHEBI:27539 1.1.1.184 #25# wild-type CBR1 <75> Y Y ECO:0000006 Pubmed:19061875 BRENDA <75> El-Hawari, Y.; Favia, A.D.; Pilka, E.S.; Kisiela, M.; Oppermann,U.; Martin, H.J.; Maser, E.: Analysis of the substrate-binding site ofhuman carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.Chem. Biol. Interact. (2009) 178, 234-241. {Pubmed:19061875} AAP 12/7/2011 1111 2000000388 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #27# 0.0225 {isatin} (#27# residues 142-143, 230, 236-244, 270 of CBR3exchanged to the corresponding amino acids of CBR1 <75>) <75> 0.0225 mM isatin CHEBI:27539 1.1.1.184 #27# residues 142-143, 230, 236-244, 270 of CBR3exchanged to the corresponding amino acids of CBR1 <75> Y Y ECO:0000006 Pubmed:19061875 BRENDA <75> El-Hawari, Y.; Favia, A.D.; Pilka, E.S.; Kisiela, M.; Oppermann,U.; Martin, H.J.; Maser, E.: Analysis of the substrate-binding site ofhuman carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.Chem. Biol. Interact. (2009) 178, 234-241. {Pubmed:19061875} ; PENTACON Notes: Mutant: residues 142-143, 230, 236-244, 270 of CBR3 exchanged to the corresponding amino acids of CBR1 AAP 12/7/2011 1111 2000000389 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #27# 0.0315 {isatin} (#27# residues 142-143, 230, 236-244 of CBR3exchanged to the corresponding amino acids of CBR1 <75>) <75> 0.0315 mM isatin CHEBI:27539 1.1.1.184 #27# residues 142-143, 230, 236-244 of CBR3exchanged to the corresponding amino acids of CBR1 <75> Y Y ECO:0000006 Pubmed:19061875 BRENDA <75> El-Hawari, Y.; Favia, A.D.; Pilka, E.S.; Kisiela, M.; Oppermann,U.; Martin, H.J.; Maser, E.: Analysis of the substrate-binding site ofhuman carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.Chem. Biol. Interact. (2009) 178, 234-241. {Pubmed:19061875} ; PENTACON Notes: Mutant: residues 142-143, 230, 236-244 of CBR3 exchanged to the corresponding amino acids of CBR1 AAP 12/7/2011 1111 2000000390 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #27# 0.0327 {isatin} (#27# residues 230, 236-244, 270 of CBR3exchanged to the corresponding amino acids of CBR1 <75>) <75> 0.0327 mM isatin CHEBI:27539 1.1.1.184 #27# residues 230, 236-244, 270 of CBR3exchanged to the corresponding amino acids of CBR1 <75> Y Y ECO:0000006 Pubmed:19061875 BRENDA <75> El-Hawari, Y.; Favia, A.D.; Pilka, E.S.; Kisiela, M.; Oppermann,U.; Martin, H.J.; Maser, E.: Analysis of the substrate-binding site ofhuman carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.Chem. Biol. Interact. (2009) 178, 234-241. {Pubmed:19061875} ; PENTACON Notes: Mutant: residues 230, 236-244, 270 of CBR3 exchanged to the corresponding amino acids of CBR1 AAP 12/7/2011 1111 2000000391 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #27# 0.0471 {isatin} (#27# residues 230, 236-244 of CBR3 exchanged tothe corresponding amino acids of CBR1 <75>) <75> 0.0471 mM isatin CHEBI:27539 1.1.1.184 #27# residues 230, 236-244 of CBR3 exchanged tothe corresponding amino acids of CBR1 <75> Y Y ECO:0000006 Pubmed:19061875 BRENDA <75> El-Hawari, Y.; Favia, A.D.; Pilka, E.S.; Kisiela, M.; Oppermann,U.; Martin, H.J.; Maser, E.: Analysis of the substrate-binding site ofhuman carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.Chem. Biol. Interact. (2009) 178, 234-241. {Pubmed:19061875} ; PENTACON Notes: Mutant: residues 230, 236-244 of CBR3 exchanged to the corresponding amino acids of CBR1 AAP 12/7/2011 1111 2000000392 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #27# 0.055 {isatin} (#27# residues 97-98, 230, 236-244 of CBR3exchanged to the corresponding amino acids of CBR1 <75>) <75> 0.055 mM isatin CHEBI:27539 1.1.1.184 #27# residues 97-98, 230, 236-244 of CBR3exchanged to the corresponding amino acids of CBR1 <75> Y Y ECO:0000006 Pubmed:19061875 BRENDA <75> El-Hawari, Y.; Favia, A.D.; Pilka, E.S.; Kisiela, M.; Oppermann,U.; Martin, H.J.; Maser, E.: Analysis of the substrate-binding site ofhuman carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.Chem. Biol. Interact. (2009) 178, 234-241. {Pubmed:19061875} ; PENTACON Notes: Mutant: residues 97-98, 230, 236-244 of CBR3 exchanged to the corresponding amino acids of CBR1 AAP 12/7/2011 1111 2000000393 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #27# 1.6 {isatin} (#27# residues 236-244 of CBR3 exchanged to thecorresponding amino acids of CBR1 <75>) <75> 1.6 mM isatin CHEBI:27539 1.1.1.184 #27# residues 236-244 of CBR3 exchanged to thecorresponding amino acids of CBR1 <75> Y Y ECO:0000006 Pubmed:19061875 BRENDA <75> El-Hawari, Y.; Favia, A.D.; Pilka, E.S.; Kisiela, M.; Oppermann,U.; Martin, H.J.; Maser, E.: Analysis of the substrate-binding site ofhuman carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.Chem. Biol. Interact. (2009) 178, 234-241. {Pubmed:19061875} ; PENTACON Notes: Mutant: residues 236-244 of CBR3 exchanged to the corresponding amino acids of CBR1 AAP 12/7/2011 1111 2000000394 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #27# 4 {isatin} (#27# wild-type CBR3 and mutant V244M. Residues262-277, 236-244/262-277 or 230 of CBR3 exchanged to the correspondingamino acids of CBR1 <75>) <75> mM isatin CHEBI:27539 1.1.1.184 #27# wild-type CBR3 and mutant V244M. Residues262-277, 236-244/262-277 or 230 of CBR3 exchanged to the correspondingamino acids of CBR1 <75> Y Y ECO:0000006 Pubmed:19061875 BRENDA <75> El-Hawari, Y.; Favia, A.D.; Pilka, E.S.; Kisiela, M.; Oppermann,U.; Martin, H.J.; Maser, E.: Analysis of the substrate-binding site ofhuman carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.Chem. Biol. Interact. (2009) 178, 234-241. {Pubmed:19061875} AAP 12/7/2011 1111 2000000395 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #27# 4 {isatin} (#27# wild-type CBR3 and mutant V244M. Residues262-277, 236-244/262-277 or 230 of CBR3 exchanged to the correspondingamino acids of CBR1 <75>) <75> mM isatin CHEBI:27539 1.1.1.184 #27# wild-type CBR3 and mutant V244M. Residues262-277, 236-244/262-277 or 230 of CBR3 exchanged to the correspondingamino acids of CBR1 <75> Y Y ECO:0000006 Pubmed:19061875 BRENDA <75> El-Hawari, Y.; Favia, A.D.; Pilka, E.S.; Kisiela, M.; Oppermann,U.; Martin, H.J.; Maser, E.: Analysis of the substrate-binding site ofhuman carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.Chem. Biol. Interact. (2009) 178, 234-241. {Pubmed:19061875}; PENTACON Notes: Mutant: mutant V244M. Residues 262-277, 236-244/262-277 or 230 of CBR3 exchanged to the corresponding amino acids of CBR1 AAP 12/7/2011 1111 2000000396 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #27# 0.0043 {9,10-Phenanthrenequinone} (#27# residues 142-143, 230,236-244, 270 of CBR3 exchanged to the corresponding amino acids of CBR1<75>) <75> 0.0043 mM 9,10-Phenanthrenequinone CHEBI:37454 1.1.1.184 #27# residues 142-143, 230,236-244, 270 of CBR3 exchanged to the corresponding amino acids of CBR1<75> Y Y ECO:0000006 Pubmed:19061875 BRENDA <75> El-Hawari, Y.; Favia, A.D.; Pilka, E.S.; Kisiela, M.; Oppermann,U.; Martin, H.J.; Maser, E.: Analysis of the substrate-binding site ofhuman carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.Chem. Biol. Interact. (2009) 178, 234-241. {Pubmed:19061875}; PENTACON Notes: Mutant: residues 142-143, 230,236-244, 270 of CBR3 exchanged to the corresponding amino acids of CBR1 AAP 12/7/2011 1111 2000000397 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #27# 0.0089 {9,10-Phenanthrenequinone} (#27# residues 230, 236-244,270 of CBR3 exchanged to the corresponding amino acids of CBR1 <75>) <75> 0.0089 mM 9,10-Phenanthrenequinone CHEBI:37454 1.1.1.184 #27# residues 230, 236-244,270 of CBR3 exchanged to the corresponding amino acids of CBR1 <75> Y Y ECO:0000006 Pubmed:19061875 BRENDA <75> El-Hawari, Y.; Favia, A.D.; Pilka, E.S.; Kisiela, M.; Oppermann,U.; Martin, H.J.; Maser, E.: Analysis of the substrate-binding site ofhuman carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.Chem. Biol. Interact. (2009) 178, 234-241. {Pubmed:19061875}; PENTACON Notes: Mutant: residues 230, 236-244,270 of CBR3 exchanged to the corresponding amino acids of CBR1 AAP 12/7/2011 1111 2000000398 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #27# 0.0092 {9,10-Phenanthrenequinone} (#27# residues 97-98, 230,236-244 of CBR3 exchanged to the corresponding amino acids of CBR1<75>) <75> 0.0092 mM 9,10-Phenanthrenequinone CHEBI:37454 1.1.1.184 #27# residues 97-98, 230,236-244 of CBR3 exchanged to the corresponding amino acids of CBR1<75> Y Y ECO:0000006 Pubmed:19061875 BRENDA <75> El-Hawari, Y.; Favia, A.D.; Pilka, E.S.; Kisiela, M.; Oppermann,U.; Martin, H.J.; Maser, E.: Analysis of the substrate-binding site ofhuman carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.Chem. Biol. Interact. (2009) 178, 234-241. {Pubmed:19061875}; PENTACON Notes: Mutant: residues 97-98, 230, 236-244 of CBR3 exchanged to the corresponding amino acids of CBR1 AAP 12/7/2011 1111 2000000399 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #25# 0.0354 {9,10-Phenanthrenequinone} (#25# wild-type CBR1 <75>) <75> 0.0354 mM 9,10-Phenanthrenequinone CHEBI:37454 1.1.1.184 #25# wild-type CBR1 <75> Y Y ECO:0000006 Pubmed:19061875 BRENDA <75> El-Hawari, Y.; Favia, A.D.; Pilka, E.S.; Kisiela, M.; Oppermann,U.; Martin, H.J.; Maser, E.: Analysis of the substrate-binding site ofhuman carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.Chem. Biol. Interact. (2009) 178, 234-241. {Pubmed:19061875} AAP 12/7/2011 1111 2000000400 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #27# 0.0393 {9,10-Phenanthrenequinone} (#27# residues 142-143, 230,236-244 of CBR3 exchanged to the corresponding amino acids of CBR1<75>) <75> 0.0393 mM 9,10-Phenanthrenequinone CHEBI:37454 1.1.1.184 #27# residues 142-143, 230,236-244 of CBR3 exchanged to the corresponding amino acids of CBR1<75> Y Y ECO:0000006 Pubmed:19061875 BRENDA <75> El-Hawari, Y.; Favia, A.D.; Pilka, E.S.; Kisiela, M.; Oppermann,U.; Martin, H.J.; Maser, E.: Analysis of the substrate-binding site ofhuman carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.Chem. Biol. Interact. (2009) 178, 234-241. {Pubmed:19061875}; PENTACON Notes: Mutant: residues 142-143, 230, 236-244 of CBR3 exchanged to the corresponding amino acids of CBR1 AAP 12/7/2011 1111 2000000401 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #27# 0.0564 {9,10-Phenanthrenequinone} (#27# residues 230, 236–244of CBR3 exchanged to the corresponding amino acids of CBR1 <75>) <75> 0.0564 mM 9,10-Phenanthrenequinone CHEBI:37454 1.1.1.184 #27# residues 230, 236–244of CBR3 exchanged to the corresponding amino acids of CBR1 <75> Y Y ECO:0000006 Pubmed:19061875 BRENDA <75> El-Hawari, Y.; Favia, A.D.; Pilka, E.S.; Kisiela, M.; Oppermann,U.; Martin, H.J.; Maser, E.: Analysis of the substrate-binding site ofhuman carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.Chem. Biol. Interact. (2009) 178, 234-241. {Pubmed:19061875}; PENTACON Notes: Mutant: residues 230, 236-€“244 of CBR3 exchanged to the corresponding amino acids of CBR1 AAP 12/7/2011 1111 2000000402 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #27# 0.078 {9,10-Phenanthrenequinone} (#27# wild-type CBR3 and mutantV244M. Residues 236-244, 262-277, 236-244/262-277 or 230 of CBR3exchanged to the corresponding amino acids of CBR1 <75>) <75> mM 9,10-Phenanthrenequinone CHEBI:37454 1.1.1.184 #27# wild-type CBR3 and mutantV244M. Residues 236-244, 262-277, 236-244/262-277 or 230 of CBR3exchanged to the corresponding amino acids of CBR1 <75> Y Y ECO:0000006 Pubmed:19061875 BRENDA <75> El-Hawari, Y.; Favia, A.D.; Pilka, E.S.; Kisiela, M.; Oppermann,U.; Martin, H.J.; Maser, E.: Analysis of the substrate-binding site ofhuman carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.Chem. Biol. Interact. (2009) 178, 234-241. {Pubmed:19061875} AAP 12/7/2011 1111 2000000403 Jenn O75828 874 CBR3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #27# 0.078 {9,10-Phenanthrenequinone} (#27# wild-type CBR3 and mutantV244M. Residues 236-244, 262-277, 236-244/262-277 or 230 of CBR3exchanged to the corresponding amino acids of CBR1 <75>) <75> mM 9,10-Phenanthrenequinone CHEBI:37454 1.1.1.184 #27# wild-type CBR3 and mutantV244M. Residues 236-244, 262-277, 236-244/262-277 or 230 of CBR3exchanged to the corresponding amino acids of CBR1 <75> Y Y ECO:0000006 Pubmed:19061875 BRENDA <75> El-Hawari, Y.; Favia, A.D.; Pilka, E.S.; Kisiela, M.; Oppermann,U.; Martin, H.J.; Maser, E.: Analysis of the substrate-binding site ofhuman carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.Chem. Biol. Interact. (2009) 178, 234-241. {Pubmed:19061875} ; PENTACON Notes: Mutant: mutant V244M. Residues 236-244, 262-277, 236-244/262-277 or 230 of CBR3 exchanged to the corresponding amino acids of CBR1 AAP 12/7/2011 1111 2000000404 Jodi P41222 5730 PTGDS Homo sapiens 9606 Comment/biophysicochemical properties/KM #4,13# 0.014 {(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate} (#4,13# pH 8.0 <65>) <65> 0.014 mM prostaglandin H2 CHEBI:15554 5.3.99.2 #4,13# pH 8.0 <65> Y Y ECO:0000006 Pubmed:19131342 BRENDA <65> Irikura, D.; Aritake, K.; Nagata, N.; Maruyama, T.; Shimamoto, S.;Urade, Y.: Biochemical, functional and pharmacological characterizationof AT-56, an orally active and selective inhibitor of lipocalin-typeprostaglandin d synthase. J. Biol. Chem. (2009) 284, 7623-7630.{Pubmed:19131342} AAP 12/7/2011 1111 2000000405 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #25# 0.287 {Doxorubicin} (#25# wild-type <77>) <77> 0.287 mM Doxorubicin CHEBI:28748 1.1.1.184 #25# wild-type <77> Y Y ECO:0000006 Pubmed:19204081 BRENDA <77> Bains, O.S.; Karkling, M.J.; Grigliatti, T.A.; Reid, R.E.; Riggs,K.W.: Two nonsynonymous single nucleotide polymorphisms of humancarbonyl reductase 1 demonstrate reduced in vitro metabolism ofdaunorubicin and doxorubicin. Drug Metab. Dispos. (2009) 37, 1107-1114.{Pubmed:19204081} AAP 12/7/2011 1111 2000000406 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #25# 0.325 {Doxorubicin} (#25# single nucleotide polymorphism P131Smutation <77>) <77> 0.325 mM Doxorubicin CHEBI:28748 1.1.1.184 #25# single nucleotide polymorphism P131Smutation <77> Y Y ECO:0000006 Pubmed:19204081 BRENDA <77> Bains, O.S.; Karkling, M.J.; Grigliatti, T.A.; Reid, R.E.; Riggs,K.W.: Two nonsynonymous single nucleotide polymorphisms of humancarbonyl reductase 1 demonstrate reduced in vitro metabolism ofdaunorubicin and doxorubicin. Drug Metab. Dispos. (2009) 37, 1107-1114.{Pubmed:19204081}; PENTACON Notes: Mutant: P131S mutation AAP 12/7/2011 1111 2000000407 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #25# 0.335 {Doxorubicin} (#25# single nucleotide polymorphism V88Imutation <77>) <77> 0.335 mM Doxorubicin CHEBI:28748 1.1.1.184 #25# single nucleotide polymorphism V88Imutation <77> Y Y ECO:0000006 Pubmed:19204081 BRENDA <77> Bains, O.S.; Karkling, M.J.; Grigliatti, T.A.; Reid, R.E.; Riggs,K.W.: Two nonsynonymous single nucleotide polymorphisms of humancarbonyl reductase 1 demonstrate reduced in vitro metabolism ofdaunorubicin and doxorubicin. Drug Metab. Dispos. (2009) 37, 1107-1114.{Pubmed:19204081}; PENTACON Notes: Mutant: V88I mutation AAP 12/7/2011 1111 2000000408 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #25# 0.018 {menadione} (#25# single nucleotide polymorphism V88Imutation <77>) <77> 0.018 mM menadione CHEBI:28869 1.1.1.184 #25# single nucleotide polymorphism V88Imutation <77> Y Y ECO:0000006 Pubmed:19204081 BRENDA <77> Bains, O.S.; Karkling, M.J.; Grigliatti, T.A.; Reid, R.E.; Riggs,K.W.: Two nonsynonymous single nucleotide polymorphisms of humancarbonyl reductase 1 demonstrate reduced in vitro metabolism ofdaunorubicin and doxorubicin. Drug Metab. Dispos. (2009) 37, 1107-1114.{Pubmed:19204081}; PENTACON Notes: Mutant: V88I mutation AAP 12/7/2011 1111 2000000409 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #25# 0.024 {menadione} (#25# wild-type <77>) <77> 0.024 mM menadione CHEBI:28869 1.1.1.184 #25# wild-type <77> Y Y ECO:0000006 Pubmed:19204081 BRENDA <77> Bains, O.S.; Karkling, M.J.; Grigliatti, T.A.; Reid, R.E.; Riggs,K.W.: Two nonsynonymous single nucleotide polymorphisms of humancarbonyl reductase 1 demonstrate reduced in vitro metabolism ofdaunorubicin and doxorubicin. Drug Metab. Dispos. (2009) 37, 1107-1114.{Pubmed:19204081} AAP 12/7/2011 1111 2000000410 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #25# 0.045 {menadione} (#25# single nucleotide polymorphism P131Smutation <77>) <77> 0.045 mM menadione CHEBI:28869 1.1.1.184 #25# single nucleotide polymorphism P131Smutation <77> Y Y ECO:0000006 Pubmed:19204081 BRENDA <77> Bains, O.S.; Karkling, M.J.; Grigliatti, T.A.; Reid, R.E.; Riggs,K.W.: Two nonsynonymous single nucleotide polymorphisms of humancarbonyl reductase 1 demonstrate reduced in vitro metabolism ofdaunorubicin and doxorubicin. Drug Metab. Dispos. (2009) 37, 1107-1114.{Pubmed:19204081}; PENTACON Notes: Mutant: P131S mutation AAP 12/7/2011 1111 2000000411 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #25# 0.051 {daunorubicin} (#25# wild-type <77>) <77> 0.051 mM daunorubicin CHEBI:41977 1.1.1.184 #25# wild-type <77> Y Y ECO:0000006 Pubmed:19204081 BRENDA <77> Bains, O.S.; Karkling, M.J.; Grigliatti, T.A.; Reid, R.E.; Riggs,K.W.: Two nonsynonymous single nucleotide polymorphisms of humancarbonyl reductase 1 demonstrate reduced in vitro metabolism ofdaunorubicin and doxorubicin. Drug Metab. Dispos. (2009) 37, 1107-1114.{Pubmed:19204081} AAP 12/7/2011 1111 2000000412 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #25# 0.089 {daunorubicin} (#25# single nucleotide polymorphism P131Smutation <77>) <77> 0.089 mM daunorubicin CHEBI:41977 1.1.1.184 #25# single nucleotide polymorphism P131Smutation <77> Y Y ECO:0000006 Pubmed:19204081 BRENDA <77> Bains, O.S.; Karkling, M.J.; Grigliatti, T.A.; Reid, R.E.; Riggs,K.W.: Two nonsynonymous single nucleotide polymorphisms of humancarbonyl reductase 1 demonstrate reduced in vitro metabolism ofdaunorubicin and doxorubicin. Drug Metab. Dispos. (2009) 37, 1107-1114.{Pubmed:19204081}; PENTACON Notes: Mutant: P131S mutation AAP 12/7/2011 1111 2000000413 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 257 {doxorubicin} single nucleotide polymorphism V88I mutation 257 nmol/min/mg Doxorubicin CHEBI:28748 Y Y ECO:0000006 Pubmed:19204081 PENTACON Added by PENTACON; PENTACON Notes: Mutant: V88I mutation AAP 2000000414 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 325 {doxorubicin} single nucleotide polymorphism P131S mutation 325 nmol/min/mg Doxorubicin CHEBI:28748 Y Y ECO:0000006 Pubmed:19204081 PENTACON Added by PENTACON; PENTACON Notes: Mutant: P131S mutation AAP 2000000415 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 364 {doxorubicin} wild-type 364 nmol/min/mg Doxorubicin CHEBI:28748 Y Y ECO:0000006 Pubmed:19204081 PENTACON Added by PENTACON AAP 2000000416 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 334 {menadione} single nucleotide polymorphism V88I mutation 334 nmol/min/mg menadione CHEBI:28869 Y Y ECO:0000006 Pubmed:19204081 PENTACON Added by PENTACON; PENTACON Notes: Mutant: V88I mutation AAP 2000000417 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 537 {menadione} wild-type 537 nmol/min/mg menadione CHEBI:28869 Y Y ECO:0000006 Pubmed:19204081 PENTACON Added by PENTACON AAP 2000000418 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 581 {menadione} single nucleotide polymorphism P131S mutation 581 nmol/min/mg menadione CHEBI:28869 Y Y ECO:0000006 Pubmed:19204081 PENTACON Added by PENTACON; PENTACON Notes: Mutant: P131S mutation AAP 2000000419 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #25# 0.051 {daunorubicin} (#25# single nucleotidepolymorphism V88I mutation <77>) <77> 0.051 mM daunorubicin CHEBI:41977 1.1.1.184 #25# single nucleotidepolymorphism V88I mutation <77> Y Y ECO:0000006 Pubmed:19204081 BRENDA <77> Bains, O.S.; Karkling, M.J.; Grigliatti, T.A.; Reid, R.E.; Riggs,K.W.: Two nonsynonymous single nucleotide polymorphisms of humancarbonyl reductase 1 demonstrate reduced in vitro metabolism ofdaunorubicin and doxorubicin. Drug Metab. Dispos. (2009) 37, 1107-1114.{Pubmed:19204081}; PENTACON Notes: Mutant: V88I mutation AAP 12/7/2011 1111 2000000420 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 2090 {daunorubicin} single nucleotide polymorphism V88I mutation 2090 nmol/min/mg daunorubicin CHEBI:41977 Y Y ECO:0000006 Pubmed:19204081 PENTACON Added by PENTACON; PENTACON Notes: Mutant: V88I mutation AAP 2000000421 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 3430 {daunorubicin} wild-type 3430 nmol/min/mg daunorubicin CHEBI:41977 Y Y ECO:0000006 Pubmed:19204081 PENTACON Added by PENTACON AAP 2000000422 Christie P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 3570 {daunorubicin} single nucleotide polymorphism P131S mutation 3570 nmol/min/mg daunorubicin CHEBI:41977 Y Y ECO:0000006 Pubmed:19204081 PENTACON Added by PENTACON; PENTACON Notes: Mutant: P131S mutation AAP 2000000423 Christie P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #14# 0.0055 {Linoleic acid} (#14# isozyme PGHS-1, in 100 mM Tris-HClbuffer (pH 7.4), at 24°C <73>) <73> 0.0055 mM Linoleic acid CHEBI:17351 1.14.99.1 #14# isozyme PGHS-1, in 100 mM Tris-HClbuffer (pH 7.4), at 24°C <73> Y Y ECO:0000006 Pubmed:19457650 BRENDA <73> Kawakami, Y.; Nakamura, T.; Hosokawa, T.; Suzuki-Yamamoto, T.;Yamashita, H.; Kimoto, M.; Tsuji, H.; Yoshida, H.; Hada, T.; Takahashi,Y.: Antiproliferative activity of guava leaf extract via inhibition ofprostaglandin endoperoxide H synthase isoforms. Prostaglandins Leukot.Essent. Fatty Acids (2009) 80, 239-245. {Pubmed:19457650} AAP 12/7/2011 1111 2000000424 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #16# 0.0068 {Linoleic acid} (#16# isozyme PGHS-2, in 100 mM Tris-HClbuffer (pH 7.4), at 24°C <73>) <73> 0.0068 mM Linoleic acid CHEBI:17351 1.14.99.1 #16# isozyme PGHS-2, in 100 mM Tris-HClbuffer (pH 7.4), at 24°C <73> Y Y ECO:0000006 Pubmed:19457650 BRENDA <73> Kawakami, Y.; Nakamura, T.; Hosokawa, T.; Suzuki-Yamamoto, T.;Yamashita, H.; Kimoto, M.; Tsuji, H.; Yoshida, H.; Hada, T.; Takahashi,Y.: Antiproliferative activity of guava leaf extract via inhibition ofprostaglandin endoperoxide H synthase isoforms. Prostaglandins Leukot.Essent. Fatty Acids (2009) 80, 239-245. {Pubmed:19457650} AAP 12/7/2011 1111 2000000425 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #14# 0.0009 {arachidonate} (#14# purified isoform PGHS-2, method:coupled, homo-vanilic acid <66>) <66> 0.0009 mM arachidonate CHEBI:32395 Y Y ECO:0000033 Pubmed:19728984 PENTACON Added by PENTACON; PENTACON Notes: purified isoform PGHS-2, method:coupled, homo-vanilic acid AAP 2000000426 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #14# 0.0011 {arachidonate} (#14# purified isoform PGHS-2, method:direct, O2 <66>) <66> 0.0011 mM arachidonate CHEBI:32395 Y Y ECO:0000033 Pubmed:19728984 PENTACON Added by PENTACON; PENTACON Notes: purified isoform PGHS-2, method:direct, O2 AAP 2000000427 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #14# 0.0017 {arachidonate} (#14# purified isoform PGHS-2, method:direct, O2 <66>) <66> 0.0017 mM arachidonate CHEBI:32395 Y Y ECO:0000033 Pubmed:19728984 PENTACON Added by PENTACON; PENTACON Notes: purified isoform PGHS-2, method:direct, O2 AAP 2000000428 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #14# 0.002 {arachidonate} (#14# purified isoform PGHS-2, method:direct, O2 <66>) <66> 0.002 mM arachidonate CHEBI:32395 Y Y ECO:0000033 Pubmed:19728984 PENTACON Added by PENTACON; PENTACON Notes: purified isoform PGHS-2, method:direct, O2 AAP 2000000429 Jodi P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #16# 0.0045 {arachidonate} (#16# purified isoform PGHS-1, method:direct, O2 <66>) <66> 0.0045 mM arachidonate CHEBI:32395 Y Y ECO:0000033 Pubmed:19728984 PENTACON Added by PENTACON; PENTACON Notes: purified isoform PGHS-1, method:direct, O2 AAP 2000000430 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #14# 0.005 {arachidonate} (#14# purified isoform PGHS-2, method:direct, O2 <66>) <66> 0.005 mM arachidonate CHEBI:32395 Y Y ECO:0000033 Pubmed:19728984 PENTACON Added by PENTACON; PENTACON Notes: purified isoform PGHS-2, method:direct, O2 AAP 2000000431 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #14# 0.0051 {arachidonate} (#14# purified isoform PGHS-2, method:direct, O2 <66>) <66> 0.0051 mM arachidonate CHEBI:32395 Y Y ECO:0000033 Pubmed:19728984 PENTACON Added by PENTACON; PENTACON Notes: purified isoform PGHS-2, method:direct, O2 AAP 2000000432 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #14# 0.009 {arachidonate} (#14# purified isoform PGHS-2, method:direct, O2 <66>) <66> 0.009 mM arachidonate CHEBI:32395 Y Y ECO:0000033 Pubmed:19728984 PENTACON Added by PENTACON; PENTACON Notes: purified isoform PGHS-2, method:direct, O2 AAP 2000000433 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #14# 0.0092 {arachidonate} (#14# purified isoform PGHS-2, method:direct, O2 <66>) <66> 0.0092 mM arachidonate CHEBI:32395 Y Y ECO:0000033 Pubmed:19728984 PENTACON Added by PENTACON; PENTACON Notes: purified isoform PGHS-2, method:direct, O2 AAP 2000000434 Jodi P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #14# 0.01 {arachidonate} (#14# purified isoform PGHS-2, method:direct, arachidonate <66>; #14# purified isoform PGHS-2, method:direct, trimethyl phosphine oxide <66>) <66> 0.01 mM arachidonate CHEBI:32395 Y Y ECO:0000033 Pubmed:19728984 PENTACON Added by PENTACON; PENTACON Notes: purified isoform PGHS-2, method:direct, O2 AAP 2000000435 Jodi P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #16# 0.0102 {arachidonate} (#16# purified isoform PGHS-1, method:direct, arachidonate <66>) <66> 0.0102 mM arachidonate CHEBI:32395 Y Y ECO:0000033 Pubmed:19728984 PENTACON Added by PENTACON; PENTACON Notes: purified isoform PGHS-1, method:direct, O2 AAP 2000000436 Jodi P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.232 {NADPH} (#4# pH 6.0, 30°C, ALR2 <137>) <137> 0.232 mM NADPH CHEBI:16474 1.1.1.21 #4# pH 6.0, 30°C, ALR2 <137> Y Y ECO:0000006 Pubmed:19850041 BRENDA <137> Muthenna, P.; Suryanarayana, P.; Gunda, S.K.; Petrash, J.M.;Reddy, G.B.: Inhibition of aldose reductase by dietary antioxidantcurcumin: mechanism of inhibition, specificity and significance. FEBSLett. (2009) 583, 3637-3642. {Pubmed:19850041} AAP 12/7/2011 1111 2000000437 Jodi P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #4# 0.074 {NADPH} (#4# pH 6.0, 30°C, ALR2 <137>) <137> 0.074 umol/min/mg NADPH CHEBI:16474 Y Y ECO:0000006 Pubmed:19850041 PENTACON Added by PENTACON; PENTACON Notes: pH 6.0, 30°C, ALR2 AAP 2000000438 Chandra O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.215 {prostaglandin H2} (#2# wild type enzyme <80>) <80> 0.215 mM prostaglandin H2 CHEBI:15554 5.3.99.3 #2# wild type enzyme <80> Y Y ECO:0000006 Pubmed:20369883 BRENDA <80> Hamza, A.; Tong, M.; AbdulHameed, M.D.; Liu, J.; Goren, A.C.; Tai,H.H.; Zhan, C.G.: Understanding microscopic binding of human microsomalprostaglandin E synthase-1 (mPGES-1) trimer with substrate PGH2 andcofactor GSH: insights from computational alanine scanning andsite-directed mutagenesis. J. Phys. Chem. B (2010) 114, 5605-5616.{Pubmed:20369883} AAP 12/7/2011 1111 2000000439 Chandra O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.2832 {prostaglandin H2} (#2# mutant enzyme Y117S <80>) <80> 0.2832 mM prostaglandin H2 CHEBI:15554 5.3.99.3 #2# mutant enzyme Y117S <80> Y Y ECO:0000006 Pubmed:20369883 BRENDA <80> Hamza, A.; Tong, M.; AbdulHameed, M.D.; Liu, J.; Goren, A.C.; Tai,H.H.; Zhan, C.G.: Understanding microscopic binding of human microsomalprostaglandin E synthase-1 (mPGES-1) trimer with substrate PGH2 andcofactor GSH: insights from computational alanine scanning andsite-directed mutagenesis. J. Phys. Chem. B (2010) 114, 5605-5616.{Pubmed:20369883}; PENTACON Notes: Mutant: Y117S AAP 12/7/2011 1111 2000000440 Chandra O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.296 {prostaglandin H2} (#2# mutant enzyme R70A <80>) <80> 0.296 mM prostaglandin H2 CHEBI:15554 5.3.99.3 #2# mutant enzyme R70A <80> Y Y ECO:0000006 Pubmed:20369883 BRENDA <80> Hamza, A.; Tong, M.; AbdulHameed, M.D.; Liu, J.; Goren, A.C.; Tai,H.H.; Zhan, C.G.: Understanding microscopic binding of human microsomalprostaglandin E synthase-1 (mPGES-1) trimer with substrate PGH2 andcofactor GSH: insights from computational alanine scanning andsite-directed mutagenesis. J. Phys. Chem. B (2010) 114, 5605-5616.{Pubmed:20369883}; PENTACON Notes: Mutant: R70A AAP 12/7/2011 1111 2000000441 Chandra O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.372 {prostaglandin H2} (#2# mutant enzyme R122A <80>) <80> 0.372 mM prostaglandin H2 CHEBI:15554 5.3.99.3 #2# mutant enzyme R122A <80> Y Y ECO:0000006 Pubmed:20369883 BRENDA <80> Hamza, A.; Tong, M.; AbdulHameed, M.D.; Liu, J.; Goren, A.C.; Tai,H.H.; Zhan, C.G.: Understanding microscopic binding of human microsomalprostaglandin E synthase-1 (mPGES-1) trimer with substrate PGH2 andcofactor GSH: insights from computational alanine scanning andsite-directed mutagenesis. J. Phys. Chem. B (2010) 114, 5605-5616.{Pubmed:20369883}; PENTACON Notes: Mutant: R122A AAP 12/7/2011 1111 2000000442 Chandra O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.3842 {prostaglandin H2} (#2# mutant enzyme T129V <80>) <80> 0.3842 mM prostaglandin H2 CHEBI:15554 5.3.99.3 #2# mutant enzyme T129V <80> Y Y ECO:0000006 Pubmed:20369883 BRENDA <80> Hamza, A.; Tong, M.; AbdulHameed, M.D.; Liu, J.; Goren, A.C.; Tai,H.H.; Zhan, C.G.: Understanding microscopic binding of human microsomalprostaglandin E synthase-1 (mPGES-1) trimer with substrate PGH2 andcofactor GSH: insights from computational alanine scanning andsite-directed mutagenesis. J. Phys. Chem. B (2010) 114, 5605-5616.{Pubmed:20369883}; PENTACON Notes: Mutant: T129V AAP 12/7/2011 1111 2000000443 Chandra O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.4643 {prostaglandin H2} (#2# mutant enzyme N74A <80>) <80> 0.4643 mM prostaglandin H2 CHEBI:15554 5.3.99.3 #2# mutant enzyme N74A <80> Y Y ECO:0000006 Pubmed:20369883 BRENDA <80> Hamza, A.; Tong, M.; AbdulHameed, M.D.; Liu, J.; Goren, A.C.; Tai,H.H.; Zhan, C.G.: Understanding microscopic binding of human microsomalprostaglandin E synthase-1 (mPGES-1) trimer with substrate PGH2 andcofactor GSH: insights from computational alanine scanning andsite-directed mutagenesis. J. Phys. Chem. B (2010) 114, 5605-5616.{Pubmed:20369883}; PENTACON Notes: Mutant: N74A AAP 12/7/2011 1111 2000000444 Chandra O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.4737 {prostaglandin H2} (#2# mutant enzyme R70A/R122A <80>) <80> 0.4737 mM prostaglandin H2 CHEBI:15554 5.3.99.3 #2# mutant enzyme R70A/R122A <80> Y Y ECO:0000006 Pubmed:20369883 BRENDA <80> Hamza, A.; Tong, M.; AbdulHameed, M.D.; Liu, J.; Goren, A.C.; Tai,H.H.; Zhan, C.G.: Understanding microscopic binding of human microsomalprostaglandin E synthase-1 (mPGES-1) trimer with substrate PGH2 andcofactor GSH: insights from computational alanine scanning andsite-directed mutagenesis. J. Phys. Chem. B (2010) 114, 5605-5616.{Pubmed:20369883}; PENTACON Notes: Mutant: R70A/R122A AAP 12/7/2011 1111 2000000445 Chandra O14684 9536 PTGES Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.5345 {prostaglandin H2} (#2# mutant enzyme Y117A <80>) <80> 0.5345 mM prostaglandin H2 CHEBI:15554 5.3.99.3 #2# mutant enzyme Y117A <80> Y Y ECO:0000006 Pubmed:20369883 BRENDA <80> Hamza, A.; Tong, M.; AbdulHameed, M.D.; Liu, J.; Goren, A.C.; Tai,H.H.; Zhan, C.G.: Understanding microscopic binding of human microsomalprostaglandin E synthase-1 (mPGES-1) trimer with substrate PGH2 andcofactor GSH: insights from computational alanine scanning andsite-directed mutagenesis. J. Phys. Chem. B (2010) 114, 5605-5616.{Pubmed:20369883}; PENTACON Notes: Mutant: Y117A AAP 12/7/2011 1111 2000000446 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 40 {D-galactose} <6> 40 mM D-galactose CHEBI:12936 1.1.1.21 Y Y ECO:0000006 Pubmed:6814912 BRENDA <6> Wermuth, B.; Burgisser, H.; Bohren, K.; von Wartburg, J.P.:Purification and characterization of human-brain aldose reductase. Eur.J. Biochem. (1982) 127, 279-284. {Pubmed:6814912} AAP 12/7/2011 1111 2000000447 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4,8# 5 {D-glucuronate} <6,12> 5 mM D-glucuronate CHEBI:15748 1.1.1.21 Y Y ECO:0000006 Pubmed:6814912 BRENDA <6> Wermuth, B.; Burgisser, H.; Bohren, K.; von Wartburg, J.P.:Purification and characterization of human-brain aldose reductase. Eur.J. Biochem. (1982) 127, 279-284. {Pubmed:6814912} AAP 12/7/2011 1111 2000000448 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.035 {D-glyceraldehyde} <6> 0.035 mM D-glyceraldehyde CHEBI:17378 1.1.1.21 Y Y ECO:0000006 Pubmed:6814912 BRENDA <6> Wermuth, B.; Burgisser, H.; Bohren, K.; von Wartburg, J.P.:Purification and characterization of human-brain aldose reductase. Eur.J. Biochem. (1982) 127, 279-284. {Pubmed:6814912} AAP 12/7/2011 1111 2000000449 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 95 {D-glucose} <6> 95 mM D-glucose CHEBI:17634 1.1.1.21 Y Y ECO:0000006 Pubmed:6814912 BRENDA <6> Wermuth, B.; Burgisser, H.; Bohren, K.; von Wartburg, J.P.:Purification and characterization of human-brain aldose reductase. Eur.J. Biochem. (1982) 127, 279-284. {Pubmed:6814912} AAP 12/7/2011 1111 2000000450 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.018 {L-Glyceraldehyde} (#4# recombinant from baculovirus systemwith Spodoptera frugiperda cells <26>) <6,26> 0.018 mM L-Glyceraldehyde CHEBI:27975 1.1.1.21 #4# recombinant from baculovirus systemwith Spodoptera frugiperda cells <26> Y Y ECO:0000006 Pubmed:6814912 BRENDA <6> Wermuth, B.; Burgisser, H.; Bohren, K.; von Wartburg, J.P.:Purification and characterization of human-brain aldose reductase. Eur.J. Biochem. (1982) 127, 279-284. {Pubmed:6814912} AAP 12/7/2011 1111 2000000451 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.025 {DL-glyceraldehyde} <2,6> 0.025 mM glyceraldehyde CHEBI:5445 1.1.1.21 Y Y ECO:0000006 Pubmed:6814912 BRENDA <6> Wermuth, B.; Burgisser, H.; Bohren, K.; von Wartburg, J.P.:Purification and characterization of human-brain aldose reductase. Eur.J. Biochem. (1982) 127, 279-284. {Pubmed:6814912} AAP 12/7/2011 1111 2000000452 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 5.1 {D-xylose} <6> 5.1 mM D-xylose CHEBI:65327 1.1.1.21 Y Y ECO:0000006 Pubmed:6814912 BRENDA <6> Wermuth, B.; Burgisser, H.; Bohren, K.; von Wartburg, J.P.:Purification and characterization of human-brain aldose reductase. Eur.J. Biochem. (1982) 127, 279-284. {Pubmed:6814912} AAP 12/7/2011 1111 2000000453 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 100 {L-Xylose} <6> 100 mM L-Xylose CHEBI:65328 1.1.1.21 Y Y ECO:0000006 Pubmed:6814912 BRENDA <6> Wermuth, B.; Burgisser, H.; Bohren, K.; von Wartburg, J.P.:Purification and characterization of human-brain aldose reductase. Eur.J. Biochem. (1982) 127, 279-284. {Pubmed:6814912} AAP 12/7/2011 1111 2000000454 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.002 {4-Nitrobenzaldehyde} <6> 0.002 mM 4-Nitrobenzaldehyde CHEBI:66926 1.1.1.21 Y Y ECO:0000006 Pubmed:6814912 BRENDA <6> Wermuth, B.; Burgisser, H.; Bohren, K.; von Wartburg, J.P.:Purification and characterization of human-brain aldose reductase. Eur.J. Biochem. (1982) 127, 279-284. {Pubmed:6814912} AAP 12/7/2011 1111 2000000455 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4,22# 0.003 {4-Nitrobenzaldehyde} (#4# 4-hydroxyphenylglycolaldehyde<6>) <3,6> 0.003 mM 4-Nitrobenzaldehyde CHEBI:66926 1.1.1.21 #4# 4-hydroxyphenylglycolaldehyde<6> Y Y ECO:0000006 Pubmed:6814912 BRENDA <6> Wermuth, B.; Burgisser, H.; Bohren, K.; von Wartburg, J.P.:Purification and characterization of human-brain aldose reductase. Eur.J. Biochem. (1982) 127, 279-284. {Pubmed:6814912} AAP 12/7/2011 1111 2000000456 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.01 {4-Hydroxyphenylacetaldehyde} <6> 0.01 mM (4-hydroxyphenyl)acetaldehyde CHEBI:15621 1.1.1.21 Y Y ECO:0000006 Pubmed:6814912 BRENDA <6> Wermuth, B.; Burgisser, H.; Bohren, K.; von Wartburg, J.P.:Purification and characterization of human-brain aldose reductase. Eur.J. Biochem. (1982) 127, 279-284. {Pubmed:6814912} AAP 12/7/2011 1111 2000000457 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.016 {Indole-3-acetaldehyde} <6> 0.016 mM indol-3-ylacetaldehyde CHEBI:18086 1.1.1.21 Y Y ECO:0000006 Pubmed:6814912 BRENDA <6> Wermuth, B.; Burgisser, H.; Bohren, K.; von Wartburg, J.P.:Purification and characterization of human-brain aldose reductase. Eur.J. Biochem. (1982) 127, 279-284. {Pubmed:6814912} AAP 12/7/2011 1111 2000000458 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.001 {20alpha-Isocorticosterone} (#4# and 20alpha-isocortisol,values below <6>) <6> 0.001 mM 20alpha-Isocorticosterone 1.1.1.21 #4# and 20alpha-isocortisol,values below <6> Y Y ECO:0000006 Pubmed:6814912 BRENDA <6> Wermuth, B.; Burgisser, H.; Bohren, K.; von Wartburg, J.P.:Purification and characterization of human-brain aldose reductase. Eur.J. Biochem. (1982) 127, 279-284. {Pubmed:6814912}; PENTACON Notes: Request ChEBI ID: 20alpha-Isocorticosterone AAP 12/7/2011 1111 2000000459 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.45 {prostaglandin E1} (#6# enzyme form CR8 <2>) <2> 0.45 mM prostaglandin E1 CHEBI:15544 1.1.1.184 #6# enzyme form CR8 <2> Y Y ECO:0000006 Pubmed:7005231 BRENDA <2> Wermuth, B.: Purification and properties of an NADPH-dependentcarbonyl reductase from human brain. Relationship to prostaglandin9-ketoreductase and xenobiotic ketone reductase. J. Biol. Chem. (1981)256, 1206-1213. {Pubmed:7005231} AAP 12/7/2011 1111 2000000460 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.004-0.01 {NADPH} (#6# + 4-nitrobenzaldehyde, Km depending onenzyme form <2>) <2> mM NADPH CHEBI:16474 1.1.1.184 #6# + 4-nitrobenzaldehyde, Km depending onenzyme form <2> Y Y ECO:0000006 Pubmed:7005231 BRENDA <2> Wermuth, B.: Purification and properties of an NADPH-dependentcarbonyl reductase from human brain. Relationship to prostaglandin9-ketoreductase and xenobiotic ketone reductase. J. Biol. Chem. (1981)256, 1206-1213. {Pubmed:7005231} AAP 12/7/2011 1111 2000000461 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.045-0.06 {menadione} (#6# Km depending on enzyme form <2>) <2> mM menadione CHEBI:28869 1.1.1.184 #6# Km depending on enzyme form <2> Y Y ECO:0000006 Pubmed:7005231 BRENDA <2> Wermuth, B.: Purification and properties of an NADPH-dependentcarbonyl reductase from human brain. Relationship to prostaglandin9-ketoreductase and xenobiotic ketone reductase. J. Biol. Chem. (1981)256, 1206-1213. {Pubmed:7005231} AAP 12/7/2011 1111 2000000462 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.13 {daunorubicin} (#6# enzyme form CR8 <2>) <2> 0.13 mM daunorubicin CHEBI:41977 1.1.1.184 #6# enzyme form CR8 <2> Y Y ECO:0000006 Pubmed:7005231 BRENDA <2> Wermuth, B.: Purification and properties of an NADPH-dependentcarbonyl reductase from human brain. Relationship to prostaglandin9-ketoreductase and xenobiotic ketone reductase. J. Biol. Chem. (1981)256, 1206-1213. {Pubmed:7005231} AAP 12/7/2011 1111 2000000463 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.015-0.017 {ubiquinone-1} (#6# Km depending on enzyme form <2>) <2> mM ubiquinone-1 CHEBI:46234 1.1.1.184 #6# Km depending on enzyme form <2> Y Y ECO:0000006 Pubmed:7005231 BRENDA <2> Wermuth, B.: Purification and properties of an NADPH-dependentcarbonyl reductase from human brain. Relationship to prostaglandin9-ketoreductase and xenobiotic ketone reductase. J. Biol. Chem. (1981)256, 1206-1213. {Pubmed:7005231} AAP 12/7/2011 1111 2000000464 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1.6-2 {4-Nitrobenzaldehyde} (#6# Km depending on enzyme form <2>) <2> mM 4-Nitrobenzaldehyde CHEBI:66926 1.1.1.184 #6# Km depending on enzyme form <2> Y Y ECO:0000006 Pubmed:7005231 BRENDA <2> Wermuth, B.: Purification and properties of an NADPH-dependentcarbonyl reductase from human brain. Relationship to prostaglandin9-ketoreductase and xenobiotic ketone reductase. J. Biol. Chem. (1981)256, 1206-1213. {Pubmed:7005231} AAP 12/7/2011 1111 2000000465 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 4-5 {Phenylglyoxal} (#6# Km depending on enzyme form <2>) <2> mM Phenylglyoxal 1.1.1.184 #6# Km depending on enzyme form <2> Y Y ECO:0000006 Pubmed:7005231 BRENDA <2> Wermuth, B.: Purification and properties of an NADPH-dependentcarbonyl reductase from human brain. Relationship to prostaglandin9-ketoreductase and xenobiotic ketone reductase. J. Biol. Chem. (1981)256, 1206-1213. {Pubmed:7005231}; PENTACON Notes: Request ChEBI ID: Phenylglyoxal, Puchem ID: CID 14090 AAP 12/7/2011 1111 2000000466 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #6# 0.1 {FAD} (#6# enzyme form CR8 <2>) <2> 0.1 mM FAD CHEBI:16238 4-nitrobenzaldehyde CHEBI:66926 Y Y ECO:0000006 Pubmed:7005231 PENTACON Added by PENTACON AAP 2000000467 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #6# 0.2 {dicoumarol} (#6# enzyme form CR8 <2>) <2> 0.2 mM dicoumarol CHEBI:4513 4-nitrobenzaldehyde CHEBI:66926 Y Y ECO:0000006 Pubmed:7005231 PENTACON Added by PENTACON AAP 2000000468 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #6# 0.005 {cibacron blue} (#6# enzyme form CR8 <2>) <2> 0.005 mM CIBACRON BLUE CHEBI:47301 4-nitrobenzaldehyde CHEBI:66926 Y Y ECO:0000006 Pubmed:7005231 PENTACON Added by PENTACON AAP 2000000469 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #6# 0.1 {indometacin} (#6# enzyme form CR8 <2>) <2> 0.1 mM indometacin CHEBI:49662 4-nitrobenzaldehyde CHEBI:66926 Y Y ECO:0000006 Pubmed:7005231 PENTACON Added by PENTACON AAP 2000000470 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 #6# 1 {iodoacetic acid} (#6# enzyme form CR8 <2>) <2> 1 mM iodoacetic acid CHEBI:74571 4-nitrobenzaldehyde CHEBI:66926 Y Y ECO:0000006 Pubmed:7005231 PENTACON Added by PENTACON AAP 2000000471 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #6# 1.7 {prostaglandin E1} (#6# enzyme form CR8 <2>) <2> 1.7 nmol/min/mg prostaglandin E1 CHEBI:15544 Y Y ECO:0000006 Pubmed:7005231 PENTACON Added by PENTACON AAP 2000000472 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #6# 25 {daunorubicin} (#6# enzyme form CR8 <2>) <2> 25 nmol/min/mg daunorubicin CHEBI:41977 Y Y ECO:0000006 Pubmed:7005231 PENTACON Added by PENTACON AAP 2000000473 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4,17# 42.9 {D-galactose} (#4# recombinant from E. coli <25>) <20,25> 42.9 mM D-galactose CHEBI:12936 1.1.1.21 #4# recombinant from E. coli <25> Y Y ECO:0000006 Pubmed:7484387 BRENDA <25> Sato, S.; Old, S.; Carper, D.; Kador, P.F.: Purification andcharacterization of recombinant human placental and rat lens aldosereductases expressed in Escherichia coli. Enzymol. Mol. Biol. CarbonylMetab. (1995) 5, 259-268. {Pubmed:7484387} AAP 12/7/2011 1111 2000000474 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 46.7 {D-galactose} <25> 46.7 mM D-galactose CHEBI:12936 1.1.1.21 Y Y ECO:0000006 Pubmed:7484387 BRENDA <25> Sato, S.; Old, S.; Carper, D.; Kador, P.F.: Purification andcharacterization of recombinant human placental and rat lens aldosereductases expressed in Escherichia coli. Enzymol. Mol. Biol. CarbonylMetab. (1995) 5, 259-268. {Pubmed:7484387} AAP 12/7/2011 1111 2000000475 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 4.8 {D-glucuronate} <25> 4.8 mM D-glucuronate CHEBI:15748 1.1.1.21 Y Y ECO:0000006 Pubmed:7484387 BRENDA <25> Sato, S.; Old, S.; Carper, D.; Kador, P.F.: Purification andcharacterization of recombinant human placental and rat lens aldosereductases expressed in Escherichia coli. Enzymol. Mol. Biol. CarbonylMetab. (1995) 5, 259-268. {Pubmed:7484387} AAP 12/7/2011 1111 2000000476 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 6.4 {D-glucuronate} (#4# recombinant from E. coli <25>) <25> 6.4 mM D-glucuronate CHEBI:15748 1.1.1.21 #4# recombinant from E. coli <25> Y Y ECO:0000006 Pubmed:7484387 BRENDA <25> Sato, S.; Old, S.; Carper, D.; Kador, P.F.: Purification andcharacterization of recombinant human placental and rat lens aldosereductases expressed in Escherichia coli. Enzymol. Mol. Biol. CarbonylMetab. (1995) 5, 259-268. {Pubmed:7484387} AAP 12/7/2011 1111 2000000477 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 86.8 {D-glucose} <25> 86.8 mM D-glucose CHEBI:17634 1.1.1.21 Y Y ECO:0000006 Pubmed:7484387 BRENDA <25> Sato, S.; Old, S.; Carper, D.; Kador, P.F.: Purification andcharacterization of recombinant human placental and rat lens aldosereductases expressed in Escherichia coli. Enzymol. Mol. Biol. CarbonylMetab. (1995) 5, 259-268. {Pubmed:7484387} AAP 12/7/2011 1111 2000000478 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 98.1 {D-glucose} (#4# recombinant from E. coli <25>; #4#recombinant from baculovirus system in Spodoptera frugiperda cells<26>) <25,26> 98.1 mM D-glucose CHEBI:17634 1.1.1.21 #4# recombinant from E. coli <25>; #4#recombinant from baculovirus system in Spodoptera frugiperda cells<26> Y Y ECO:0000006 Pubmed:7484387 BRENDA <25> Sato, S.; Old, S.; Carper, D.; Kador, P.F.: Purification andcharacterization of recombinant human placental and rat lens aldosereductases expressed in Escherichia coli. Enzymol. Mol. Biol. CarbonylMetab. (1995) 5, 259-268. {Pubmed:7484387} AAP 12/7/2011 1111 2000000479 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.046 {DL-glyceraldehyde} <25> 0.046 mM glyceraldehyde CHEBI:5445 1.1.1.21 Y Y ECO:0000006 Pubmed:7484387 BRENDA <25> Sato, S.; Old, S.; Carper, D.; Kador, P.F.: Purification andcharacterization of recombinant human placental and rat lens aldosereductases expressed in Escherichia coli. Enzymol. Mol. Biol. CarbonylMetab. (1995) 5, 259-268. {Pubmed:7484387} AAP 12/7/2011 1111 2000000480 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.047 {DL-glyceraldehyde} (#4# recombinant from E. coli <25>) <25> 0.047 mM glyceraldehyde CHEBI:5445 1.1.1.21 #4# recombinant from E. coli <25> Y Y ECO:0000006 Pubmed:7484387 BRENDA <25> Sato, S.; Old, S.; Carper, D.; Kador, P.F.: Purification andcharacterization of recombinant human placental and rat lens aldosereductases expressed in Escherichia coli. Enzymol. Mol. Biol. CarbonylMetab. (1995) 5, 259-268. {Pubmed:7484387} AAP 12/7/2011 1111 2000000481 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 8.2 {D-xylose} <25> 8.2 mM D-xylose CHEBI:65327 1.1.1.21 Y Y ECO:0000006 Pubmed:7484387 BRENDA <25> Sato, S.; Old, S.; Carper, D.; Kador, P.F.: Purification andcharacterization of recombinant human placental and rat lens aldosereductases expressed in Escherichia coli. Enzymol. Mol. Biol. CarbonylMetab. (1995) 5, 259-268. {Pubmed:7484387} AAP 12/7/2011 1111 2000000482 Chandra P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 8.7 {D-xylose} (#4# recombinant from E. coli <25>) <25> 8.7 mM D-xylose CHEBI:65327 1.1.1.21 #4# recombinant from E. coli <25> Y Y ECO:0000006 Pubmed:7484387 BRENDA <25> Sato, S.; Old, S.; Carper, D.; Kador, P.F.: Purification andcharacterization of recombinant human placental and rat lens aldosereductases expressed in Escherichia coli. Enzymol. Mol. Biol. CarbonylMetab. (1995) 5, 259-268. {Pubmed:7484387} AAP 12/7/2011 1111 2000000483 Chandra P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0045 {arachidonic acid} (#3# isozyme 1 <34>) <34> 0.0045 mM arachidonic acid CHEBI:15843 1.14.99.1 #3# isozyme 1 <34> Y Y ECO:0000006 Pubmed:7947975 BRENDA <34> Barnett, J.; Chow, J.; Ives, D.; Chiou, M.; Mackenzie, R.; Osen,E.; Nguyen, B.; Tsing, S.; Bach, C.; Freire, J.; et al.: Purification,characterization and selective inhibition of human prostaglandin G/Hsynthase 1 and 2 expressed in the baculovirus system. Biochim. Biophys.Acta (1994) 1209, 130-139. {Pubmed:7947975} AAP 12/7/2011 1111 2000000484 Chandra P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.005 {arachidonic acid} (#3# isozyme 2 <34>) <34> 0.005 mM arachidonic acid CHEBI:15843 1.14.99.1 #3# isozyme 2 <34> Y Y ECO:0000006 Pubmed:7947975 BRENDA <34> Barnett, J.; Chow, J.; Ives, D.; Chiou, M.; Mackenzie, R.; Osen,E.; Nguyen, B.; Tsing, S.; Bach, C.; Freire, J.; et al.: Purification,characterization and selective inhibition of human prostaglandin G/Hsynthase 1 and 2 expressed in the baculovirus system. Biochim. Biophys.Acta (1994) 1209, 130-139. {Pubmed:7947975} AAP 12/7/2011 1111 2000000485 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.1 {prostaglandin E2} <23> 0.1 mM prostaglandin E2 CHEBI:15551 1.1.1.184 Y Y ECO:0000006 Pubmed:7990149 BRENDA <23> Bohren, K.M.; Wermuth, B.; Harrison, D.; Ringe, D.; Petsko, G.A.;Gabbay, K.H.: Expression, crystallization and preliminarycrystallographic analysis of human carbonyl reductase. J. Mol. Biol.(1994) 244, 659-664. {Pubmed:7990149} AAP 12/7/2011 1111 2000000486 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.1 {5alpha-androstan-17beta-ol-3-one} <23> 0.1 mM 5alpha-androstan-17beta-ol-3-one CHEBI:16330 1.1.1.184 Y Y ECO:0000006 Pubmed:7990149 BRENDA <23> Bohren, K.M.; Wermuth, B.; Harrison, D.; Ringe, D.; Petsko, G.A.;Gabbay, K.H.: Expression, crystallization and preliminarycrystallographic analysis of human carbonyl reductase. J. Mol. Biol.(1994) 244, 659-664. {Pubmed:7990149} AAP 12/7/2011 1111 2000000487 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1.8 {2,3-Butanedione} <23> 1.8 mM 2,3-Butanedione CHEBI:16583 1.1.1.184 Y Y ECO:0000006 Pubmed:7990149 BRENDA <23> Bohren, K.M.; Wermuth, B.; Harrison, D.; Ringe, D.; Petsko, G.A.;Gabbay, K.H.: Expression, crystallization and preliminarycrystallographic analysis of human carbonyl reductase. J. Mol. Biol.(1994) 244, 659-664. {Pubmed:7990149} AAP 12/7/2011 1111 2000000488 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.03 {menadione} <23> 0.03 mM menadione CHEBI:28869 1.1.1.184 Y Y ECO:0000006 Pubmed:7990149 BRENDA <23> Bohren, K.M.; Wermuth, B.; Harrison, D.; Ringe, D.; Petsko, G.A.;Gabbay, K.H.: Expression, crystallization and preliminarycrystallographic analysis of human carbonyl reductase. J. Mol. Biol.(1994) 244, 659-664. {Pubmed:7990149} AAP 12/7/2011 1111 2000000489 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.3 {daunorubicin} <23> 0.3 mM daunorubicin CHEBI:41977 1.1.1.184 Y Y ECO:0000006 Pubmed:7990149 BRENDA <23> Bohren, K.M.; Wermuth, B.; Harrison, D.; Ringe, D.; Petsko, G.A.;Gabbay, K.H.: Expression, crystallization and preliminarycrystallographic analysis of human carbonyl reductase. J. Mol. Biol.(1994) 244, 659-664. {Pubmed:7990149} AAP 12/7/2011 1111 2000000490 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1.1 {4-Nitrobenzaldehyde} <23> 1.1 mM 4-Nitrobenzaldehyde CHEBI:66926 1.1.1.184 Y Y ECO:0000006 Pubmed:7990149 BRENDA <23> Bohren, K.M.; Wermuth, B.; Harrison, D.; Ringe, D.; Petsko, G.A.;Gabbay, K.H.: Expression, crystallization and preliminarycrystallographic analysis of human carbonyl reductase. J. Mol. Biol.(1994) 244, 659-664. {Pubmed:7990149} AAP 12/7/2011 1111 2000000491 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.8 {2-Nitrobenzaldehyde} <23> 0.8 mM 2-Nitrobenzaldehyde CHEBI:66927 1.1.1.184 Y Y ECO:0000006 Pubmed:7990149 BRENDA <23> Bohren, K.M.; Wermuth, B.; Harrison, D.; Ringe, D.; Petsko, G.A.;Gabbay, K.H.: Expression, crystallization and preliminarycrystallographic analysis of human carbonyl reductase. J. Mol. Biol.(1994) 244, 659-664. {Pubmed:7990149} AAP 12/7/2011 1111 2000000492 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.3 {benzoylpyridine} <23> 0.3 mM benzoylpyridine 1.1.1.184 Y Y ECO:0000006 Pubmed:7990149 BRENDA <23> Bohren, K.M.; Wermuth, B.; Harrison, D.; Ringe, D.; Petsko, G.A.;Gabbay, K.H.: Expression, crystallization and preliminarycrystallographic analysis of human carbonyl reductase. J. Mol. Biol.(1994) 244, 659-664. {Pubmed:7990149}; PENTACON Notes: Request ChEBI ID:benzoylpyridine, Puchem ID: CID 7038 AAP 12/7/2011 1111 2000000493 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1 {Phenylglyoxal} <23> 1 mM Phenylglyoxal 1.1.1.184 Y Y ECO:0000006 Pubmed:7990149 BRENDA <23> Bohren, K.M.; Wermuth, B.; Harrison, D.; Ringe, D.; Petsko, G.A.;Gabbay, K.H.: Expression, crystallization and preliminarycrystallographic analysis of human carbonyl reductase. J. Mol. Biol.(1994) 244, 659-664. {Pubmed:7990149}; PENTACON Notes: Request ChEBI ID: Phenylglyoxal, Puchem ID: CID 14090 AAP 12/7/2011 1111 2000000494 Jenn P16152 873 CBR1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1.4 {pyridine-4-carboxaldehyde} <23> 1.4 mM pyridine-4-carboxaldehyde 1.1.1.184 Y Y ECO:0000006 Pubmed:7990149 BRENDA <23> Bohren, K.M.; Wermuth, B.; Harrison, D.; Ringe, D.; Petsko, G.A.;Gabbay, K.H.: Expression, crystallization and preliminarycrystallographic analysis of human carbonyl reductase. J. Mol. Biol.(1994) 244, 659-664. {Pubmed:7990149}; PENTACON Notes: Request ChEBI ID: pyridine-4-carboxaldehyde, Puchem ID: CID 13389 AAP 12/7/2011 1111 2000000495 Jodi P41222 5730 PTGDS Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.004 {prostaglandin H2} <14> 0.004 mM prostaglandin H2 CHEBI:15554 5.3.99.2 Y Y ECO:0000006 Pubmed:8093029 BRENDA <14> Watanabe, K.; Urade, Y.; Mäder, M.; Murphy, C.; Hayaishi, O.:Identification of beta-trace as prostaglandin D synthase. Biochem.Biophys. Res. Commun. (1994) 203, 1110-1116. {Pubmed:8093029} (c) AAP 12/7/2011 1111 2000000496 Jodi P41222 5730 PTGDS Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #4# 1000 {prostaglandin H2} <14> 1000 nmol/min/mg prostaglandin H2 CHEBI:15554 Y Y ECO:0000006 Pubmed:8093029 PENTACON Added by PENTACON AAP 2000000497 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.02 {DL-glyceraldehyde} <19> 0.02 mM glyceraldehyde CHEBI:5445 1.1.1.21 Y Y ECO:0000006 Pubmed:8117659 BRENDA <19> Bohren, K.M.; Grimshaw, C.E.; Lai, C.J.; Harrison, D.H.; Ringe,D.; Petsko, G.A.; Gabbay, K.H.: Tyrosine-48 is the proton donor andhistidine-110 directs substrate stereochemical selectivity in thereduction reaction of human aldose reductase: enzyme kinetics andcrystal structure of the Y48H mutant enzyme. Biochemistry (1994) 33,2021-2032. {Pubmed:8117659} AAP 12/7/2011 1111 2000000498 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 12 {DL-glyceraldehyde} (#4# mutant H110Q <19>) <19> 12 mM glyceraldehyde CHEBI:5445 1.1.1.21 #4# mutant H110Q <19> Y Y ECO:0000006 Pubmed:8117659 BRENDA <19> Bohren, K.M.; Grimshaw, C.E.; Lai, C.J.; Harrison, D.H.; Ringe,D.; Petsko, G.A.; Gabbay, K.H.: Tyrosine-48 is the proton donor andhistidine-110 directs substrate stereochemical selectivity in thereduction reaction of human aldose reductase: enzyme kinetics andcrystal structure of the Y48H mutant enzyme. Biochemistry (1994) 33,2021-2032. {Pubmed:8117659}; PENTACON Notes: Mutant: H110Q mutant AAP 12/7/2011 1111 2000000499 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 64 {DL-glyceraldehyde} (#4# mutant Y48S <19>) <19> 64 mM glyceraldehyde CHEBI:5445 1.1.1.21 #4# mutant Y48S <19> Y Y ECO:0000006 Pubmed:8117659 BRENDA <19> Bohren, K.M.; Grimshaw, C.E.; Lai, C.J.; Harrison, D.H.; Ringe,D.; Petsko, G.A.; Gabbay, K.H.: Tyrosine-48 is the proton donor andhistidine-110 directs substrate stereochemical selectivity in thereduction reaction of human aldose reductase: enzyme kinetics andcrystal structure of the Y48H mutant enzyme. Biochemistry (1994) 33,2021-2032. {Pubmed:8117659}; PENTACON Notes: Mutant: Y48S mutant AAP 12/7/2011 1111 2000000500 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 71 {DL-glyceraldehyde} (#4# mutant Y48H <19>) <19> 71 mM glyceraldehyde CHEBI:5445 1.1.1.21 #4# mutant Y48H <19> Y Y ECO:0000006 Pubmed:8117659 BRENDA <19> Bohren, K.M.; Grimshaw, C.E.; Lai, C.J.; Harrison, D.H.; Ringe,D.; Petsko, G.A.; Gabbay, K.H.: Tyrosine-48 is the proton donor andhistidine-110 directs substrate stereochemical selectivity in thereduction reaction of human aldose reductase: enzyme kinetics andcrystal structure of the Y48H mutant enzyme. Biochemistry (1994) 33,2021-2032. {Pubmed:8117659}; PENTACON Notes: Mutant: Y48H mutant AAP 12/7/2011 1111 2000000501 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 84 {DL-glyceraldehyde} (#4# mutant H110A <19>) <19> 84 mM glyceraldehyde CHEBI:5445 1.1.1.21 #4# mutant H110A <19> Y Y ECO:0000006 Pubmed:8117659 BRENDA <19> Bohren, K.M.; Grimshaw, C.E.; Lai, C.J.; Harrison, D.H.; Ringe,D.; Petsko, G.A.; Gabbay, K.H.: Tyrosine-48 is the proton donor andhistidine-110 directs substrate stereochemical selectivity in thereduction reaction of human aldose reductase: enzyme kinetics andcrystal structure of the Y48H mutant enzyme. Biochemistry (1994) 33,2021-2032. {Pubmed:8117659}; PENTACON Notes: Mutant: H110A mutant AAP 12/7/2011 1111 2000000502 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 506 {D-Lyxose} (#4# mutant H110Q <19>) <19> 506 mM D-Lyxose CHEBI:62318 1.1.1.21 #4# mutant H110Q <19> Y Y ECO:0000006 Pubmed:8117659 BRENDA <19> Bohren, K.M.; Grimshaw, C.E.; Lai, C.J.; Harrison, D.H.; Ringe,D.; Petsko, G.A.; Gabbay, K.H.: Tyrosine-48 is the proton donor andhistidine-110 directs substrate stereochemical selectivity in thereduction reaction of human aldose reductase: enzyme kinetics andcrystal structure of the Y48H mutant enzyme. Biochemistry (1994) 33,2021-2032. {Pubmed:8117659}; PENTACON Notes: Mutant: H110Q mutant AAP 12/7/2011 1111 2000000503 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 2630 {D-Lyxose} <19> 2630 mM D-Lyxose CHEBI:62318 1.1.1.21 Y Y ECO:0000006 Pubmed:8117659 BRENDA <19> Bohren, K.M.; Grimshaw, C.E.; Lai, C.J.; Harrison, D.H.; Ringe,D.; Petsko, G.A.; Gabbay, K.H.: Tyrosine-48 is the proton donor andhistidine-110 directs substrate stereochemical selectivity in thereduction reaction of human aldose reductase: enzyme kinetics andcrystal structure of the Y48H mutant enzyme. Biochemistry (1994) 33,2021-2032. {Pubmed:8117659} AAP 12/7/2011 1111 2000000504 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 2740 {D-Lyxose} (#4# mutant H110A <19>) <19> 2740 mM D-Lyxose CHEBI:62318 1.1.1.21 #4# mutant H110A <19> Y Y ECO:0000006 Pubmed:8117659 BRENDA <19> Bohren, K.M.; Grimshaw, C.E.; Lai, C.J.; Harrison, D.H.; Ringe,D.; Petsko, G.A.; Gabbay, K.H.: Tyrosine-48 is the proton donor andhistidine-110 directs substrate stereochemical selectivity in thereduction reaction of human aldose reductase: enzyme kinetics andcrystal structure of the Y48H mutant enzyme. Biochemistry (1994) 33,2021-2032. {Pubmed:8117659}; PENTACON Notes: Mutant: H110A mutant AAP 12/7/2011 1111 2000000505 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 7.4 {D-xylose} <19> 7.4 mM D-xylose CHEBI:65327 1.1.1.21 Y Y ECO:0000006 Pubmed:8117659 BRENDA <19> Bohren, K.M.; Grimshaw, C.E.; Lai, C.J.; Harrison, D.H.; Ringe,D.; Petsko, G.A.; Gabbay, K.H.: Tyrosine-48 is the proton donor andhistidine-110 directs substrate stereochemical selectivity in thereduction reaction of human aldose reductase: enzyme kinetics andcrystal structure of the Y48H mutant enzyme. Biochemistry (1994) 33,2021-2032. {Pubmed:8117659} AAP 12/7/2011 1111 2000000506 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 861 {D-xylose} (#4# mutant H110Q <19>) <19> 861 mM D-xylose CHEBI:65327 1.1.1.21 #4# mutant H110Q <19> Y Y ECO:0000006 Pubmed:8117659 BRENDA <19> Bohren, K.M.; Grimshaw, C.E.; Lai, C.J.; Harrison, D.H.; Ringe,D.; Petsko, G.A.; Gabbay, K.H.: Tyrosine-48 is the proton donor andhistidine-110 directs substrate stereochemical selectivity in thereduction reaction of human aldose reductase: enzyme kinetics andcrystal structure of the Y48H mutant enzyme. Biochemistry (1994) 33,2021-2032. {Pubmed:8117659}; PENTACON Notes: Mutant: H110Q mutant AAP 12/7/2011 1111 2000000507 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 1340 {D-xylose} (#4# mutant H110A <19>) <19> 1340 mM D-xylose CHEBI:65327 1.1.1.21 #4# mutant H110A <19> Y Y ECO:0000006 Pubmed:8117659 BRENDA <19> Bohren, K.M.; Grimshaw, C.E.; Lai, C.J.; Harrison, D.H.; Ringe,D.; Petsko, G.A.; Gabbay, K.H.: Tyrosine-48 is the proton donor andhistidine-110 directs substrate stereochemical selectivity in thereduction reaction of human aldose reductase: enzyme kinetics andcrystal structure of the Y48H mutant enzyme. Biochemistry (1994) 33,2021-2032. {Pubmed:8117659}; PENTACON Notes: Mutant: H110A mutant AAP 12/7/2011 1111 2000000508 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 111 {L-Xylose} <19> 111 mM L-Xylose CHEBI:65328 1.1.1.21 Y Y ECO:0000006 Pubmed:8117659 BRENDA <19> Bohren, K.M.; Grimshaw, C.E.; Lai, C.J.; Harrison, D.H.; Ringe,D.; Petsko, G.A.; Gabbay, K.H.: Tyrosine-48 is the proton donor andhistidine-110 directs substrate stereochemical selectivity in thereduction reaction of human aldose reductase: enzyme kinetics andcrystal structure of the Y48H mutant enzyme. Biochemistry (1994) 33,2021-2032. {Pubmed:8117659} AAP 12/7/2011 1111 2000000509 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 360 {L-Xylose} (#4# mutant H110A <19>) <19> 360 mM L-Xylose CHEBI:65328 1.1.1.21 #4# mutant H110A <19> Y Y ECO:0000006 Pubmed:8117659 BRENDA <19> Bohren, K.M.; Grimshaw, C.E.; Lai, C.J.; Harrison, D.H.; Ringe,D.; Petsko, G.A.; Gabbay, K.H.: Tyrosine-48 is the proton donor andhistidine-110 directs substrate stereochemical selectivity in thereduction reaction of human aldose reductase: enzyme kinetics andcrystal structure of the Y48H mutant enzyme. Biochemistry (1994) 33,2021-2032. {Pubmed:8117659}; PENTACON Notes: Mutant: H110A mutant AAP 12/7/2011 1111 2000000510 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 1190 {L-Xylose} (#4# mutant H110Q <19>) <19> 1190 mM L-Xylose CHEBI:65328 1.1.1.21 #4# mutant H110Q <19> Y Y ECO:0000006 Pubmed:8117659 BRENDA <19> Bohren, K.M.; Grimshaw, C.E.; Lai, C.J.; Harrison, D.H.; Ringe,D.; Petsko, G.A.; Gabbay, K.H.: Tyrosine-48 is the proton donor andhistidine-110 directs substrate stereochemical selectivity in thereduction reaction of human aldose reductase: enzyme kinetics andcrystal structure of the Y48H mutant enzyme. Biochemistry (1994) 33,2021-2032. {Pubmed:8117659}; PENTACON Notes: Mutant: H110Q mutant AAP 12/7/2011 1111 2000000511 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM .004 {4-nitrobenzaldehyde} 0.004 mM 4-nitrobenzaldehyde CHEBI:66926 Y Y ECO:0000006 Pubmed:8117659 PENTACON Added by PENTACON AAP 2000000512 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM .1 {4-nitrobenzaldehyde} mutant Y48H 0.1 mM 4-nitrobenzaldehyde CHEBI:66926 Y Y ECO:0000006 Pubmed:8117659 PENTACON Added by PENTACON; PENTACON Notes: Mutant: Y48H mutant AAP 2000000513 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM .19 {4-nitrobenzaldehyde} mutant H110A 0.19 mM 4-nitrobenzaldehyde CHEBI:66926 Y Y ECO:0000006 Pubmed:8117659 PENTACON Added by PENTACON; PENTACON Notes: Mutant: H110A mutant AAP 2000000514 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM .86 {4-nitrobenzaldehyde} mutant H110Q 0.86 mM 4-nitrobenzaldehyde CHEBI:66926 Y Y ECO:0000006 Pubmed:8117659 PENTACON Added by PENTACON; PENTACON Notes: Mutant: H110Q mutant AAP 2000000515 Christie P15121 231 AKR1B1 Homo sapiens 9606 Comment/biophysicochemical properties/KM .88 {4-nitrobenzaldehyde} mutant Y48S 0.88 mM 4-nitrobenzaldehyde CHEBI:66926 Y Y ECO:0000006 Pubmed:8117659 PENTACON Added by PENTACON; PENTACON Notes: Mutant: Y48S mutant AAP 2000000516 Chandra P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.001 {arachidonic acid} (#3# isozyme 1 and 2 <28>) <28> 0.001 mM arachidonic acid CHEBI:15843 1.14.99.1 #3# isozyme 1 and 2 <28> Y Y ECO:0000006 Pubmed:8831731 BRENDA <28> Kargman, S.; Wong, E.; Greig, G.M.; Falgueyret, J.P.; Cromlish,W.; Ethier, D.; Yergey, J.A.; Riendeau, D.; Evans, J.F.; Kennedy, B.;Tagari, P.; Francis, D.A.; O'Neill, G.P.: Mechanism of selectiveinhibition of human prostaglandin G/H synthase-1 and -2 in intactcells. Biochem. Pharmacol. (1996) 52, 1113-1125. {Pubmed:8831731} AAP 12/7/2011 1111 2000000517 Chandra P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.001 {arachidonic acid} (#3# isozyme 1 and 2 <28>) <28> 0.001 mM arachidonic acid CHEBI:15843 1.14.99.1 #3# isozyme 1 and 2 <28> Y Y ECO:0000006 Pubmed:8831731 BRENDA <28> Kargman, S.; Wong, E.; Greig, G.M.; Falgueyret, J.P.; Cromlish,W.; Ethier, D.; Yergey, J.A.; Riendeau, D.; Evans, J.F.; Kennedy, B.;Tagari, P.; Francis, D.A.; O'Neill, G.P.: Mechanism of selectiveinhibition of human prostaglandin G/H synthase-1 and -2 in intactcells. Biochem. Pharmacol. (1996) 52, 1113-1125. {Pubmed:8831731} AAP 12/7/2011 1111 2000000518 Chandra P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.0074 {arachidonic acid} 0.0074 mM arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:8831731 PENTACON Added by PENTACON AAP 2000000519 Chandra P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.015 {arachidonic acid} <31> 0.015 mM arachidonic acid CHEBI:15843 1.14.99.1 Y Y ECO:0000006 Pubmed:9172778 BRENDA <31> George, H.J.; Van Dyk, D.E.; Straney, R.A.; Trzaskos, J.M.;Copeland, R.A.: Expression purification and characterization ofrecombinant human inducible prostaglandin G/H synthase frombaculovirus-infected insect cells. Protein Expr. Purif. (1996) 7,19-26. {Pubmed:9172778} AAP 12/7/2011 1111 2000000520 Chandra P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.006 {arachidonic acid} <29> 0.006 mM arachidonic acid CHEBI:15843 1.14.99.1 Y Y ECO:0000006 Pubmed:9866686 BRENDA <29> Forghani, F.; Ouellet, M.; Keen, S.; Percival, M.D.; Tagari, P.:Analysis of prostaglandin G/H synthase-2 inhibition usingperoxidase-induced luminol luminescence. Anal. Biochem. (1998) 264,216-221. {Pubmed:9866686} AAP 12/7/2011 1111 2000000521 Jenn O15296 247 ALOX15B Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 2000 {arachidonic acid} (splice variant 15-LOb2) 2000 nmol/min/mg arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:10542053 PENTACON Added by PENTACON; PENTACON Notes: splice variant 15-LOb2 AAP 2000000522 Jenn O15296 247 ALOX15B Homo sapiens 9606 Comment/biophysicochemical properties/IC50 >1 {CDP-choline} (splice variant 15-LOb2) mM CDP-choline CHEBI:16436 arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:10542053 PENTACON Added by PENTACON; PENTACON Notes: splice variant 15-LOb2 AAP 2000000523 Jenn O15296 247 ALOX15B Homo sapiens 9606 Comment/biophysicochemical properties/IC50 >1 {nordihydroguaiaretic acid} (splice variant 15-LOb2) mM nordihydroguaiaretic acid CHEBI:7625 arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:10542053 PENTACON Added by PENTACON; PENTACON Notes: splice variant 15-LOb2 AAP 2000000524 Jenn O15296 247 ALOX15B Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 4000 {arachidonic acid} (splice variant 15-LOb1) 4000 nmol/min/mg arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:10542053 PENTACON Added by PENTACON; PENTACON Notes: splice variant 15-LOb1 AAP 2000000525 Jenn O15296 247 ALOX15B Homo sapiens 9606 Comment/biophysicochemical properties/IC50 0.0085 {CDP-choline} (splice variant 15-LOb1) 0.0085 mM CDP-choline CHEBI:16436 arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:10542053 PENTACON Added by PENTACON; PENTACON Notes: splice variant 15-LOb1 AAP 2000000526 Jenn O15296 247 ALOX15B Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 4000 {lipoic acid} (splice variant 15-LOb1) 4000 nmol/min/mg lipoic acid CHEBI:16494 Y Y ECO:0000006 Pubmed:10542053 PENTACON Added by PENTACON; PENTACON Notes: splice variant 15-LOb1 AAP 2000000527 Jenn O15296 247 ALOX15B Homo sapiens 9606 Comment/biophysicochemical properties/IC50 0.0769 {nordihydroguaiaretic acid} (splice variant 15-LOb1) 0.0769 mM nordihydroguaiaretic acid CHEBI:7625 arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:10542053 PENTACON Added by PENTACON; PENTACON Notes: splice variant 15-LOb1 AAP 2000000528 Jenn O15296 247 ALOX15B Homo sapiens 9606 Comment/biophysicochemical properties/IC50 >1 {Eicosatetraynoic acid} (splice variant 15-LOb2) mM Eicosatetraynoic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:10542053 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: Eicosatetraynoic acid; Pubchem ID: CID 135235; splice variant 15-LOb2 AAP 2000000529 Jenn O15296 247 ALOX15B Homo sapiens 9606 Comment/biophysicochemical properties/IC50 0.180 {Eicosatetraynoic acid} (splice variant 15-LOb1) 0.18 mM Eicosatetraynoic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:10542053 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: Eicosatetraynoic acid; Pubchem ID: CID 135235; splice variant 15-LOb1 AAP 2000000530 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 .0065 {Eicosatetraynoic acid} 0.0065 mM Eicosatetraynoic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:10542053 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: Eicosatetraynoic acid; Pubchem ID: CID 135235 AAP 2000000531 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 .0033 {CDP-choline} 0.0033 mM CDP-choline CHEBI:16436 arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:10542053 PENTACON Added by PENTACON AAP 2000000532 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 .023 {nordihydroguaiaretic acid} 0.023 mM nordihydroguaiaretic acid CHEBI:7625 arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:10542053 PENTACON Added by PENTACON AAP 2000000533 Jenn O15296 247 ALOX15B Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 1.1 {arachidonic acid} (#2# splice variant 15-LOb2 <29>) <29> 1.1 mM arachidonic acid CHEBI:15843 1.13.11.33 #2# splice variant 15-LOb2 <29> Y Y ECO:0000006 Pubmed:10542053 BRENDA <29> Kilty, I.; Logan, A.; Vickers, P.J.: Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 15S-lipoxygenase. Eur. J. Biochem. (1999) 266, 83-93. {Pubmed:10542053} AAP 12/7/2011 1111 2000000534 Jenn O15296 247 ALOX15B Homo sapiens 9606 Comment/biophysicochemical properties/KM #2,10# 0.025 {arachidonic acid} (#2# splice variant 15-LOb1 <29>) <7,29> 0.025 mM arachidonic acid CHEBI:15843 1.13.11.33 #2# splice variant 15-LOb1 <29> Y Y ECO:0000006 Pubmed:10542053 BRENDA <29> Kilty, I.; Logan, A.; Vickers, P.J.: Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 15S-lipoxygenase. Eur. J. Biochem. (1999) 266, 83-93. {Pubmed:10542053} AAP 12/7/2011 1111 2000000535 Jenn O15296 247 ALOX15B Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.01 {lipoic acid} (#2# splice variant 15-LOb1 <29>) <29> 0.01 mM lipoic acid CHEBI:16494 1.13.11.33 #2# splice variant 15-LOb1 <29> Y Y ECO:0000006 Pubmed:10542053 BRENDA <29> Kilty, I.; Logan, A.; Vickers, P.J.: Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 15S-lipoxygenase. Eur. J. Biochem. (1999) 266, 83-93. {Pubmed:10542053} AAP 12/7/2011 1111 2000000536 Jenn P34913 2053 EPHX2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 40 {trans-diphenylpropene oxide} ( pH 7.4, 37°C ) 40 nmol/min/mg trans-diphenylpropene oxide Y Y ECO:0000006 Pubmed:10568695 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: trans-diphenylpropene oxide; pH 7.4, 37°C AAP 2000000537 Jenn P34913 2053 EPHX2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.0081 {trans-diphenylpropene oxide} (#6# pH 7.4, 37°C <66>) <66> 0.0081 mM trans-diphenylpropene oxide 3.3.2.10 #6# pH 7.4, 37°C <66> Y Y ECO:0000006 Pubmed:10568695 BRENDA <66> Draper, A.J.; Hammock, B.D.: Inhibition of soluble and microsomal epoxide hydrolase by zinc and other metals. Toxicol. Sci. (1999) 52, 26-32. {Pubmed:10568695}; PENTACON NOTES: Request ChEBI ID: trans-diphenylpropene oxide AAP 12/7/2011 1111 2000000538 Jenn P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/IC50 0.00002 {thioamine} ( pH 7.5, 22°C) 0.00002 mM thioamine leucine-4-nitroanilide Y Y ECO:0000006 Pubmed:10574934 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: thioamine; pH 7.5, 22°C AAP 2000000539 Jenn P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 310 {leucine-4-nitroanilide} ( pH 7.5, 22°C) 310 nmol/min/mg leucine-4-nitroanilide Y Y ECO:0000006 Pubmed:10574934 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: leucine-4-nitroanilide; pH 7.5, 22°C AAP 2000000540 Jenn P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/IC50 0.0005 {bestatin} ( pH 7.5, 22°C) 0.0005 mM bestatin leucine-4-nitroanilide Y Y ECO:0000006 Pubmed:10574934 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: bestatin, Chembl ID: CHEMBL29292; pH 7.5, 22°C AAP 2000000541 Jenn P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/IC50 0.00003 {hydroxamic acid} ( pH 7.5, 22°C) 0.00003 mM hydroxamic acid CHEBI:24650 leucine-4-nitroanilide Y Y ECO:0000006 Pubmed:10574934 PENTACON Added by PENTACON; PENTACON Notes: pH 7.5, 22°C AAP 2000000542 Jenn P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.15 {leucine-4-nitroanilide} (#4# pH 7.5, 22°C <32>) <32> 0.15 mM leucine-4-nitroanilide 3.3.2.6 #4# pH 7.5, 22°C <32> Y Y ECO:0000006 Pubmed:10574934 BRENDA <32> Kull, F.; Ohlson, E.; Haeggstrom, J.Z.: Cloning and characterization of a bifunctional leukotriene A4 hydrolase from Saccharomyces cerevisiae. J. Biol. Chem. (1999) 274, 34683-34690. {Pubmed:10574934}; PENTACON Notes: Request ChEBI ID: leucine-4-nitroanilide AAP 12/7/2011 1111 2000000543 Jenn O00154 11332 ACOT7 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 270000 {arachidoyl-CoA} (#41# pH 7.4, 30°C <52>) <52> 270000 nmol/min/mg icosanoyl-CoA CHEBI:15527 Y Y ECO:0000006 Pubmed:10578051 PENTACON Added by PENTACON; PENTACON Notes: pH 7.4, 30°C AAP 2000000544 Jenn O00154 11332 ACOT7 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 295000 {Dodecanoyl-CoA} (#41# pH 7.4, 30°C <52>) <52> 295000 nmol/min/mg lauroyl-CoA CHEBI:15521 Y Y ECO:0000006 Pubmed:10578051 PENTACON Added by PENTACON; PENTACON Notes: pH 7.4, 30°C AAP 2000000545 Jenn O00154 11332 ACOT7 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 269000 {Octanoyl-CoA} (pH 7.4, 30°C) 269000 nmol/min/mg Octanoyl-CoA CHEBI:15533 Y Y ECO:0000006 Pubmed:10578051 PENTACON Added by PENTACON; PENTACON Notes: pH 7.4, 30°C AAP 2000000546 Jenn O00154 11332 ACOT7 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 50000 {oleoyl-CoA} (#41# pH 7.4, 30°C <52>) <52> 50000 nmol/min/mg oleoyl-CoA CHEBI:15534 Y Y ECO:0000006 Pubmed:10578051 PENTACON Added by PENTACON; PENTACON Notes: pH 7.4, 30°C AAP 2000000547 Jenn O00154 11332 ACOT7 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 275000 {hexadecanoyl-CoA} (#41# pH 7.4, 30°C <52>) <52> 275000 nmol/min/mg palmitoyl-CoA CHEBI:15525 Y Y ECO:0000006 Pubmed:10578051 PENTACON Added by PENTACON; PENTACON Notes: pH 7.4, 30°C AAP 2000000548 Jenn O00154 11332 ACOT7 Homo sapiens 9606 Comment/biophysicochemical properties/KM #41# 0.0092 {arachidoyl-CoA} (#41# pH 7.4, 30°C <52>) <52> 0.0092 mM icosanoyl-CoA CHEBI:15527 3.1.2.2 #41# pH 7.4, 30°C <52> Y Y ECO:0000006 Pubmed:10578051 BRENDA <52> Yamada, J.; Kurata, A.; Hirata, M.; Taniguchi, T.; Takama, H.; Furihata, T.; Shiratori, K.; Iida, N.; Takagi-Sakuma, M.; Watanabe, T.; Kurosaki, K.; Endo, T.; Suga, T.: Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase. J. Biochem. (1999) 126, 1013-1019. {Pubmed:10578051} AAP 12/7/2011 1111 2000000549 Jenn O00154 11332 ACOT7 Homo sapiens 9606 Comment/biophysicochemical properties/KM #41# 0.0076 {Dodecanoyl-CoA} (#41# pH 7.4, 30°C <52>) <52> 0.0076 mM lauroyl-CoA CHEBI:15521 3.1.2.2 #41# pH 7.4, 30°C <52> Y Y ECO:0000006 Pubmed:10578051 BRENDA <52> Yamada, J.; Kurata, A.; Hirata, M.; Taniguchi, T.; Takama, H.; Furihata, T.; Shiratori, K.; Iida, N.; Takagi-Sakuma, M.; Watanabe, T.; Kurosaki, K.; Endo, T.; Suga, T.: Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase. J. Biochem. (1999) 126, 1013-1019. {Pubmed:10578051} AAP 12/7/2011 1111 2000000550 Jenn O00154 11332 ACOT7 Homo sapiens 9606 Comment/biophysicochemical properties/KM #41# 0.014 {Octanoyl-CoA} (#41# pH 7.4, 30°C <52>) <52> 0.014 mM Octanoyl-CoA CHEBI:15533 3.1.2.2 #41# pH 7.4, 30°C <52> Y Y ECO:0000006 Pubmed:10578051 BRENDA <52> Yamada, J.; Kurata, A.; Hirata, M.; Taniguchi, T.; Takama, H.; Furihata, T.; Shiratori, K.; Iida, N.; Takagi-Sakuma, M.; Watanabe, T.; Kurosaki, K.; Endo, T.; Suga, T.: Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase. J. Biochem. (1999) 126, 1013-1019. {Pubmed:10578051} AAP 12/7/2011 1111 2000000551 Jenn O00154 11332 ACOT7 Homo sapiens 9606 Comment/biophysicochemical properties/KM #41# 0.0088 {oleoyl-CoA} (#41# pH 7.4, 30°C <52>) <52> 0.0088 mM oleoyl-CoA CHEBI:15534 3.1.2.2 #41# pH 7.4, 30°C <52> Y Y ECO:0000006 Pubmed:10578051 BRENDA <52> Yamada, J.; Kurata, A.; Hirata, M.; Taniguchi, T.; Takama, H.; Furihata, T.; Shiratori, K.; Iida, N.; Takagi-Sakuma, M.; Watanabe, T.; Kurosaki, K.; Endo, T.; Suga, T.: Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase. J. Biochem. (1999) 126, 1013-1019. {Pubmed:10578051} AAP 12/7/2011 1111 2000000552 Jenn O00154 11332 ACOT7 Homo sapiens 9606 Comment/biophysicochemical properties/KM #41# 0.0064 {hexadecanoyl-CoA} (#41# pH 7.4, 30°C <52>) <52> 0.0064 mM palmitoyl-CoA CHEBI:15525 3.1.2.2 #41# pH 7.4, 30°C <52> Y Y ECO:0000006 Pubmed:10578051 BRENDA <52> Yamada, J.; Kurata, A.; Hirata, M.; Taniguchi, T.; Takama, H.; Furihata, T.; Shiratori, K.; Iida, N.; Takagi-Sakuma, M.; Watanabe, T.; Kurosaki, K.; Endo, T.; Suga, T.: Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase. J. Biochem. (1999) 126, 1013-1019. {Pubmed:10578051} AAP 12/7/2011 1111 2000000553 Christie Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0099 {leukotriene A4} <3> 0.0099 mM leukotriene A4 CHEBI:15651 4.4.1.20 Y Y ECO:0000033 Pubmed:10591082 BRENDA <3> Penrose, J.F.; Austen, K.F.: The biochemical, molecular, and genomic aspects of leukotriene C4 synthase. Proc. Assoc. Am. Phys. (1999) 111, 537-546. {Pubmed:} (c) AAP 12/7/2011 1111 2000000554 Jenn P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 25.9 {cholesterol} (#3# recombinant enzyme expressed in hepatic Mc-7777 cells <39>) <39> 25.9 nmol/min/mg cholesterol CHEBI:16113 Y Y ECO:0000006 Pubmed:10685026 PENTACON Added by PENTACON AAP 2000000555 Jenn P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 27.6 {cholesterol} (#3# recombinant enzyme expressed in baby hamster kidney cells <39>) <39> 27.6 nmol/min/mg cholesterol CHEBI:16113 Y Y ECO:0000006 Pubmed:10685026 PENTACON Added by PENTACON AAP 2000000556 Jenn P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.00083 {cholesterol} (#3# recombinant enzyme expressed in hepatic Mc-7777 cells <39>) <39> 0.00083 mM cholesterol CHEBI:16113 2.3.1.43 #3# recombinant enzyme expressed in hepatic Mc-7777 cells <39> Y Y ECO:0000006 Pubmed:10685026 BRENDA <39> Ayyobi, A.F.; Lacko, A.G.; Murray, K.; Nair, M.; Li, M.; Molhuizen, H.O.F.; Pritchard, P.H.: Biochemical and compositional analyses of recombinant lecithin:cholesterol acyltransferase (LCAT) obtained from a hepatic source. Biochim. Biophys. Acta (2000) 1484, 1-13. {Pubmed:10685026} AAP 12/7/2011 1111 2000000557 Jenn P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.00057 {cholesterol} (#3# recombinant enzyme expressed in baby hamster kidney cells <39>) <39> 0.00057 mM cholesterol CHEBI:16113 2.3.1.43 #3# recombinant enzyme expressed in baby hamster kidney cells <39> Y Y ECO:0000006 Pubmed:10685026 BRENDA <39> Ayyobi, A.F.; Lacko, A.G.; Murray, K.; Nair, M.; Li, M.; Molhuizen, H.O.F.; Pritchard, P.H.: Biochemical and compositional analyses of recombinant lecithin:cholesterol acyltransferase (LCAT) obtained from a hepatic source. Biochim. Biophys. Acta (2000) 1484, 1-13. {Pubmed:10685026} AAP 12/7/2011 1111 2000000558 Jenn P34913 2053 EPHX2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.0062 {2,3-epoxy-1,3-diphenyl-propane} (#6# 30°C <23>) <23> 0.0062 mM 2,3-epoxy-1,3-diphenyl-propane 3.3.2.10 #6# 30°C <23> Y Y ECO:0000006 Pubmed:10860549 BRENDA <23> Morisseau, C.; Beetham, J.K.; Pinot, F.; Debernard, S.; Newman, J.W.; Hammock, B.D.: Cress and potato soluble epoxide hydrolases: purification, biochemical characterization, and comparison to mammalian enzymes. Arch. Biochem. Biophys. (2000) 378, 321-332. {Pubmed:10860549} (c) AAP 12/7/2011 1111 2000000559 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM .0051 {PGE2-ester} 0.0051 mM prostaglandin E2 methyl ester Y Y ECO:0000006 Pubmed:11422365 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: prostaglandin E2 methyl ester; Pubchem CID 6434107 AAP 2000000560 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 13480 {PGE2-ester} 13480 nmol/min/mg prostaglandin E2 methyl ester Y Y ECO:0000006 Pubmed:11422365 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: prostaglandin E2 methyl ester; Pubchem CID 6434107 AAP 2000000561 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM .0456 {NAD+} 0.0456 mM NAD(+) CHEBI:15846 Y Y ECO:0000006 Pubmed:11422365 PENTACON Added by PENTACON AAP 2000000562 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM .0384 {NAD+} 0.0384 mM NAD(+) CHEBI:15846 Y Y ECO:0000006 Pubmed:11422365 PENTACON Added by PENTACON AAP 2000000563 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 19200 {NAD+} 19200 nmol/min/mg NAD(+) CHEBI:15846 Y Y ECO:0000006 Pubmed:11422365 PENTACON Added by PENTACON AAP 2000000564 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 21300 {NAD+} 21300 nmol/min/mg NAD(+) CHEBI:15846 Y Y ECO:0000006 Pubmed:11422365 PENTACON Added by PENTACON AAP 2000000565 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM .0039 {PGE2} 0.0039 mM prostaglandin E2 CHEBI:15551 Y Y ECO:0000006 Pubmed:11422365 PENTACON Added by PENTACON AAP 2000000566 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM .0043 {PGE2} 0.0043 mM prostaglandin E2 CHEBI:15551 Y Y ECO:0000006 Pubmed:11422365 PENTACON Added by PENTACON AAP 2000000567 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 18600 {PGE2} 18600 nmol/min/mg prostaglandin E2 CHEBI:15551 Y Y ECO:0000006 Pubmed:11422365 PENTACON Added by PENTACON AAP 2000000568 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 20450 {PGE2} 20450 nmol/min/mg prostaglandin E2 CHEBI:15551 Y Y ECO:0000006 Pubmed:11422365 PENTACON Added by PENTACON AAP 2000000569 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM 2.3-3.8 {alanine-p-nitroanilide} mM alanine-4-nitroanilide Y Y ECO:0000006 Pubmed:11675384 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: alanine-4-nitroanilide; Pubchem CID 150936 AAP 2000000570 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.006-0.028 {leukotriene A4} (#4# pH 8.0, wild-type enzyme in comparison to mutant enzymes <36,37>) <36,37> mM leukotriene A4 CHEBI:15651 3.3.2.6 #4# pH 8.0, wild-type enzyme in comparison to mutant enzymes <36,37> Y Y ECO:0000006 Pubmed:11675384 BRENDA <36> Rudberg, P.C.; Tholander, F.; Thunnissen, M.M.; Haeggstrom, J.Z.: Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms. J. Biol. Chem. (2002) 277, 1398-1404. {Pubmed:11675384} AAP 12/7/2011 1111 2000000571 Christie P35610 6646 SOAT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM .0147 {oleoyl-CoA} (mutant C92A/C333A/C345A/C365A/C467A/C516A/C546A) 0.0147 mM oleoyl-CoA CHEBI:15534 Y Y ECO:0000006 Pubmed:11684695 PENTACON Added by PENTACON; PENTACON Notes: Mutant: C92A/C333A/C345A/C365A/C467A/C516A/C546A AAP 2000000572 Christie P35610 6646 SOAT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM .013 {oleoyl-CoA} (mutant C92A/C333A/C345A/C365A/C387A/C467A/C516A/C546A) 0.013 mM oleoyl-CoA CHEBI:15534 Y Y ECO:0000006 Pubmed:11684695 PENTACON Added by PENTACON; PENTACON Notes: Mutant: C92A/C333A/C345A/C365A/C387A/C467A/C516A/C546A AAP 2000000573 Christie P35610 6646 SOAT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM .0118 {oleoyl-CoA} (mutant C92A/C333A/C345A/C365A/C387A/C467A/C516A/C528A/C546A) 0.0118 mM oleoyl-CoA CHEBI:15534 Y Y ECO:0000006 Pubmed:11684695 PENTACON Added by PENTACON; PENTACON Notes: Mutant: C92A/C333A/C345A/C365A/C387A/C467A/C516A/C528A/C546A AAP 2000000574 Christie P35610 6646 SOAT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.0071 {oleoyl-CoA} (#6# wild-type enzyme <36>) <36> 0.0071 mM oleoyl-CoA CHEBI:15534 2.3.1.26 #6# wild-type enzyme <36> Y Y ECO:0000006 Pubmed:11684695 BRENDA <36> Lu, X.; Lin, S.; Chang, C.C.Y.; Chang, T.: Mutant acyl-coenzyme A: cholesterol acyltransferase 1 devoid of cysteine residues remains catalytically active. J. Biol. Chem. (2002) 277, 711-718. {Pubmed:11684695} AAP 12/7/2011 1111 2000000575 Christie P35610 6646 SOAT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.0072 {oleoyl-CoA} (#6# mutant HisACAT1/P64 <37>) <37> 0.0072 mM oleoyl-CoA CHEBI:15534 2.3.1.26 #6# HisACAT1, mutant HisACAT1/P64 <37> Y Y ECO:0000006 Pubmed:11888294 BRENDA <37> Yu, C.; Zhang, Y.; Lu, X.; Chen, J.; Chang, C.C.Y.; Chang, T.: Role of the N-terminal hydrophilic domain of acyl-coenzyme A:cholesterol acyltransferase 1 on the enzymes's quaternary structure and catalytic efficiency. Biochemistry (2002) 41, 3762-3769. {Pubmed:11888294}; PENTACON Notes: Mutant: P64 AAP 12/7/2011 1111 2000000576 Christie P35610 6646 SOAT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.0154 {oleoyl-CoA} (#6# mutant HisACAT1/1-65 <37>) <37> 0.0154 mM oleoyl-CoA CHEBI:15534 2.3.1.26 #6# mutant HisACAT1/1-65 <37> Y Y ECO:0000006 Pubmed:11888294 BRENDA <37> Yu, C.; Zhang, Y.; Lu, X.; Chen, J.; Chang, C.C.Y.; Chang, T.: Role of the N-terminal hydrophilic domain of acyl-coenzyme A:cholesterol acyltransferase 1 on the enzymes's quaternary structure and catalytic efficiency. Biochemistry (2002) 41, 3762-3769. {Pubmed:11888294}; PENTACON Notes: Mutant: delta1-65 AAP 12/7/2011 1111 2000000577 Christie P35610 6646 SOAT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.0072 {oleoyl-CoA} (#6# HisACAT1 <37>) <37> 0.0072 mM oleoyl-CoA CHEBI:15534 2.3.1.26 #6# HisACAT1 <37> Y Y ECO:0000006 Pubmed:11888294 BRENDA <37> Yu, C.; Zhang, Y.; Lu, X.; Chen, J.; Chang, C.C.Y.; Chang, T.: Role of the N-terminal hydrophilic domain of acyl-coenzyme A:cholesterol acyltransferase 1 on the enzymes's quaternary structure and catalytic efficiency. Biochemistry (2002) 41, 3762-3769. {Pubmed:11888294} AAP 12/7/2011 1111 2000000578 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM 2.3-3.8 {alanine-p-nitroanilide} mM alanine-4-nitroanilide Y Y ECO:0000006 Pubmed:11917124 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: alanine-4-nitroanilide; Pubchem CID 150936 AAP 2000000579 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.006-0.028 {leukotriene A4} (#4# pH 8.0, wild-type enzyme in comparison to mutant enzymes <36,37>) <36,37> mM leukotriene A4 CHEBI:15651 3.3.2.6 #4# pH 8.0, wild-type enzyme in comparison to mutant enzymes <36,37> Y Y ECO:0000006 Pubmed:11917124 BRENDA <37> Rudberg, P.C.; Tholander, F.; Thunnissen, M.M.; Samuelsson, B.; Haeggstrom, J.Z.: Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375. Proc. Natl. Acad. Sci. USA (2002) 99, 4215-4220. {Pubmed:11917124} AAP 12/7/2011 1111 2000000580 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.7 {NAD+} (#4# 37°C, pH 7.5, T11S mutant <35>) <35> 0.7 mM NAD(+) CHEBI:15846 1.1.1.141 #4# 37°C, pH 7.5, T11S mutant <35> Y Y ECO:0000006 Pubmed:12144871 BRENDA <35> Cho, H.; Tai, H.H.: Threonine 11 of human NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase may interact with NAD(+) during catalysis. Prostaglandins (2002) 66, 505-509. {Pubmed:12144871}; PENTACON Notes: Mutant: T11S AAP 12/7/2011 1111 2000000581 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0086 {(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate} (#4# 37°C, pH 7.5, T11S mutant <35>) <35> 0.0086 mM prostaglandin E2 CHEBI:15551 1.1.1.141 #4# 37°C, pH 7.5, T11S mutant <35> Y Y ECO:0000006 Pubmed:12144871 BRENDA <35> Cho, H.; Tai, H.H.: Threonine 11 of human NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase may interact with NAD(+) during catalysis. Prostaglandins (2002) 66, 505-509. {Pubmed:12144871}; PENTACON Notes: Mutant: T11S AAP 12/7/2011 1111 2000000582 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.03 {NAD+} (#4# 37°C, pH 7.5 <35>) <35> 0.03 mM NAD(+) CHEBI:15846 1.1.1.141 #4# 37°C, pH 7.5 <35> Y Y ECO:0000006 Pubmed:12144871 BRENDA <35> Cho, H.; Tai, H.H.: Threonine 11 of human NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase may interact with NAD(+) during catalysis. Prostaglandins (2002) 66, 505-509. {Pubmed:12144871} AAP 12/7/2011 1111 2000000583 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0071 {(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate} (#4# 37°C, pH 7.5 <35>) <35> 0.0071 mM prostaglandin E2 CHEBI:15551 1.1.1.141 #4# 37°C, pH 7.5 <35> Y Y ECO:0000006 Pubmed:12144871 BRENDA <35> Cho, H.; Tai, H.H.: Threonine 11 of human NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase may interact with NAD(+) during catalysis. Prostaglandins (2002) 66, 505-509. {Pubmed:12144871} AAP 12/7/2011 1111 2000000584 Jodi P34913 2053 EPHX2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 338 {threo-10-hydroxy-9-phosphonooxy-octadecanoic acid} 338 nmol/min/mg threo-10-hydroxy-9-phosphonooxy-octadecanoic acid Y Y ECO:0000006 Pubmed:12574510 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: threo-10-hydroxy-9-phosphonooxy-octadecanoic acid AAP 2000000585 Jodi P34913 2053 EPHX2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 57.6 {p-nitrophenyl phosphate} 57.6 nmol/min/mg 4-nitrophenyl phosphate CHEBI:17440 Y Y ECO:0000006 Pubmed:12574510 PENTACON Added by PENTACON AAP 2000000586 Jodi P34913 2053 EPHX2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1.6 {p-nitrophenyl phosphate} <33> 1.6 mM 4-nitrophenyl phosphate CHEBI:17440 3.3.2.10 Y Y ECO:0000006 Pubmed:12574510 BRENDA <33> Newman, J.W.; Morisseau, C.; Harris, T.R.; Hammock, B.D.: The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity. Proc. Natl. Acad. Sci. USA (2003) 100, 1558-1563. {Pubmed:12574510} (c); PENTACON Notes: Request ChEBI ID: threo-10-hydroxy-9-phosphonooxy-octadecanoic acid AAP 12/7/2011 1111 2000000587 Jodi P34913 2053 EPHX2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.0209 {threo-10-hydroxy-9-phosphonooxy-octadecanoic acid} <33> 0.0209 mM threo-10-hydroxy-9-phosphonooxy-octadecanoic acid 3.3.2.10 Y Y ECO:0000006 Pubmed:12574510 BRENDA <33> Newman, J.W.; Morisseau, C.; Harris, T.R.; Hammock, B.D.: The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity. Proc. Natl. Acad. Sci. USA (2003) 100, 1558-1563. {Pubmed:12574510} (c) AAP 12/7/2011 1111 2000000588 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0039 {(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate} <30> 0.0039 mM prostaglandin E2 CHEBI:15551 1.1.1.141 Y Y ECO:0000033 Pubmed:12664592 BRENDA <30> Tai, H.H.; Ensor, C.M.; Zhou, H.; Yan, F.: Structure and function of human NAD+-linked 15-hydroxyprostaglandin dehydrogenase. Adv. Exp. Med. Biol. (2002) 507, 245-250. {Pubmed:12664592} AAP 12/7/2011 1111 2000000589 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.046 {NAD+} <30> 0.046 mM NAD+ CHEBI:15846 1.1.1.141 Y Y ECO:0000033 Pubmed:12664592 BRENDA <30> Tai, H.H.; Ensor, C.M.; Zhou, H.; Yan, F.: Structure and function of human NAD+-linked 15-hydroxyprostaglandin dehydrogenase. Adv. Exp. Med. Biol. (2002) 507, 245-250. {Pubmed:12664592} AAP 12/7/2011 1111 2000000590 Christie P18054 239 ALOX12 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# .007 {O2} <40> 0.007 mM O2 CHEBI:15379 1.13.11.31 Y Y ECO:0000006 Pubmed:12731864 BRENDA <40> Segraves, E.N.; Holman, T.R.: Kinetic investigations of the rate-limiting step in human 12- and 15-lipoxygenase. Biochemistry (2003) 42, 5236-5243. {Pubmed:12731864} (c) AAP 12/7/2011 1111 2000000591 Christie P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# .0042 {O2} <34> 0.0042 mM O2 CHEBI:15379 1.13.11.33 Y Y ECO:0000006 Pubmed:12731864 BRENDA <34> Segraves, E.N.; Holman, T.R.: Kinetic investigations of the rate-limiting step in human 12- and 15-lipoxygenase. Biochemistry (2003) 42, 5236-5243. {Pubmed:12731864} (c) AAP 12/7/2011 1111 2000000592 Jenn Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #11# 1.6 {glutathione} (#11# human recombinant enzyme <37>) <37> 2700 nmol/min/mg glutathione CHEBI:16856 Y Y ECO:0000033 Pubmed:12895593 PENTACON Added by PENTACON; PENTACON Notes: human recombinant enzyme AAP 2000000593 Jenn Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 1300 {leukotriene A4} (#11# human recombinant enzyme <37>) <37> 1300 nmol/min/mg leukotriene A4 CHEBI:15651 Y Y ECO:0000033 Pubmed:12895593 PENTACON Added by PENTACON; PENTACON Notes: human recombinant enzyme AAP 2000000594 Jenn Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/KM #11# 1.6 {glutathione} (#11# human recombinant enzyme <37>) <37> 1.6 mM glutathione CHEBI:16856 4.4.1.20 #11# human recombinant enzyme <37> Y Y ECO:0000033 Pubmed:12895593 BRENDA <37> Lam, B.K.: Leukotriene C4 synthase. Prostaglandins Leukot. Essent. Fatty Acids (2003) 69, 111-116. {Pubmed:} AAP 12/7/2011 1111 2000000595 Jenn Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/KM #11# 0.0036 {leukotriene A4} (#11# human recombinant enzyme <37>) <37> 0.0036 mM leukotriene A4 CHEBI:15651 4.4.1.20 #11# human recombinant enzyme <37> Y Y ECO:0000033 Pubmed:12895593 BRENDA <37> Lam, B.K.: Leukotriene C4 synthase. Prostaglandins Leukot. Essent. Fatty Acids (2003) 69, 111-116. {Pubmed:} AAP 12/7/2011 1111 2000000596 Jenn Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.11 {leukotriene A5} (#3# pH 6.5, 30°C <15>) 0.11 mM leukotriene A5 Y Y ECO:0000006 Pubmed:1312812 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: Leukotriene A5; pH 6.5, 30°C AAP 2000000597 Jenn Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 0.41 {leukotriene A5} (#3# pH 6.5, 30°C <15>) 0.41 nmol/min/mg leukotriene A5 Y Y ECO:0000006 Pubmed:1312812 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: Leukotriene A5; pH 6.5, 30°C AAP 2000000598 Jenn Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 0.04 {leukotriene methyl ester} (#3# pH 6.5, 30°C <15>; #1# 22°C, pH 7.6 <23>) <15,23> 0.04 nmol/min/mg leukotriene methyl ester Y Y ECO:0000006 Pubmed:1312812 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: 5S-​trans-​5,​6-​oxido-​7E,​9E,​11Z,​14Z-​eicosatetraenoic acid,​ methyl ester AAP 2000000599 Jenn Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 0.56 {leukotriene A4} (#3# pH 6.5, 30°C <15>) <15> 0.56 nmol/min/mg leukotriene A4 CHEBI:15651 Y Y ECO:0000006 Pubmed:1312812 PENTACON Added by PENTACON; PENTACON Notes: pH 6.5, 30°C AAP 2000000600 Jenn Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/KM #1,3# 0.015 {leukotriene methyl ester} (#3# pH 6.5, 30°C <15>; #1# 22°C, pH 7.6 <23>) <15,23> 0.015 mM leukotriene methyl ester 4.4.1.20 #3# pH 6.5, 30°C <15>; #1# 22°C, pH 7.6 <23> Y Y ECO:0000006 Pubmed:1312812 BRENDA <15> Söderström, M.; Mannervik, B.; Garkov, V.; Hammarström, S.: On the nature of leukotriene C4 synthase in human platelets. Arch. Biochem. Biophys. (1992) 294, 70-74. {Pubmed:1312812} (c); PENTACON Notes: Request ChEBI ID: 5S-​trans-​5,​6-​oxido-​7E,​9E,​11Z,​14Z-​eicosatetraenoic acid,​ methyl ester AAP 12/7/2011 1111 2000000601 Jenn Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.007 {leukotriene A4} (#3# pH 6.5, 30°C <15>) <15> 0.007 mM leukotriene A4 CHEBI:15651 4.4.1.20 #3# pH 6.5, 30°C <15> Y Y ECO:0000006 Pubmed:1312812 BRENDA <15> Söderström, M.; Mannervik, B.; Garkov, V.; Hammarström, S.: On the nature of leukotriene C4 synthase in human platelets. Arch. Biochem. Biophys. (1992) 294, 70-74. {Pubmed:1312812} (c) AAP 12/7/2011 1111 2000000602 Jenn Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/KM 1.83 {glutathione} <21> 1.83 mM glutathione CHEBI:16856 Y Y ECO:0000006 Pubmed:1425677 PENTACON Added by PENTACON AAP 2000000603 Jenn Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0166 {leukotriene A4} <21> 0.0166 mM leukotriene A4 CHEBI:15651 4.4.1.20 Y Y ECO:0000006 Pubmed:1425677 BRENDA <21> Nicholson, D.W.; Klemba, M.W.; Rasper, D.M.; Metters, K.M.; Zamboni, R.J.: Purification of human leukotriene C4 synthase from dimethylsulfoxide-differentiated U937 cells. Eur. J. Biochem. (1992) 209, 725-734. {Pubmed:1425677} (c) AAP 12/7/2011 1111 2000000604 Jenn P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0279-0.9145 {NAD+} (#4# 37°C, pH 7.5 <32>; #4# 37°C, pH 7.5, various mutants <33>) <32,33> mM NAD(+) CHEBI:15846 1.1.1.141 #4# 37°C, pH 7.5 <32>; #4# 37°C, pH 7.5, various mutants <33> Y Y ECO:0000006 Pubmed:14592457 BRENDA <32> Cho, H.; Oliveira, M.A.; Tai, H.H.: Critical residues for the coenzyme specificity of NAD+-dependent 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2003) 419, 139-146. {Pubmed:14592457}; PENTACON Notes: various mutants AAP 12/7/2011 1111 2000000605 Jenn P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.0053-1.068 {prostaglandin E2} (#4# 37°C, pH 7.5, various mutants <32>) <32> mM prostaglandin E2 CHEBI:15551 1.1.1.141 #4# 37°C, pH 7.5, various mutants <32> Y Y ECO:0000006 Pubmed:14592457 BRENDA <32> Cho, H.; Oliveira, M.A.; Tai, H.H.: Critical residues for the coenzyme specificity of NAD+-dependent 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2003) 419, 139-146. {Pubmed:14592457}; PENTACON Notes: various mutants AAP 12/7/2011 1111 2000000606 Jenn P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0315 {NAD+} (#4# 37°C, pH 7.5 <32>; #4# 37°C, pH 7.5 <33>) <32,33> 0.032 mM NAD(+) CHEBI:15846 1.1.1.141 #4# 37°C, pH 7.5 <32>; #4# 37°C, pH 7.5 <33> Y Y ECO:0000006 Pubmed:14592457 BRENDA <32> Cho, H.; Oliveira, M.A.; Tai, H.H.: Critical residues for the coenzyme specificity of NAD+-dependent 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2003) 419, 139-146. {Pubmed:14592457} AAP 12/7/2011 1111 2000000607 Jenn P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0063 {(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate} (#4# 37°C, pH 7.5 <32>) <32> 0.0063 mM prostaglandin E2 CHEBI:15551 1.1.1.141 #4# 37°C, pH 7.5 <32> Y Y ECO:0000006 Pubmed:14592457 BRENDA <32> Cho, H.; Oliveira, M.A.; Tai, H.H.: Critical residues for the coenzyme specificity of NAD+-dependent 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2003) 419, 139-146. {Pubmed:14592457} AAP 12/7/2011 1111 2000000608 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0117 {prostaglandin E2} <22> 0.0117 mM prostaglandin E2 CHEBI:15551 1.1.1.141 Y Y ECO:0000006 Pubmed:1508959 BRENDA <22> Mibe, M.; Nagai, K.; Oshige, T.; Mori, N.: Endogenous inhibitors of human placental prostaglandin dehydrogenase. Prostaglandins Leukot. Essent. Fatty Acids (1992) 46, 241-245. {Pubmed:1508959} AAP 12/7/2011 1111 2000000609 Jodi Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/IC50 0.050 {diethylcarbamazine} 0.05 mM diethylcarbamazine CHEBI:4527 Y Y ECO:0000006 Pubmed:1517222 PENTACON Added by PENTACON AAP 2000000610 Jodi Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/IC50 0.020 {N-ethylmaleimide} 0.02 mM N-ethylmaleimide CHEBI:44485 Y Y ECO:0000006 Pubmed:1517222 PENTACON Added by PENTACON AAP 2000000611 Jodi Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 1.2 {glutathione} (#3# pH 7.4, 25°C <10>) <10> 1.2 mM glutathione CHEBI:16856 4.4.1.20 #3# pH 7.4, 25°C <10> Y Y ECO:0000006 Pubmed:1517222 BRENDA <10> Nicholson, D.W.; Ali, A.; Klemba, M.W.; Munday, N.A.; Zamboni, R.J.; Ford-Hutchinson, A.W.: Human leukotriene C4 synthase expression in dimethyl sulfoxide-differentiated U937 cells. J. Biol. Chem. (1992) 267, 17849-17857. {Pubmed:1517222} (c) AAP 12/7/2011 1111 2000000612 Jodi Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0056 {leukotriene A4} (#3# pH 7.4, 25°C <10>) <10> 0.0056 mM leukotriene A4 CHEBI:15651 4.4.1.20 #3# pH 7.4, 25°C <10> Y Y ECO:0000006 Pubmed:1517222 BRENDA <10> Nicholson, D.W.; Ali, A.; Klemba, M.W.; Munday, N.A.; Zamboni, R.J.; Ford-Hutchinson, A.W.: Human leukotriene C4 synthase expression in dimethyl sulfoxide-differentiated U937 cells. J. Biol. Chem. (1992) 267, 17849-17857. {Pubmed:1517222} (c) AAP 12/7/2011 1111 2000000613 Jodi P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 27.2 {1,2-bis[4-(1-pyreno)butanoyl]-sn-glycero-3-phosphocholine} 27.2 uM/min/ug 1,2-bis[4-(1-pyreno)butanoyl]-sn-glycero-3-phosphocholine Y Y ECO:0000006 Pubmed:15249036 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: 1,2-bis[4-(1-pyreno)butanoyl]-sn-glycero-3-phosphocholine AAP 2000000614 Jodi P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 10.0 {Phosphatidylcholine} 10 uM/min/ug Phosphatidylcholine CHEBI:49183 Y Y ECO:0000006 Pubmed:15249036 PENTACON Added by PENTACON AAP 2000000615 Jodi P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/KM #13# 0.00056 {1,2-bis[4-(1-pyreno)butanoyl]-sn-glycero-3-phosphocholine} (#13# fluorescent assay, pH 7.4, 25°C, recombinant enzyme <61>) <61> 0.00056 mM 1,2-bis[4-(1-pyreno)butanoyl]-sn-glycero-3-phosphocholine 2.3.1.43 #13# fluorescent assay, pH 7.4, 25°C, recombinant enzyme <61> Y Y ECO:0000006 Pubmed:15249036 BRENDA <61> Lane, S.B.; Tchedre, K.T.; Nair, M.P.; Thigpen, A.E.; Lacko, A.G.: Characterization of lecithin:cholesterol acyltransferase expressed in a human lung cell line. Protein Expr. Purif. (2004) 36, 157-164. {Pubmed:15249036}; PENTACON Notes: Request ChEBI ID: 1,2-bis[4-(1-pyreno)butanoyl]-sn-glycero-3-phosphocholine AAP 12/7/2011 1111 2000000616 Jodi P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/KM #13# 0.0006 {Phosphatidylcholine} (#13# radioassay, pH 7.4, 37°C, recombinant enzyme <61>) <61> 0.0006 mM Phosphatidylcholine CHEBI:49183 2.3.1.43 #13# radioassay, pH 7.4, 37°C, recombinant enzyme <61> Y Y ECO:0000006 Pubmed:15249036 BRENDA <61> Lane, S.B.; Tchedre, K.T.; Nair, M.P.; Thigpen, A.E.; Lacko, A.G.: Characterization of lecithin:cholesterol acyltransferase expressed in a human lung cell line. Protein Expr. Purif. (2004) 36, 157-164. {Pubmed:15249036} AAP 12/7/2011 1111 2000000617 Jodi Q05469 3991 LIPE Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 70 {vinyl propionate} (#2# 37°C, pH 8.0 <16>) <16> 70 mM vinyl propionate 3.1.1.79 #2# 37°C, pH 8.0 <16> Y Y ECO:0000006 Pubmed:15260473 BRENDA <16> Ben Ali, Y.; Chahinian, H.; Petry, S.; Muller, G.; Carriere, F.; Verger, R.; Abousalham, A.: Might the kinetic behavior of hormone-sensitive lipase reflect the absence of the lid domain?. Biochemistry (2004) 43, 9298-9306. {Pubmed:15260473}; PENTACON Notes: Request ChEBI ID: vinyl propionate; Pubchem ID: CID 7750 AAP 12/7/2011 1111 2000000618 Jodi Q05469 3991 LIPE Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 10 {vinyl butyrate} (#2# 37°C, pH 8.0 <16>) <16> 10 mM vinyl butyrate 3.1.1.79 #2# 37°C, pH 8.0 <16> Y Y ECO:0000006 Pubmed:15260473 BRENDA <16> Ben Ali, Y.; Chahinian, H.; Petry, S.; Muller, G.; Carriere, F.; Verger, R.; Abousalham, A.: Might the kinetic behavior of hormone-sensitive lipase reflect the absence of the lid domain?. Biochemistry (2004) 43, 9298-9306. {Pubmed:15260473}; PENTACON Notes: Request ChEBI ID: vinyl butyrate; Pubchem ID: CID 31247 AAP 12/7/2011 1111 2000000619 Jodi Q05469 3991 LIPE Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 15 {tripropionyl glycerol} (#2# 37°C, pH 8.0 <16>) <16> 15 mM tripropionyl glycerol 3.1.1.79 #2# 37°C, pH 8.0 <16> Y Y ECO:0000006 Pubmed:15260473 BRENDA <16> Ben Ali, Y.; Chahinian, H.; Petry, S.; Muller, G.; Carriere, F.; Verger, R.; Abousalham, A.: Might the kinetic behavior of hormone-sensitive lipase reflect the absence of the lid domain?. Biochemistry (2004) 43, 9298-9306. {Pubmed:15260473}; PENTACON Notes: Request ChEBI ID: tripropionyl glycerol; Pubchem ID: CID 8763 AAP 12/7/2011 1111 2000000620 Jodi Q05469 3991 LIPE Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.4 {tributanoyl glycerol} (#2# 37°C, pH 8.0 <16>) <16> 0.4 mM tributanoyl glycerol 3.1.1.79 #2# 37°C, pH 8.0 <16> Y Y ECO:0000006 Pubmed:15260473 BRENDA <16> Ben Ali, Y.; Chahinian, H.; Petry, S.; Muller, G.; Carriere, F.; Verger, R.; Abousalham, A.: Might the kinetic behavior of hormone-sensitive lipase reflect the absence of the lid domain?. Biochemistry (2004) 43, 9298-9306. {Pubmed:15260473}; PENTACON Notes: Request ChEBI ID: tributanoyl glycerol AAP 12/7/2011 1111 2000000621 Jodi Q05469 3991 LIPE Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 170 {vinyl acetate} (#2# 37°C, pH 8.0 <16>) <16> 170 mM vinyl acetate CHEBI:46916 3.1.1.79 #2# 37°C, pH 8.0 <16> Y Y ECO:0000006 Pubmed:15260473 BRENDA <16> Ben Ali, Y.; Chahinian, H.; Petry, S.; Muller, G.; Carriere, F.; Verger, R.; Abousalham, A.: Might the kinetic behavior of hormone-sensitive lipase reflect the absence of the lid domain?. Biochemistry (2004) 43, 9298-9306. {Pubmed:15260473} AAP 12/7/2011 1111 2000000622 Jodi P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 130 {proline-4-nitroanilide} 130 nmol/min/mg proline-4-nitroanilide Y Y ECO:0000006 Pubmed:1536866 PENTACON Added by PENTACON; PENTACON Notes: pH 7.6, 22°C, 100 mM NaCl; Request ChEBI ID: proline-4-nitroanilide AAP 2000000623 Jodi P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 30 {lysine-4-nitroanilide} 30 nmol/min/mg lysine-4-nitroanilide Y Y ECO:0000006 Pubmed:1536866 PENTACON Added by PENTACON; PENTACON Notes: pH 7.6, 22°C, 100 mM NaCl; Request ChEBI ID: lysine-4-nitroanilide AAP 2000000624 Jodi P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 130 {leucine-4-nitroanilide} 130 nmol/min/mg leucine-4-nitroanilide Y Y ECO:0000006 Pubmed:1536866 PENTACON Added by PENTACON; PENTACON Notes: pH 7.6, 22°C, 100 mM NaCl; Request ChEBI ID: leucine-4-nitroanilide: CID 121895 AAP 2000000625 Jodi P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 140 {arginine-4-nitroanilide} 140 nmol/min/mg arginine-4-nitroanilide Y Y ECO:0000006 Pubmed:1536866 PENTACON Added by PENTACON; PENTACON Notes: pH 7.6, 22°C, 100 mM NaCl; Request ChEBI ID: arginine-4-nitroanilide AAP 2000000626 Jodi P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 530 {alanine-4-nitroanilide} 530 nmol/min/mg alanine-4-nitroanilide Y Y ECO:0000006 Pubmed:1536866 PENTACON Added by PENTACON; PENTACON Notes: pH 7.6, 22°C, 100 mM NaCl; Request ChEBI ID: alanine-4-nitroanilide; Pubchem ID: CID 150936 AAP 2000000627 Jodi P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.1 {lysine-4-nitroanilide} (#4# pH 7.6, 22°C <17>) <17> 0.1 mM lysine-4-nitroanilide 3.3.2.6 #4# pH 7.6, 22°C <17> Y Y ECO:0000006 Pubmed:1536866 BRENDA <17> Wetterholm, A.; Haeggström, J.Z.: Leukotriene A4 hydrolase: an anion activated peptidase. Biochim. Biophys. Acta (1992) 1123, 275-281. {Pubmed:1536866}; PENTACON Notes: Request ChEBI ID: lysine-4-nitroanilide AAP 12/7/2011 1111 2000000628 Jodi P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.1 {proline-4-nitroanilide} (#4# pH 7.6, 22°C <17>) <17> 0.1 mM proline-4-nitroanilide 3.3.2.6 #4# pH 7.6, 22°C <17> Y Y ECO:0000006 Pubmed:1536866 BRENDA <17> Wetterholm, A.; Haeggström, J.Z.: Leukotriene A4 hydrolase: an anion activated peptidase. Biochim. Biophys. Acta (1992) 1123, 275-281. {Pubmed:1536866}; PENTACON Notes: 100 mM NaCl; Request ChEBI ID: proline-4-nitroanilide AAP 12/7/2011 1111 2000000629 Jodi P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.3 {leucine-4-nitroanilide} (#4# pH 7.6, 22°C <17>) <17> 0.3 mM leucine-4-nitroanilide 3.3.2.6 #4# pH 7.6, 22°C <17> Y Y ECO:0000006 Pubmed:1536866 BRENDA <17> Wetterholm, A.; Haeggström, J.Z.: Leukotriene A4 hydrolase: an anion activated peptidase. Biochim. Biophys. Acta (1992) 1123, 275-281. {Pubmed:1536866}; PENTACON Notes: 100 mM NaCl; Request ChEBI ID: leucine-4-nitroanilide AAP 12/7/2011 1111 2000000630 Jodi P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.2 {arginine-4-nitroanilide} (#4# pH 7.6, 22°C <17>) <17> 0.2 mM arginine-4-nitroanilide 3.3.2.6 #4# pH 7.6, 22°C <17> Y Y ECO:0000006 Pubmed:1536866 BRENDA <17> Wetterholm, A.; Haeggström, J.Z.: Leukotriene A4 hydrolase: an anion activated peptidase. Biochim. Biophys. Acta (1992) 1123, 275-281. {Pubmed:1536866}; PENTACON Notes: 100 mM NaCl; Request ChEBI ID: arginine-4-nitroanilide AAP 12/7/2011 1111 2000000631 Jodi P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.5 {alanine-4-nitroanilide} (#4# pH 7.6, 22°C <17>) <17> 0.5 mM alanine-4-nitroanilide 3.3.2.6 #4# pH 7.6, 22°C <17> Y Y ECO:0000006 Pubmed:1536866 BRENDA <17> Wetterholm, A.; Haeggström, J.Z.: Leukotriene A4 hydrolase: an anion activated peptidase. Biochim. Biophys. Acta (1992) 1123, 275-281. {Pubmed:1536866}; PENTACON Notes: 100 mM NaCl; Request ChEBI ID: alanine-4-nitroanilide; Pubchem ID: CID 150936 AAP 12/7/2011 1111 2000000632 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.022 {NAD+} (#4# recombinant enzyme expressed in E. coli <26>; #4# 37°C, pH 7.5, V186K mutant <33>) <26,33> 0.022 mM NAD(+) CHEBI:15846 1.1.1.141 #4# recombinant enzyme expressed in E. coli <26>; #4# 37°C, pH 7.5, V186K mutant <33> Y Y ECO:0000006 Pubmed:15581601 BRENDA <33> Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.: Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2005) 433, 447-453. {Pubmed:15581601}; PENTACON Notes: Mutant: V186K AAP 12/7/2011 1111 2000000633 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0035 {(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate} (#4# 37°C, pH 7.5, V186K mutant <33>) <33> 0.0035 mM prostaglandin E2 CHEBI:15551 1.1.1.141 #4# 37°C, pH 7.5, V186K mutant <33> Y Y ECO:0000006 Pubmed:15581601 BRENDA <33> Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.: Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2005) 433, 447-453. {Pubmed:15581601}; PENTACON Notes: Mutant: V186K AAP 12/7/2011 1111 2000000634 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.27 {NAD+} (#4# 37°C, pH 7.5, V186I mutant <33>) <33> 0.27 mM NAD(+) CHEBI:15846 1.1.1.141 #4# 37°C, pH 7.5, V186I mutant <33> Y Y ECO:0000006 Pubmed:15581601 BRENDA <33> Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.: Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2005) 433, 447-453. {Pubmed:15581601}; PENTACON Notes: Mutant: V186I AAP 12/7/2011 1111 2000000635 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.022 {(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate} (#4# 37°C, pH 7.5, V186I mutant <33>) <33> 0.022 mM prostaglandin E2 CHEBI:15551 1.1.1.141 #4# 37°C, pH 7.5, V186I mutant <33> Y Y ECO:0000006 Pubmed:15581601 BRENDA <33> Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.: Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2005) 433, 447-453. {Pubmed:15581601}; PENTACON Notes: Mutant: V186I AAP 12/7/2011 1111 2000000636 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.024 {NAD+} (#4# 37°C, pH 7.5, V186A mutant <33>) <33> 0.024 mM NAD(+) CHEBI:15846 1.1.1.141 #4# 37°C, pH 7.5, V186A mutant <33> Y Y ECO:0000006 Pubmed:15581601 BRENDA <33> Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.: Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2005) 433, 447-453. {Pubmed:15581601}; PENTACON Notes: Mutant: V186A AAP 12/7/2011 1111 2000000637 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.032 {NAD+} (#4# 37°C, pH 7.5 <32>; #4# 37°C, pH 7.5, N91D mutant <33>) <32,33> 0.032 mM NAD(+) CHEBI:15846 1.1.1.141 #4# 37°C, pH 7.5 <32>; #4# 37°C, pH 7.5, N91D mutant <33> Y Y ECO:0000006 Pubmed:15581601 BRENDA <33> Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.: Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2005) 433, 447-453. {Pubmed:15581601}; PENTACON Notes: Mutant: N91D AAP 12/7/2011 1111 2000000638 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0026 {(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate} (#4# 37°C, pH 7.5, N91D mutant <33>) <33> 0.0026 mM prostaglandin E2 CHEBI:15551 1.1.1.141 #4# 37°C, pH 7.5, N91D mutant <33> Y Y ECO:0000006 Pubmed:15581601 BRENDA <33> Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.: Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2005) 433, 447-453. {Pubmed:15581601}; PENTACON Notes: Mutant: N91D AAP 12/7/2011 1111 2000000639 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.72 {NAD+} (#4# 37°C, pH 7.5, N91A mutant <33>) <33> 0.72 mM NAD(+) CHEBI:15846 1.1.1.141 #4# 37°C, pH 7.5, N91A mutant <33> Y Y ECO:0000006 Pubmed:15581601 BRENDA <33> Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.: Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2005) 433, 447-453. {Pubmed:15581601}; PENTACON Notes: Mutant: N91A AAP 12/7/2011 1111 2000000640 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.006 {(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate} (#4# 37°C, pH 7.5, N91A mutant <33>) <33> 0.006 mM prostaglandin E2 CHEBI:15551 1.1.1.141 #4# 37°C, pH 7.5, N91A mutant <33> Y Y ECO:0000006 Pubmed:15581601 BRENDA <33> Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.: Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2005) 433, 447-453. {Pubmed:15581601}; PENTACON Notes: Mutant: N91A AAP 12/7/2011 1111 2000000641 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.098 {NAD+} (#4# 37°C, pH 7.5, I17V mutant <33>) <33> 0.098 mM NAD(+) CHEBI:15846 1.1.1.141 #4# 37°C, pH 7.5, I17V mutant <33> Y Y ECO:0000006 Pubmed:15581601 BRENDA <33> Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.: Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2005) 433, 447-453. {Pubmed:15581601}; PENTACON Notes: Mutant: I17V AAP 12/7/2011 1111 2000000642 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.011 {(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate} (#4# 37°C, pH 7.5, I17V mutant <33>) <33> 0.011 mM prostaglandin E2 CHEBI:15551 1.1.1.141 #4# 37°C, pH 7.5, I17V mutant <33> Y Y ECO:0000006 Pubmed:15581601 BRENDA <33> Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.: Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2005) 433, 447-453. {Pubmed:15581601}; PENTACON Notes: Mutant: I17V AAP 12/7/2011 1111 2000000643 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.059 {NAD+} (#4# 37°C, pH 7.5, I17L mutant <33>) <33> 0.059 mM NAD(+) CHEBI:15846 1.1.1.141 #4# 37°C, pH 7.5, I17L mutant <33> Y Y ECO:0000006 Pubmed:15581601 BRENDA <33> Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.: Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2005) 433, 447-453. {Pubmed:15581601}; PENTACON Notes: Mutant: I17L AAP 12/7/2011 1111 2000000644 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0012 {(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate} (#4# 37°C, pH 7.5, I17L mutant <33>) <33> 0.0012 mM prostaglandin E2 CHEBI:15551 1.1.1.141 #4# 37°C, pH 7.5, I17L mutant <33> Y Y ECO:0000006 Pubmed:15581601 BRENDA <33> Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.: Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2005) 433, 447-453. {Pubmed:15581601}; PENTACON Notes: Mutant: I17L AAP 12/7/2011 1111 2000000645 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.55 {NAD+} (#4# 37°C, pH 7.5, I17A mutant <33>) <33> 0.55 mM NAD(+) CHEBI:15846 1.1.1.141 #4# 37°C, pH 7.5, I17A mutant <33> Y Y ECO:0000006 Pubmed:15581601 BRENDA <33> Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.: Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2005) 433, 447-453. {Pubmed:15581601}; PENTACON Notes: Mutant: I17A AAP 12/7/2011 1111 2000000646 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.011 {(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate} (#4# 37°C, pH 7.5, I17A mutant <33>) <33> 0.011 mM prostaglandin E2 CHEBI:15551 1.1.1.141 #4# 37°C, pH 7.5, I17A mutant <33> Y Y ECO:0000006 Pubmed:15581601 BRENDA <33> Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.: Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2005) 433, 447-453. {Pubmed:15581601}; PENTACON Notes: Mutant: I17A AAP 12/7/2011 1111 2000000647 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.038 {NAD+} (#4# 37°C, pH 7.5 <33>) <33> 0.038 mM NAD(+) CHEBI:15846 1.1.1.141 #4# 37°C, pH 7.5 <33> Y Y ECO:0000006 Pubmed:15581601 BRENDA <33> Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.: Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2005) 433, 447-453. {Pubmed:15581601} AAP 12/7/2011 1111 2000000648 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0034 {(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate} (#4# 37°C, pH 7.5 <33>) <33> 0.0034 mM prostaglandin E2 CHEBI:15551 1.1.1.141 #4# 37°C, pH 7.5 <33> Y Y ECO:0000006 Pubmed:15581601 BRENDA <33> Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.: Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2005) 433, 447-453. {Pubmed:15581601} AAP 12/7/2011 1111 2000000649 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0045 {(5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-5,13-dienoate} (#4# 37°C, pH 7.5, V186A mutant <33>) <33> 0.0045 mM prostaglandin E2 CHEBI:15551 1.1.1.141 #4# 37°C, pH 7.5, V186A mutant <33> Y Y ECO:0000006 Pubmed:15581601 BRENDA <33> Cho, H.; Hamza, A.; Zhan, C.G.; Tai, H.H.: Key NAD+-binding residues in human 15-hydroxyprostaglandin dehydrogenase. Arch. Biochem. Biophys. (2005) 433, 447-453. {Pubmed:15581601} AAP 12/7/2011 1111 2000000650 Chandra Q9UJ14 2686 GGT7 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1.8 {5-L-Glutamyl-4-nitroanilide} <84> 1.8 mM gamma-L-Glutamyl-p-nitroanilide Glycylglycine CHEBI:17201 2.3.2.2 Y Y ECO:0000006 Pubmed:15943911 BRENDA <84> Sener, A.; Yardimci, T.: Activity determination, kinetic analyses and isoenzyme identification of gamma glutamyltransferase in human neutrophils. J. Biochem. Mol. Biol. (2005) 38, 343-349. {Pubmed:15943911} (c); PENTACON Notes: Request ChEBI ID: gamma-L-Glutamyl-p-nitroanilide: CID 16219428; GGT 4 is an alias for GGT7 AAP 12/7/2011 1111 2000000651 Chandra Q9UJ14 2686 GGT7 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 16.9 {Glycylglycine} <84> 16.9 mM Glycylglycine CHEBI:17201 gamma-L-Glutamyl-p-nitroanilide 2.3.2.2 Y Y ECO:0000006 Pubmed:15943911 BRENDA <84> Sener, A.; Yardimci, T.: Activity determination, kinetic analyses and isoenzyme identification of gamma glutamyltransferase in human neutrophils. J. Biochem. Mol. Biol. (2005) 38, 343-349. {Pubmed:15943911} (c); PENTACON Notes: Request ChEBI ID: gamma-L-Glutamyl-p-nitroanilide: CID 16219428; GGT 4 is an alias for GGT7 AAP 12/7/2011 1111 2000000652 Jenn Q7L5N7 54947 LPCAT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 2.83 {acetyl-CoA} (#2# total membrane fractions of mesangial cells <27>) <27> 2.83 nmol/min/mg acetyl-CoA CHEBI:15351 Y Y ECO:0000006 Pubmed:16258193 PENTACON Added by PENTACON; PENTACON Notes: Acetyl-CoA concentration range: 0.025-0.8 mM AAP 2000000653 Jenn Q7L5N7 54947 LPCAT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 2.69 {acetyl-CoA} (#2# total membrane fractions of mesangial cells <27>) <27> 2.69 nmol/min/mg acetyl-CoA CHEBI:15351 Y Y ECO:0000006 Pubmed:16258193 PENTACON Added by PENTACON; PENTACON Notes: Acetyl-CoA concentration 0.2 mM AAP 2000000654 Jenn Q7L5N7 54947 LPCAT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.00921 {acetyl-CoA} (#2# total membrane fractions of mesangial cells <27>) <27> 0.00921 mM acetyl-CoA CHEBI:15351 2.3.1.67 #2# total membrane fractions of mesangial cells <27> Y Y ECO:0000006 Pubmed:16258193 BRENDA <27> Fragopoulou, E.; Iatrou, C.; Demopoulos, C.A.: Characterization of acetyl-CoA:lyso-PAF acetyltransferase of human mesangial cells. Mediators Inflamm. (2005) 2005, 263-272. {Pubmed:16258193}; PENTACON Notes: Acetyl-CoA concentration range: 0.025-0.8 mM AAP 12/7/2011 1111 2000000655 Jenn Q7L5N7 54947 LPCAT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.0712 {acetyl-CoA} (#2# total membrane fractions of mesangial cells <27>) <27> 0.0712 mM acetyl-CoA CHEBI:15351 2.3.1.67 #2# total membrane fractions of mesangial cells <27> Y Y ECO:0000006 Pubmed:16258193 BRENDA <27> Fragopoulou, E.; Iatrou, C.; Demopoulos, C.A.: Characterization of acetyl-CoA:lyso-PAF acetyltransferase of human mesangial cells. Mediators Inflamm. (2005) 2005, 263-272. {Pubmed:16258193}; PENTACON Notes: Acetyl-CoA concentration 0.2 mM AAP 12/7/2011 1111 2000000656 Jenn Q05469 3991 LIPE Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 70 {vinyl propionate} <31> 70 mM vinyl propionate 3.1.1.79 Y Y ECO:0000006 Pubmed:16325466 BRENDA <31> Chahinian, H.; Ali, Y.B.; Abousalham, A.; Petry, S.; Mandrich, L.; Manco, G.; Canaan, S.; Sarda, L.: Substrate specificity and kinetic properties of enzymes belonging to the hormone-sensitive lipase family: comparison with non-lipolytic and lipolytic carboxylesterases. Biochim. Biophys. Acta (2005) 1738, 29-36. {Pubmed:16325466} (c); PENTACON Notes: Request ChEBI ID: vinyl propionate; Pubchem:CID 7750 AAP 12/7/2011 1111 2000000657 Jenn Q05469 3991 LIPE Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 3 {vinyl laurate} <31> 3 mM vinyl laurate 3.1.1.79 Y Y ECO:0000006 Pubmed:16325466 BRENDA <31> Chahinian, H.; Ali, Y.B.; Abousalham, A.; Petry, S.; Mandrich, L.; Manco, G.; Canaan, S.; Sarda, L.: Substrate specificity and kinetic properties of enzymes belonging to the hormone-sensitive lipase family: comparison with non-lipolytic and lipolytic carboxylesterases. Biochim. Biophys. Acta (2005) 1738, 29-36. {Pubmed:16325466} (c); PENTACON Notes: Request ChEBI ID: vinyl laurate; Pubchem ID: CID 75069 AAP 12/7/2011 1111 2000000658 Jenn Q05469 3991 LIPE Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 11 {vinyl butyrate} <31> 11 mM vinyl butyrate 3.1.1.79 Y Y ECO:0000006 Pubmed:16325466 BRENDA <31> Chahinian, H.; Ali, Y.B.; Abousalham, A.; Petry, S.; Mandrich, L.; Manco, G.; Canaan, S.; Sarda, L.: Substrate specificity and kinetic properties of enzymes belonging to the hormone-sensitive lipase family: comparison with non-lipolytic and lipolytic carboxylesterases. Biochim. Biophys. Acta (2005) 1738, 29-36. {Pubmed:16325466} (c); PENTACON Notes: Request Chebi ID: vinyl butyrate; Pubchem ID:CID 31247 AAP 12/7/2011 1111 2000000659 Jenn Q05469 3991 LIPE Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 15 {tripropionin} <31> 15 mM tripropionin 3.1.1.79 Y Y ECO:0000006 Pubmed:16325466 BRENDA <31> Chahinian, H.; Ali, Y.B.; Abousalham, A.; Petry, S.; Mandrich, L.; Manco, G.; Canaan, S.; Sarda, L.: Substrate specificity and kinetic properties of enzymes belonging to the hormone-sensitive lipase family: comparison with non-lipolytic and lipolytic carboxylesterases. Biochim. Biophys. Acta (2005) 1738, 29-36. {Pubmed:16325466} (c); PENTACON Notes: Request Chebi ID: tripropionin; Pubchem ID: CID 8763 AAP 12/7/2011 1111 2000000660 Jenn Q05469 3991 LIPE Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.4 {tributyrin} <31> 0.4 mM tributyrin CHEBI:65001 3.1.1.79 Y Y ECO:0000006 Pubmed:16325466 BRENDA <31> Chahinian, H.; Ali, Y.B.; Abousalham, A.; Petry, S.; Mandrich, L.; Manco, G.; Canaan, S.; Sarda, L.: Substrate specificity and kinetic properties of enzymes belonging to the hormone-sensitive lipase family: comparison with non-lipolytic and lipolytic carboxylesterases. Biochim. Biophys. Acta (2005) 1738, 29-36. {Pubmed:16325466} (c) AAP 12/7/2011 1111 2000000661 Jenn Q05469 3991 LIPE Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 170 {vinyl acetate} <31> 170 mM vinyl acetate CHEBI:46916 3.1.1.79 Y Y ECO:0000006 Pubmed:16325466 BRENDA <31> Chahinian, H.; Ali, Y.B.; Abousalham, A.; Petry, S.; Mandrich, L.; Manco, G.; Canaan, S.; Sarda, L.: Substrate specificity and kinetic properties of enzymes belonging to the hormone-sensitive lipase family: comparison with non-lipolytic and lipolytic carboxylesterases. Biochim. Biophys. Acta (2005) 1738, 29-36. {Pubmed:16325466} (c) AAP 12/7/2011 1111 2000000662 Christie P35610 6646 SOAT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 21.8 {oleoyl-CoA} 21.8 nmol/min/mg oleoyl-CoA CHEBI:15534 Y Y ECO:0000006 Pubmed:16820149 PENTACON Added by PENTACON AAP 2000000663 Christie P35610 6646 SOAT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.00462 {oleoyl-CoA} <69> 0.00462 mM oleoyl-CoA CHEBI:15534 2.3.1.26 Y Y ECO:0000006 Pubmed:16820149 BRENDA <69> Ikenoya, M.; Yoshinaka, Y.; Kobayashi, H.; Kawamine, K.; Shibuya, K.; Sato, F.; Sawanobori, K.; Watanabe, T.; Miyazaki, A.: A selective ACAT-1 inhibitor, K-604, suppresses fatty streak lesions in fat-fed hamsters without affecting plasma cholesterol levels. Atherosclerosis (2007) 191, 290-297. {Pubmed:16820149} AAP 12/7/2011 1111 2000000664 Jenn Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 224 {Decanoyl-CoA} <107> 224 nmol/min/mg Decanoyl-CoA CHEBI:28493 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000665 Jenn P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 212 {Decanoyl-CoA} <107> 212 nmol/min/mg Decanoyl-CoA CHEBI:28493 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000666 Jenn Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 700 {Dodecanoyl-CoA} <107> 700 nmol/min/mg Dodecanoyl-CoA CHEBI:15521 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000667 Jenn P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 681 {Dodecanoyl-CoA} <107> 681 nmol/min/mg Dodecanoyl-CoA CHEBI:15521 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000668 Jenn Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 520 {eicosanoyl-CoA} <107> 520 nmol/min/mg eicosanoyl-CoA CHEBI:15527 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000669 Jenn P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 408 {eicosanoyl-CoA} <107> 408 nmol/min/mg eicosanoyl-CoA CHEBI:15527 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000670 Jenn Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 691 {hexadecanoyl-CoA} <107> 691 nmol/min/mg hexadecanoyl-CoA CHEBI:24544 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000671 Jenn P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 656 {hexadecanoyl-CoA} <60,107> 656 nmol/min/mg hexadecanoyl-CoA CHEBI:24544 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000672 Jenn Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 597 {Octadecanoyl-CoA} <107> 597 nmol/min/mg Octadecanoyl-CoA CHEBI:15541 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000673 Jenn P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 488 {Octadecanoyl-CoA} <107> 488 nmol/min/mg Octadecanoyl-CoA CHEBI:15541 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000674 Jenn Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 258 {oleoyl-CoA} <107> 258 nmol/min/mg oleoyl-CoA CHEBI:15534 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000675 Jenn P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 304 {oleoyl-CoA} <107> 304 nmol/min/mg oleoyl-CoA CHEBI:15534 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000676 Jenn Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 577 {Palmitoleoyl-CoA} <107> 577 nmol/min/mg Palmitoleoyl-CoA CHEBI:53152 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000677 Jenn P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 661 {Palmitoleoyl-CoA} <107> 661 nmol/min/mg Palmitoleoyl-CoA CHEBI:53152 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000678 Jenn Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 912 {tetradecanoyl-CoA} <107> 912 nmol/min/mg tetradecanoyl-CoA CHEBI:15532 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000679 Jenn P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 766 {tetradecanoyl-CoA} <107> 766 nmol/min/mg tetradecanoyl-CoA CHEBI:15532 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000680 Jenn Q8N9L9 122970 ACOT4 Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.147 {glutaryl-CoA} <92> 0.147 mM glutaryl-CoA CHEBI:15524 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000681 Jenn Q8N9L9 122970 ACOT4 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 132 {glutaryl-CoA} <92> 132 nmol/min/mg glutaryl-CoA CHEBI:15524 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000682 Jenn Q8N9L9 122970 ACOT4 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 581 {succinyl-CoA} <92> 581 nmol/min/mg succinyl-CoA CHEBI:15380 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000683 Jenn Q8N9L9 122970 ACOT4 Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.00034 {tetradecanoyl-CoA} <92> 0.00034 mM tetradecanoyl-CoA CHEBI:15532 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000684 Jenn Q8N9L9 122970 ACOT4 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 137 {tetradecanoyl-CoA} <92> 137 nmol/min/mg tetradecanoyl-CoA CHEBI:15532 Y Y ECO:0000006 Pubmed:16940157 PENTACON Added by PENTACON AAP 2000000685 Jenn Q8N9L9 122970 ACOT4 Homo sapiens 9606 Comment/biophysicochemical properties/KM #10# 0.014 {succinyl-CoA} <92> 0.014 mM succinyl-CoA CHEBI:15380 3.1.2.20 Y Y ECO:0000006 Pubmed:16940157 BRENDA <92> Hunt, M.C.; Rautanen, A.; Westin, M.A.; Svensson, L.T.; Alexson, S.E.: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. (2006) 20, 1855-1864. {Pubmed:16940157} AAP 12/7/2011 1111 2000000686 Jenn Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #65# 0.0358 {Decanoyl-CoA} <107> 0.0358 mM Decanoyl-CoA CHEBI:28493 3.1.2.2 Y Y ECO:0000006 Pubmed:16940157 BRENDA <107> Hunt, M.C.; Rautanen, A.; Westin, M.A.; Svensson, L.T.; Alexson, S.E.: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. (2006) 20, 1855-1864. {Pubmed:16940157} AAP 12/7/2011 1111 2000000687 Jenn P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #64# 0.0403 {Decanoyl-CoA} <107> 0.0403 mM Decanoyl-CoA CHEBI:28493 3.1.2.2 Y Y ECO:0000006 Pubmed:16940157 BRENDA <107> Hunt, M.C.; Rautanen, A.; Westin, M.A.; Svensson, L.T.; Alexson, S.E.: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. (2006) 20, 1855-1864. {Pubmed:16940157} AAP 12/7/2011 1111 2000000688 Jenn Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #65# 0.0036 {Dodecanoyl-CoA} <107> 0.0036 mM Dodecanoyl-CoA CHEBI:15521 3.1.2.2 Y Y ECO:0000006 Pubmed:16940157 BRENDA <107> Hunt, M.C.; Rautanen, A.; Westin, M.A.; Svensson, L.T.; Alexson, S.E.: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. (2006) 20, 1855-1864. {Pubmed:16940157} AAP 12/7/2011 1111 2000000689 Jenn P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #64# 0.0089 {Dodecanoyl-CoA} <107> 0.0089 mM Dodecanoyl-CoA CHEBI:15521 3.1.2.2 Y Y ECO:0000006 Pubmed:16940157 BRENDA <107> Hunt, M.C.; Rautanen, A.; Westin, M.A.; Svensson, L.T.; Alexson, S.E.: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. (2006) 20, 1855-1864. {Pubmed:16940157} AAP 12/7/2011 1111 2000000690 Jenn Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #65# 0.002 {eicosanoyl-CoA} <107> 0.002 mM eicosanoyl-CoA CHEBI:15527 3.1.2.2 Y Y ECO:0000006 Pubmed:16940157 BRENDA <107> Hunt, M.C.; Rautanen, A.; Westin, M.A.; Svensson, L.T.; Alexson, S.E.: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. (2006) 20, 1855-1864. {Pubmed:16940157} AAP 12/7/2011 1111 2000000691 Jenn P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #64# 0.0048 {eicosanoyl-CoA} <107> 0.0048 mM eicosanoyl-CoA CHEBI:15527 3.1.2.2 Y Y ECO:0000006 Pubmed:16940157 BRENDA <107> Hunt, M.C.; Rautanen, A.; Westin, M.A.; Svensson, L.T.; Alexson, S.E.: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. (2006) 20, 1855-1864. {Pubmed:16940157} AAP 12/7/2011 1111 2000000692 Jenn Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #65# 0.0036 {hexadecanoyl-CoA} <107> 0.0036 mM hexadecanoyl-CoA CHEBI:24544 3.1.2.2 Y Y ECO:0000006 Pubmed:16940157 BRENDA <107> Hunt, M.C.; Rautanen, A.; Westin, M.A.; Svensson, L.T.; Alexson, S.E.: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. (2006) 20, 1855-1864. {Pubmed:16940157} AAP 12/7/2011 1111 2000000693 Jenn P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2,64# 0.002 {hexadecanoyl-CoA} <60,107> 0.002 mM hexadecanoyl-CoA CHEBI:24544 3.1.2.2 Y Y ECO:0000006 Pubmed:16940157 BRENDA <107> Hunt, M.C.; Rautanen, A.; Westin, M.A.; Svensson, L.T.; Alexson, S.E.: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. (2006) 20, 1855-1864. {Pubmed:16940157} AAP 12/7/2011 1111 2000000694 Jenn Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #65# 0.0024 {Octadecanoyl-CoA} <107> 0.0024 mM Octadecanoyl-CoA CHEBI:15541 3.1.2.2 Y Y ECO:0000006 Pubmed:16940157 BRENDA <107> Hunt, M.C.; Rautanen, A.; Westin, M.A.; Svensson, L.T.; Alexson, S.E.: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. (2006) 20, 1855-1864. {Pubmed:16940157} AAP 12/7/2011 1111 2000000695 Jenn P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #64# 0.0028 {Octadecanoyl-CoA} <107> 0.0028 mM Octadecanoyl-CoA CHEBI:15541 3.1.2.2 Y Y ECO:0000006 Pubmed:16940157 BRENDA <107> Hunt, M.C.; Rautanen, A.; Westin, M.A.; Svensson, L.T.; Alexson, S.E.: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. (2006) 20, 1855-1864. {Pubmed:16940157} AAP 12/7/2011 1111 2000000696 Jenn Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #65# 0.0041 {oleoyl-CoA} <107> 0.0041 mM oleoyl-CoA CHEBI:15534 3.1.2.2 Y Y ECO:0000006 Pubmed:16940157 BRENDA <107> Hunt, M.C.; Rautanen, A.; Westin, M.A.; Svensson, L.T.; Alexson, S.E.: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. (2006) 20, 1855-1864. {Pubmed:16940157} AAP 12/7/2011 1111 2000000697 Jenn P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #64# 0.0061 {oleoyl-CoA} <107> 0.0061 mM oleoyl-CoA CHEBI:15534 3.1.2.2 Y Y ECO:0000006 Pubmed:16940157 BRENDA <107> Hunt, M.C.; Rautanen, A.; Westin, M.A.; Svensson, L.T.; Alexson, S.E.: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. (2006) 20, 1855-1864. {Pubmed:16940157} AAP 12/7/2011 1111 2000000698 Jenn Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #65# 0.0024 {Palmitoleoyl-CoA} <107> 0.0024 mM Palmitoleoyl-CoA CHEBI:53152 3.1.2.2 Y Y ECO:0000006 Pubmed:16940157 BRENDA <107> Hunt, M.C.; Rautanen, A.; Westin, M.A.; Svensson, L.T.; Alexson, S.E.: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. (2006) 20, 1855-1864. {Pubmed:16940157} AAP 12/7/2011 1111 2000000699 Jenn P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #64# 0.0045 {Palmitoleoyl-CoA} <107> 0.0045 mM Palmitoleoyl-CoA CHEBI:53152 3.1.2.2 Y Y ECO:0000006 Pubmed:16940157 BRENDA <107> Hunt, M.C.; Rautanen, A.; Westin, M.A.; Svensson, L.T.; Alexson, S.E.: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. (2006) 20, 1855-1864. {Pubmed:16940157} AAP 12/7/2011 1111 2000000700 Jenn Q86TX2 641371 ACOT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #65# 0.0028 {tetradecanoyl-CoA} <107> 0.0028 mM tetradecanoyl-CoA CHEBI:15532 3.1.2.2 Y Y ECO:0000006 Pubmed:16940157 BRENDA <107> Hunt, M.C.; Rautanen, A.; Westin, M.A.; Svensson, L.T.; Alexson, S.E.: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. (2006) 20, 1855-1864. {Pubmed:16940157} AAP 12/7/2011 1111 2000000701 Jenn P49753 10965 ACOT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #64# 0.0016 {tetradecanoyl-CoA} <107> 0.0016 mM tetradecanoyl-CoA CHEBI:15532 3.1.2.2 Y Y ECO:0000006 Pubmed:16940157 BRENDA <107> Hunt, M.C.; Rautanen, A.; Westin, M.A.; Svensson, L.T.; Alexson, S.E.: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. (2006) 20, 1855-1864. {Pubmed:16940157} AAP 12/7/2011 1111 2000000702 Jenn P09917 240 ALOX5 Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.0075 {arachidonate} (reaction mixture contains 1 mM DTT, 1 mM ATP, 2 mM CaCl2, 0.005 mM RBx 7796 and 0.01 mM indomethacin in phosphate buffered saline, at 37°C) 0.0075 mM arachidonate CHEBI:32395 RBx 7796 Y Y ECO:0000006 Pubmed:17039282 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: RBx 7796; reaction mixture contains 1 mM DTT, 1 mM ATP, 2 mM CaCl2, 0.005 mM RBx 7796 and 0.01 mM indomethacin in phosphate buffered saline, at 37°C AAP 2000000703 Jenn P09917 240 ALOX5 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 0.0151 {RBx 7796} (in the presence of 0.003 mM arachidonate at 37°C) 0.0151 mM RBx 7796 arachidonate CHEBI:32395 Y Y ECO:0000006 Pubmed:17039282 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: RBx 7796; in the presence of 0.03 mM arachidonate at 37°C AAP 2000000704 Jenn P09917 240 ALOX5 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 0.0593 {RBx 7796} (in the presence of 0.03 mM arachidonate at 37°C) 0.0593 mM RBx 7796 arachidonate CHEBI:32395 Y Y ECO:0000006 Pubmed:17039282 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: RBx 7796; in the presence of 0.03 mM arachidonate at 37°C AAP 2000000705 Jenn P09917 240 ALOX5 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 26900 {arachidonate} (reaction mixture contains 1 mM DTT, 1 mM ATP, 2 mM CaCl2, 0.005 mM and 0.01 mM indomethacin in phosphate buffered saline, at 37°C) 26900 nmol/min/mg arachidonate CHEBI:32395 Y Y ECO:0000006 Pubmed:17039282 PENTACON Added by PENTACON; PENTACON Notes: reaction mixture contains 1 mM DTT, 1 mM ATP, 2 mM CaCl2, 0.005 mM and 0.01 mM indomethacin in phosphate buffered saline, at 37°C AAP 2000000706 Jenn P09917 240 ALOX5 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 0.0049 {RBx 7796} (in the presence of 0 arachidonate at 37°C) 0.0049 mM RBx 7796 Y Y ECO:0000006 Pubmed:17039282 PENTACON Added by PENTACON; PENTACON Notes: in the presence of 0 arachidonate at 37°C AAP 2000000707 Jenn P09917 240 ALOX5 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0051 {arachidonate} (#3# reaction mixture contains 1 mM DTT, 1 mM ATP, 2 mM CaCl2, and 0.01 mM indomethacin in phosphate buffered saline, at 37°C <52>) <52> 0.0051 mM arachidonate CHEBI:32395 1.13.11.34 #3# reaction mixture contains 1 mM DTT, 1 mM ATP, 2 mM CaCl2, and 0.01 mM indomethacin in phosphate buffered saline, at 37°C <52> Y Y ECO:0000006 Pubmed:17039282 BRENDA <52> Shirumalla R. , S.R.; Naruganahalli K. , N.K.; Dastidar S. , D.S.; Sattigeri , S.V.; Kaur , K.G.; Deb , D.C.; Gupta J. , G.J.; Salman , S.M.; Ray , R.A.: RBx 7796: A novel inhibitor of 5-lipoxygenase. Inflamm. Res. (2006) 55, 517-527. {Pubmed:17039282} AAP 12/7/2011 1111 2000000708 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 2400000 {1,2-dioctanoyl-sn-glycero-3-phosphoglycol} <30> 2400000 nmol/min/mg 1,2-dioctanoyl-sn-glycero-3-phosphoglycol Y Y ECO:0000006 Pubmed:1730245 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: 1,2-dioctanoyl-sn-glycero-3-phosphoglycol AAP 2000000709 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 700000 {1,2-dinonanoyl-sn-glycero-3-phosphocholine} <30> 700000 nmol/min/mg 1,2-dinonanoyl-sn-glycero-3-phosphocholine Y Y ECO:0000006 Pubmed:1730245 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: 1,2-dioctanoyl-sn-glycero-3-phosphocholine AAP 2000000710 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 1420000 {1,2-dioctanoyl-sn-glycero-3-phosphocholine} <30> 1420000 nmol/min/mg 1,2-dioctanoyl-sn-glycero-3-phosphocholine Y Y ECO:0000006 Pubmed:1730245 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: 1,2-dioctanoyl-sn-glycero-3-phosphocholine AAP 2000000711 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 4300000 {1,2-dihexanoyl-sn-glycero-3-phosphocholine} ([M8L and M20L]-loop-deleted PLA2 ) 4300000 nmol/min/mg 1,2-dihexanoyl-sn-glycero-3-phosphocholine Y Y ECO:0000006 Pubmed:1730245 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: 1,2-dihexanoyl-sn-glycero-3-phosphocholine; Mutant: [M8L and M20L]-loop-deleted PLA2 AAP 2000000712 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 6000000 {1,2-dihexanoyl-sn-glycero-3-phosphocholine} (#8# loop deleted PLA2 <30>) <30> 6000000 nmol/min/mg 1,2-dihexanoyl-sn-glycero-3-phosphocholine Y Y ECO:0000006 Pubmed:1730245 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: 1,2-dihexanoyl-sn-glycero-3-phosphocholine; Mutant: loop deleted PLA2 AAP 2000000713 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #8# 4.3 {1,2-dihexanoyl-sn-glycero-3-phosphocholine} <30> 23000 nmol/min/mg 1,2-dihexanoyl-sn-glycero-3-phosphocholine Y Y ECO:0000006 Pubmed:1730245 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: 1,2-dihexanoyl-sn-glycero-3-phosphocholine AAP 2000000714 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 135000 {1,2-diheptanoyl-sn-glycero-3-phosphocholine} <30> 135000 nmol/min/mg 1,2-diheptanoyl-sn-glycero-3-phosphocholine Y Y ECO:0000006 Pubmed:1730245 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: 1,2-diheptanoyl-sn-glycero-3-phosphocholine AAP 2000000715 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/KM #8,10# 0.1 {1,2-dioctanoyl-sn-glycero-3-phosphoglycol} <30> 0.1 mM 1,2-dioctanoyl-sn-glycero-3-phosphoglycol 3.1.1.4 Y Y ECO:0000006 Pubmed:1730245 BRENDA <30> Franken, P.A.; van den Berg, L.; Huang, J.; Gunyuzlu, P.; Lugtigheid, R.B.; Verheij, H.M.; de Haas, G.H.: Purification and characterization of a mutant human platelet phospholipase A2 expressed in Escherichia coli. Eur. J. Biochem. (1992) 203, 89-98. {Pubmed:1730245}; PENTACON Notes: Request ChEBI ID: 1,2-dioctanoyl-sn-glycero-3-phosphoglycol AAP 12/7/2011 1111 2000000716 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/KM #8# 0.9 {1,2-dinonanoyl-sn-glycero-3-phosphocholine} <30> 0.9 mM 1,2-dinonanoyl-sn-glycero-3-phosphocholine 3.1.1.4 Y Y ECO:0000006 Pubmed:1730245 BRENDA <30> Franken, P.A.; van den Berg, L.; Huang, J.; Gunyuzlu, P.; Lugtigheid, R.B.; Verheij, H.M.; de Haas, G.H.: Purification and characterization of a mutant human platelet phospholipase A2 expressed in Escherichia coli. Eur. J. Biochem. (1992) 203, 89-98. {Pubmed:1730245}; PENTACON Notes: Request ChEBI ID: 1,2-dioctanoyl-sn-glycero-3-phosphocholine AAP 12/7/2011 1111 2000000717 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/KM #8# 0.2 {1,2-dioctanoyl-sn-glycero-3-phosphocholine} <30> 0.2 mM 1,2-dioctanoyl-sn-glycero-3-phosphocholine 3.1.1.4 Y Y ECO:0000006 Pubmed:1730245 BRENDA <30> Franken, P.A.; van den Berg, L.; Huang, J.; Gunyuzlu, P.; Lugtigheid, R.B.; Verheij, H.M.; de Haas, G.H.: Purification and characterization of a mutant human platelet phospholipase A2 expressed in Escherichia coli. Eur. J. Biochem. (1992) 203, 89-98. {Pubmed:1730245}; PENTACON Notes: Request ChEBI ID: 1,2-dioctanoyl-sn-glycero-3-phosphocholine AAP 12/7/2011 1111 2000000718 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/KM #8# 2.4 {1,2-dihexanoyl-sn-glycero-3-phosphocholine} (#8# [M8L and M20L]-loop-deleted PLA2 <30>) <30> 2.4 mM 1,2-dihexanoyl-sn-glycero-3-phosphocholine 3.1.1.4 #8# [M8L and M20L]-loop-deleted PLA2 <30> Y Y ECO:0000006 Pubmed:1730245 BRENDA <30> Franken, P.A.; van den Berg, L.; Huang, J.; Gunyuzlu, P.; Lugtigheid, R.B.; Verheij, H.M.; de Haas, G.H.: Purification and characterization of a mutant human platelet phospholipase A2 expressed in Escherichia coli. Eur. J. Biochem. (1992) 203, 89-98. {Pubmed:1730245}; PENTACON Notes: Request ChEBI ID: 1,2-dihexanoyl-sn-glycero-3-phosphocholine; Mutant: [M8L and M20L]-loop-deleted PLA2 AAP 12/7/2011 1111 2000000719 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/KM #8# 2.8 {1,2-dihexanoyl-sn-glycero-3-phosphocholine} (#8# loop deleted PLA2 <30>) <30> 2.8 mM 1,2-dihexanoyl-sn-glycero-3-phosphocholine 3.1.1.4 #8# loop deleted PLA2 <30> Y Y ECO:0000006 Pubmed:1730245 BRENDA <30> Franken, P.A.; van den Berg, L.; Huang, J.; Gunyuzlu, P.; Lugtigheid, R.B.; Verheij, H.M.; de Haas, G.H.: Purification and characterization of a mutant human platelet phospholipase A2 expressed in Escherichia coli. Eur. J. Biochem. (1992) 203, 89-98. {Pubmed:1730245}; PENTACON Notes: Request ChEBI ID: 1,2-dihexanoyl-sn-glycero-3-phosphocholine; Mutant: loop deleted PLA2 AAP 12/7/2011 1111 2000000720 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/KM #8# 4.3 {1,2-dihexanoyl-sn-glycero-3-phosphocholine} <30> 4.3 mM 1,2-dihexanoyl-sn-glycero-3-phosphocholine 3.1.1.4 Y Y ECO:0000006 Pubmed:1730245 BRENDA <30> Franken, P.A.; van den Berg, L.; Huang, J.; Gunyuzlu, P.; Lugtigheid, R.B.; Verheij, H.M.; de Haas, G.H.: Purification and characterization of a mutant human platelet phospholipase A2 expressed in Escherichia coli. Eur. J. Biochem. (1992) 203, 89-98. {Pubmed:1730245}; PENTACON Notes: Request ChEBI ID: 1,2-dihexanoyl-sn-glycero-3-phosphocholine AAP 12/7/2011 1111 2000000721 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/KM #8# 3.6 {1,2-diheptanoyl-sn-glycero-3-phosphocholine} <30> 3.6 mM 1,2-diheptanoyl-sn-glycero-3-phosphocholine 3.1.1.4 Y Y ECO:0000006 Pubmed:1730245 BRENDA <30> Franken, P.A.; van den Berg, L.; Huang, J.; Gunyuzlu, P.; Lugtigheid, R.B.; Verheij, H.M.; de Haas, G.H.: Purification and characterization of a mutant human platelet phospholipase A2 expressed in Escherichia coli. Eur. J. Biochem. (1992) 203, 89-98. {Pubmed:1730245}; PENTACON Notes: Request ChEBI ID: 1,2-diheptanoyl-sn-glycero-3-phosphocholine AAP 12/7/2011 1111 2000000722 Jenn P18054 239 ALOX12 Homo sapiens 9606 Comment/biophysicochemical properties/KM #15# 0.0072 {arachidonic acid} (#15# cytosolic hp-12LOX, pH 7.4, recombinant wild-type enzyme <67>) <67> 0.0072 mM arachidonic acid CHEBI:15843 1.13.11.31 #15# cytosolic hp-12LOX, pH 7.4, recombinant wild-type enzyme <67> Y Y ECO:0000033 Pubmed:18155727 BRENDA <67> Aleem, A.M.; Jankun, J.; Dignam, J.D.; Walther, M.; Kuehn, H.; Svergun, D.I.; Skrzypczak-Jankun, E.: Human platelet 12-lipoxygenase, new findings about its activity, membrane binding and low-resolution structure. J. Mol. Biol. (2008) 376, 193-209. {Pubmed:18155727} AAP 12/7/2011 1111 2000000723 Jenn P18054 239 ALOX12 Homo sapiens 9606 Comment/biophysicochemical properties/KM #15# 0.0087 {arachidonic acid} (#15# membrane hp-12LOX, pH 7.4, recombinant wild-type enzyme <67>) <67> 0.0087 mM arachidonic acid CHEBI:15843 1.13.11.31 #15# membrane hp-12LOX, pH 7.4, recombinant wild-type enzyme <67> Y Y ECO:0000033 Pubmed:18155727 BRENDA <67> Aleem, A.M.; Jankun, J.; Dignam, J.D.; Walther, M.; Kuehn, H.; Svergun, D.I.; Skrzypczak-Jankun, E.: Human platelet 12-lipoxygenase, new findings about its activity, membrane binding and low-resolution structure. J. Mol. Biol. (2008) 376, 193-209. {Pubmed:18155727} AAP 12/7/2011 1111 2000000724 Jenn Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #5# 0.07219 {1-palmitoyl-lysophosphatidylcholine}(#5# Vmax: 6364 nmol/min/mg protein <56>) <56> 0.07219 mM 1-palmitoyl-lysophosphatidylcholine 2.3.1.23 #5# Vmax: 6364 nmol/min/mg protein <56> Y Y ECO:0000006 Pubmed:18195019 BRENDA <56> Zhao, Y.; Chen, Y.Q.; Bonacci, T.M.; Bredt, D.S.; Li, S.; Bensch, W.R.; Moller, D.E.; Kowala, M.; Konrad, R.J.; Cao, G.: Identification and characterization of a major liver lysophosphatidylcholine acyltransferase. J. Biol. Chem. (2008) 283, 8258-8265. {Pubmed:18195019}; PENTACON Notes: Request ChEBI ID: 1-Palmitoyl-LPC AAP 12/7/2011 1111 2000000725 Jenn Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #5# 0.07219 {1-palmitoyl-lysophosphatidylcholine}(#5# Vmax: 6364 nmol/min/mg protein <56>) <56> 6364 nmol/min/mg 1-palmitoyl-lysophosphatidylcholine 2.3.1.23 #5# Vmax: 6364 nmol/min/mg protein <56> Y Y ECO:0000006 Pubmed:18195019 BRENDA <56> Zhao, Y.; Chen, Y.Q.; Bonacci, T.M.; Bredt, D.S.; Li, S.; Bensch, W.R.; Moller, D.E.; Kowala, M.; Konrad, R.J.; Cao, G.: Identification and characterization of a major liver lysophosphatidylcholine acyltransferase. J. Biol. Chem. (2008) 283, 8258-8265. {Pubmed:18195019}; PENTACON Notes: Request ChEBI ID: 1-Palmitoyl-LPC AAP 12/7/2011 1111 2000000726 Jenn Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #5# 0.07156 {Arachidonoyl-CoA} (#5# Vmax: 6247 nmol/min/mg protein <56>) <56> 0.07156 mM Arachidonoyl-CoA CHEBI:15514 2.3.1.23 #5# Vmax: 6247 nmol/min/mg protein <56> Y Y ECO:0000006 Pubmed:18195019 BRENDA <56> Zhao, Y.; Chen, Y.Q.; Bonacci, T.M.; Bredt, D.S.; Li, S.; Bensch, W.R.; Moller, D.E.; Kowala, M.; Konrad, R.J.; Cao, G.: Identification and characterization of a major liver lysophosphatidylcholine acyltransferase. J. Biol. Chem. (2008) 283, 8258-8265. {Pubmed:18195019} AAP 12/7/2011 1111 2000000727 Jenn Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #5# 0.07156 {Arachidonoyl-CoA} (#5# Vmax: 6247 nmol/min/mg protein <56>) <56> 6247 nmol/min/mg Arachidonoyl-CoA CHEBI:15514 2.3.1.23 #5# Vmax: 6247 nmol/min/mg protein <56> Y Y ECO:0000006 Pubmed:18195019 BRENDA <56> Zhao, Y.; Chen, Y.Q.; Bonacci, T.M.; Bredt, D.S.; Li, S.; Bensch, W.R.; Moller, D.E.; Kowala, M.; Konrad, R.J.; Cao, G.: Identification and characterization of a major liver lysophosphatidylcholine acyltransferase. J. Biol. Chem. (2008) 283, 8258-8265. {Pubmed:18195019} AAP 12/7/2011 1111 2000000728 Jenn Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #5# 0.2014 {linoleoyl-CoA} (#5# Vmax: 18148 nmol/min/mg protein <56>) <56> 0.2014 mM linoleoyl-CoA CHEBI:15530 2.3.1.23 #5# Vmax: 18148 nmol/min/mg protein <56> Y Y ECO:0000006 Pubmed:18195019 BRENDA <56> Zhao, Y.; Chen, Y.Q.; Bonacci, T.M.; Bredt, D.S.; Li, S.; Bensch, W.R.; Moller, D.E.; Kowala, M.; Konrad, R.J.; Cao, G.: Identification and characterization of a major liver lysophosphatidylcholine acyltransferase. J. Biol. Chem. (2008) 283, 8258-8265. {Pubmed:18195019} AAP 12/7/2011 1111 2000000729 Jenn Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #5# 0.2014 {linoleoyl-CoA} (#5# Vmax: 18148 nmol/min/mg protein <56>) <56> 18148 nmol/min/mg linoleoyl-CoA CHEBI:15530 2.3.1.23 #5# Vmax: 18148 nmol/min/mg protein <56> Y Y ECO:0000006 Pubmed:18195019 BRENDA <56> Zhao, Y.; Chen, Y.Q.; Bonacci, T.M.; Bredt, D.S.; Li, S.; Bensch, W.R.; Moller, D.E.; Kowala, M.; Konrad, R.J.; Cao, G.: Identification and characterization of a major liver lysophosphatidylcholine acyltransferase. J. Biol. Chem. (2008) 283, 8258-8265. {Pubmed:18195019} AAP 12/7/2011 1111 2000000730 Jenn Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #5# 0.07268 {oleoyl-CoA} (#5# Vmax: 4698 nmol/min/mg protein <56>) <56> 0.07268 mM oleoyl-CoA CHEBI:15534 2.3.1.23 #5# Vmax: 4698 nmol/min/mg protein <56> Y Y ECO:0000006 Pubmed:18195019 BRENDA <56> Zhao, Y.; Chen, Y.Q.; Bonacci, T.M.; Bredt, D.S.; Li, S.; Bensch, W.R.; Moller, D.E.; Kowala, M.; Konrad, R.J.; Cao, G.: Identification and characterization of a major liver lysophosphatidylcholine acyltransferase. J. Biol. Chem. (2008) 283, 8258-8265. {Pubmed:18195019} AAP 12/7/2011 1111 2000000731 Jenn Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #5# 0.07268 {oleoyl-CoA} (#5# Vmax: 4698 nmol/min/mg protein <56>) <56> 4698 nmol/min/mg oleoyl-CoA CHEBI:15534 2.3.1.23 #5# Vmax: 4698 nmol/min/mg protein <56> Y Y ECO:0000006 Pubmed:18195019 BRENDA <56> Zhao, Y.; Chen, Y.Q.; Bonacci, T.M.; Bredt, D.S.; Li, S.; Bensch, W.R.; Moller, D.E.; Kowala, M.; Konrad, R.J.; Cao, G.: Identification and characterization of a major liver lysophosphatidylcholine acyltransferase. J. Biol. Chem. (2008) 283, 8258-8265. {Pubmed:18195019} AAP 12/7/2011 1111 2000000732 Jenn Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #5# 0.04129 {palmitoyl-CoA} (#5# Vmax: 1782 nmol/min/mg protein <56>) <56> 0.04129 mM palmitoyl-CoA CHEBI:15525 2.3.1.23 #5# Vmax: 1782 nmol/min/mg protein <56> Y Y ECO:0000006 Pubmed:18195019 BRENDA <56> Zhao, Y.; Chen, Y.Q.; Bonacci, T.M.; Bredt, D.S.; Li, S.; Bensch, W.R.; Moller, D.E.; Kowala, M.; Konrad, R.J.; Cao, G.: Identification and characterization of a major liver lysophosphatidylcholine acyltransferase. J. Biol. Chem. (2008) 283, 8258-8265. {Pubmed:18195019} AAP 12/7/2011 1111 2000000733 Jenn Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #5# 0.04129 {palmitoyl-CoA} (#5# Vmax: 1782 nmol/min/mg protein <56>) <56> 1782 nmol/min/mg palmitoyl-CoA CHEBI:15525 2.3.1.23 #5# Vmax: 1782 nmol/min/mg protein <56> Y Y ECO:0000006 Pubmed:18195019 BRENDA <56> Zhao, Y.; Chen, Y.Q.; Bonacci, T.M.; Bredt, D.S.; Li, S.; Bensch, W.R.; Moller, D.E.; Kowala, M.; Konrad, R.J.; Cao, G.: Identification and characterization of a major liver lysophosphatidylcholine acyltransferase. J. Biol. Chem. (2008) 283, 8258-8265. {Pubmed:18195019} AAP 12/7/2011 1111 2000000734 Jenn Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/KM #5# 0.03565 {stearoyl-CoA} (#5# Vmax: 996 nmol/min/mg protein <56>) <56> 0.03565 mM stearoyl-CoA CHEBI:15541 2.3.1.23 #5# Vmax: 996 nmol/min/mg protein <56> Y Y ECO:0000006 Pubmed:18195019 BRENDA <56> Zhao, Y.; Chen, Y.Q.; Bonacci, T.M.; Bredt, D.S.; Li, S.; Bensch, W.R.; Moller, D.E.; Kowala, M.; Konrad, R.J.; Cao, G.: Identification and characterization of a major liver lysophosphatidylcholine acyltransferase. J. Biol. Chem. (2008) 283, 8258-8265. {Pubmed:18195019} AAP 12/7/2011 1111 2000000735 Jenn Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #5# 0.03565 {stearoyl-CoA} (#5# Vmax: 996 nmol/min/mg protein <56>) <56> 996 nmol/min/mg stearoyl-CoA CHEBI:15541 2.3.1.23 #5# Vmax: 996 nmol/min/mg protein <56> Y Y ECO:0000006 Pubmed:18195019 BRENDA <56> Zhao, Y.; Chen, Y.Q.; Bonacci, T.M.; Bredt, D.S.; Li, S.; Bensch, W.R.; Moller, D.E.; Kowala, M.; Konrad, R.J.; Cao, G.: Identification and characterization of a major liver lysophosphatidylcholine acyltransferase. J. Biol. Chem. (2008) 283, 8258-8265. {Pubmed:18195019} AAP 12/7/2011 1111 2000000736 Chandra P19440 2678 GGT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 12.4 {Glycylglycine} <45> 12.4 mM Glycylglycine CHEBI:17201 L-Glutamic acid gamma-(4-nitroanilide) 2.3.2.2 Y Y ECO:0000006 Pubmed:18197 BRENDA <45> Huseby, N.: Purification and some properties of gamma-glutamyltransferase from human liver. Biochim. Biophys. Acta (1977) 483, 46-56. {Pubmed:18197}; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855 AAP 12/7/2011 1111 2000000737 Chandra P19440 2678 GGT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.81 {L-Glu-4-nitroanilide} <45> 0.81 mM L-Glutamic acid gamma-(4-nitroanilide) Glycylglycine CHEBI:17201 2.3.2.2 Y Y ECO:0000006 Pubmed:18197 BRENDA <45> Huseby, N.: Purification and some properties of gamma-glutamyltransferase from human liver. Biochim. Biophys. Acta (1977) 483, 46-56. {Pubmed:18197}; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855 AAP 12/7/2011 1111 2000000738 Chandra P19440 2678 GGT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1.5 {L-Glu-4-nitroanilide} (#6# recombinant wild-type <65>; #6# bile enzyme <46>) <46,65> 1.5 mM L-Glutamic acid gamma-(4-nitroanilide) 2.3.2.2 #6# recombinant wild-type <65>; #6# bile enzyme <46> Y Y ECO:0000006 Pubmed:18198 BRENDA <46> Indirani, N.; Hill, P.G.: Partial purification and some properties of gamma-glutamyl transpeptidase from human bile. Biochim. Biophys. Acta (1977) 483, 57-62. {Pubmed:18198}; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855; Enzyme was purified from bile and not recombinant AAP 12/7/2011 1111 2000000739 Jodi P18054 239 ALOX12 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.003 {5,8,11,14,17-eicosapentaenoic acid} <2> 0.003 mM all-cis-5,8,11,14,17-icosapentaenoic acid CHEBI:28364 1.13.11.31 Y Y ECO:0000006 Pubmed:1851637 BRENDA <2> Hada, T.; Ueda, N.; Takahashi, Y.; Yamamoto, S.: Catalytic properties of human platelet 12-lipoxygenase as compared with the enzymes of other origins. Biochim. Biophys. Acta (1991) 1083, 89-93. {Pubmed:1851637} (c) AAP 12/7/2011 1111 2000000740 Jodi P18054 239 ALOX12 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.0035 {8,11,14-Eicosatrienoic acid} <2> 0.0035 mM all-cis-icosa-8,11,14-trienoic acid CHEBI:53486 1.13.11.31 Y Y ECO:0000006 Pubmed:1851637 BRENDA <2> Hada, T.; Ueda, N.; Takahashi, Y.; Yamamoto, S.: Catalytic properties of human platelet 12-lipoxygenase as compared with the enzymes of other origins. Biochim. Biophys. Acta (1991) 1083, 89-93. {Pubmed:1851637} (c) AAP 12/7/2011 1111 2000000741 Jodi P18054 239 ALOX12 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.008 {arachidonic acid} <2> 0.008 mM arachidonic acid CHEBI:15843 1.13.11.31 Y Y ECO:0000006 Pubmed:1851637 BRENDA <2> Hada, T.; Ueda, N.; Takahashi, Y.; Yamamoto, S.: Catalytic properties of human platelet 12-lipoxygenase as compared with the enzymes of other origins. Biochim. Biophys. Acta (1991) 1083, 89-93. {Pubmed:1851637} (c) AAP 12/7/2011 1111 2000000742 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 10.8 {L-alanine-4-nitroanilide} <67> 10.8 mM alanine-4-nitroanilide 3.3.2.6 Y Y ECO:0000033 Pubmed:18539590 BRENDA <67> Bauvois, C.; Jacquamet, L.; Huston, A.L.; Borel, F.; Feller, G.; Ferrer, J.L.: Crystal structure of the cold-active aminopeptidase from Colwellia psychrerythraea, a close structural homologue of the human bifunctional leukotriene A4 hydrolase. J. Biol. Chem. (2008) 283, 23315-23325. {Pubmed:18539590}; PENTACON Notes: Request ChEBI ID: alanine-4-nitroanilide; Pubchem ID: CID 150936 AAP 12/7/2011 1111 2000000743 Jodi P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.0025 {arachidonic acid} (#2# 13,13-dideuterated arachidonic acid, pH 7.5, 25°C, recombinant isozyme 15-hLO-1 <72>) <72> 0.0025 mM arachidonic acid CHEBI:15843 1.13.11.33 #2# 13,13-dideuterated arachidonic acid, pH 7.5, 25°C, recombinant isozyme 15-hLO-1 <72> Y Y ECO:0000006 Pubmed:18547056 BRENDA <72> Jacquot, C.; Wecksler, A.T.; McGinley, C.M.; Segraves, E.N.; Holman, T.R.; van der Donk, W.A.: Isotope sensitive branching and kinetic isotope effects in the reaction of deuterated arachidonic acids with human 12- and 15-lipoxygenases. Biochemistry (2008) 47, 7295-7303. {Pubmed:18547056} AAP 12/7/2011 1111 2000000744 Jodi P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.0037 {arachidonic acid} (#2# unlabeled substrate, pH 7.5, 25°C, recombinant isozyme 15-hLO-1 <72>) <72> 0.0037 mM arachidonic acid CHEBI:15843 1.13.11.33 #2# unlabeled substrate, pH 7.5, 25°C, recombinant isozyme 15-hLO-1 <72> Y Y ECO:0000006 Pubmed:18547056 BRENDA <72> Jacquot, C.; Wecksler, A.T.; McGinley, C.M.; Segraves, E.N.; Holman, T.R.; van der Donk, W.A.: Isotope sensitive branching and kinetic isotope effects in the reaction of deuterated arachidonic acids with human 12- and 15-lipoxygenases. Biochemistry (2008) 47, 7295-7303. {Pubmed:18547056} AAP 12/7/2011 1111 2000000745 Jodi P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.0034 {arachidonic acid} (#2# 10,10-dideuterated arachidonic acid, pH 7.5, 25°C, recombinant isozyme 15-hLO-1 <72>) <72> 0.0034 mM arachidonic acid CHEBI:15843 1.13.11.33 #2# 10,10-dideuterated arachidonic acid, pH 7.5, 25°C, recombinant isozyme 15-hLO-1 <72> Y Y ECO:0000006 Pubmed:18547056 BRENDA <72> Jacquot, C.; Wecksler, A.T.; McGinley, C.M.; Segraves, E.N.; Holman, T.R.; van der Donk, W.A.: Isotope sensitive branching and kinetic isotope effects in the reaction of deuterated arachidonic acids with human 12- and 15-lipoxygenases. Biochemistry (2008) 47, 7295-7303. {Pubmed:18547056} AAP 12/7/2011 1111 2000000746 Jodi P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.0028 {arachidonic acid} (#2# 10,10,13,13-tetradeuterated arachidonic acid, pH 7.5, 25°C, recombinant isozyme 15-hLO-1 <72>) <72> 0.0028 mM arachidonic acid CHEBI:15843 1.13.11.33 #2# 10,10,13,13-tetradeuterated arachidonic acid, pH 7.5, 25°C, recombinant isozyme 15-hLO-1 <72> Y Y ECO:0000006 Pubmed:18547056 BRENDA <72> Jacquot, C.; Wecksler, A.T.; McGinley, C.M.; Segraves, E.N.; Holman, T.R.; van der Donk, W.A.: Isotope sensitive branching and kinetic isotope effects in the reaction of deuterated arachidonic acids with human 12- and 15-lipoxygenases. Biochemistry (2008) 47, 7295-7303. {Pubmed:18547056} AAP 12/7/2011 1111 2000000747 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0521 {15-ketoprostaglandin E1} (#4# at pH 7.0 <5>) <5> 0.0521 mM 15-keto prostaglandin E1 NADH CHEBI:16908 1.1.1.141 #4# at pH 7.0 <5> Y Y ECO:0000006 Pubmed:187123 BRENDA <5> Jabarak, J.; Braithwaite, S.S.: Kinetic studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Arch. Biochem. Biophys. (1976) 177, 245-254. {Pubmed:187123}; PENTACON Notes: Request ChEBI ID: 15-keto Prostaglandin E1; Pubchem ID: CID 440424 AAP 12/7/2011 1111 2000000748 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0156 {NADH} (#4# at pH 7.0, + 15-keto-PGE1 <5>; #4# at pH 7.0<5>) <5> 0.0156 mM NADH CHEBI:16908 15-keto prostaglandin E1 1.1.1.141 #4# at pH 7.0, + 15-keto-PGE1 <5>; #4# at pH 7.0, + 15-ketoprostaglandin E2 <5> Y Y ECO:0000006 Pubmed:187123 BRENDA <5> Jabarak, J.; Braithwaite, S.S.: Kinetic studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Arch. Biochem. Biophys. (1976) 177, 245-254. {Pubmed:187123}; PENTACON Notes: Request ChEBI ID: 15-keto Prostaglandin E1; Pubchem ID: CID 440424 AAP 12/7/2011 1111 2000000749 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0528 {15-Ketoprostaglandin E2} (#4# at pH 7.0 <5>) <5> 0.0528 mM 15-dehydro-prostaglandin E2 CHEBI:15547 NADH CHEBI:16908 1.1.1.141 #4# at pH 7.0 <5> Y Y ECO:0000006 Pubmed:187123 BRENDA <5> Jabarak, J.; Braithwaite, S.S.: Kinetic studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Arch. Biochem. Biophys. (1976) 177, 245-254. {Pubmed:187123} AAP 12/7/2011 1111 2000000750 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0266 {15-Ketoprostaglandin E2} (#4# at pH 9.0 <5>) <5> 0.0266 mM 15-dehydro-prostaglandin E2 CHEBI:15547 NADH CHEBI:16908 1.1.1.141 #4# at pH 9.0 <5> Y Y ECO:0000006 Pubmed:187123 BRENDA <5> Jabarak, J.; Braithwaite, S.S.: Kinetic studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Arch. Biochem. Biophys. (1976) 177, 245-254. {Pubmed:187123} AAP 12/7/2011 1111 2000000751 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.029 {NAD+} (#4# at pH 9.0, + prostaglandin E1 <5>) <5> 0.029 mM NAD(+) CHEBI:15846 prostaglandin E1 CHEBI:15544 1.1.1.141 #4# at pH 9.0, + prostaglandin E1 <5> Y Y ECO:0000006 Pubmed:187123 BRENDA <5> Jabarak, J.; Braithwaite, S.S.: Kinetic studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Arch. Biochem. Biophys. (1976) 177, 245-254. {Pubmed:187123} AAP 12/7/2011 1111 2000000752 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0227 {NAD+} (#4# at pH 9.0, + prostaglandin E2 <5>) <5> 0.0227 mM NAD(+) CHEBI:15846 prostaglandin E2 CHEBI:15551 1.1.1.141 #4# at pH 9.0, + prostaglandin E2 <5> Y Y ECO:0000006 Pubmed:187123 BRENDA <5> Jabarak, J.; Braithwaite, S.S.: Kinetic studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Arch. Biochem. Biophys. (1976) 177, 245-254. {Pubmed:187123} AAP 12/7/2011 1111 2000000753 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0308 {NAD+} (#4# at pH 7.0, + prostaglandin E1 <5>) <5> 0.0308 mM NAD(+) CHEBI:15846 prostaglandin E1 CHEBI:15544 1.1.1.141 #4# at pH 7.0, + prostaglandin E1 <5> Y Y ECO:0000006 Pubmed:187123 BRENDA <5> Jabarak, J.; Braithwaite, S.S.: Kinetic studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Arch. Biochem. Biophys. (1976) 177, 245-254. {Pubmed:187123} AAP 12/7/2011 1111 2000000754 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0284 {NAD+} (#4# at pH 7.0, + prostaglandin E2 <5>) <5> 0.0284 mM NAD(+) CHEBI:15846 prostaglandin E2 CHEBI:15551 1.1.1.141 #4# at pH 7.0, + prostaglandin E2 <5> Y Y ECO:0000006 Pubmed:187123 BRENDA <5> Jabarak, J.; Braithwaite, S.S.: Kinetic studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Arch. Biochem. Biophys. (1976) 177, 245-254. {Pubmed:187123} AAP 12/7/2011 1111 2000000755 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0594 {NADH} (#4# at pH 9.0, + 15-ketoprostaglandin E2 <5>) <5> 0.0594 mM NADH CHEBI:16908 15-dehydro-prostaglandin E2 CHEBI:15547 1.1.1.141 #4# at pH 9.0, + 15-ketoprostaglandin E2 <5> Y Y ECO:0000006 Pubmed:187123 BRENDA <5> Jabarak, J.; Braithwaite, S.S.: Kinetic studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Arch. Biochem. Biophys. (1976) 177, 245-254. {Pubmed:187123} AAP 12/7/2011 1111 2000000756 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0156 {NADH} (#4# at pH 7.0, + 15-ketoprostaglandin E2 <5>) <5> 0.0156 mM NADH CHEBI:16908 15-dehydro-prostaglandin E2 CHEBI:15547 1.1.1.141 #4# at pH 7.0, + 15-keto-PGE1 <5>; #4# at pH 7.0, + 15-ketoprostaglandin E2 <5> Y Y ECO:0000006 Pubmed:187123 BRENDA <5> Jabarak, J.; Braithwaite, S.S.: Kinetic studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Arch. Biochem. Biophys. (1976) 177, 245-254. {Pubmed:187123} AAP 12/7/2011 1111 2000000757 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0013 {prostaglandin E1} (#4# at pH 7.0 <5>) <5,12> 0.0013 mM prostaglandin E1 CHEBI:15544 NAD(+) CHEBI:15846 1.1.1.141 #4# at pH 7.0 <5> Y Y ECO:0000006 Pubmed:187123 BRENDA <5> Jabarak, J.; Braithwaite, S.S.: Kinetic studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Arch. Biochem. Biophys. (1976) 177, 245-254. {Pubmed:187123} AAP 12/7/2011 1111 2000000758 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0048 {prostaglandin E1} (#4# at pH 9.0 <5>) <5,12> 0.0048 mM prostaglandin E1 CHEBI:15544 NAD(+) CHEBI:15846 1.1.1.141 #4# at pH 9.0 <5> Y Y ECO:0000006 Pubmed:187123 BRENDA <5> Jabarak, J.; Braithwaite, S.S.: Kinetic studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Arch. Biochem. Biophys. (1976) 177, 245-254. {Pubmed:187123} AAP 12/7/2011 1111 2000000759 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0025 {prostaglandin E2} (#4# at pH 7.0 <5>) <5> 0.0025 mM prostaglandin E2 CHEBI:15551 NAD(+) CHEBI:15846 1.1.1.141 #4# at pH 7.0 <5> Y Y ECO:0000006 Pubmed:187123 BRENDA <5> Jabarak, J.; Braithwaite, S.S.: Kinetic studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Arch. Biochem. Biophys. (1976) 177, 245-254. {Pubmed:187123} AAP 12/7/2011 1111 2000000760 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0028 {prostaglandin E2} (#4# at pH 9.0 <5>) <5> 0.0028 mM prostaglandin E2 CHEBI:15551 NAD(+) CHEBI:15846 1.1.1.141 #4# at pH 9.0 <5> Y Y ECO:0000006 Pubmed:187123 BRENDA <5> Jabarak, J.; Braithwaite, S.S.: Kinetic studies on a 15-hydroxyprostaglandin dehydrogenase from human placenta. Arch. Biochem. Biophys. (1976) 177, 245-254. {Pubmed:187123} AAP 12/7/2011 1111 2000000761 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 1.9 {L-Ala-p-nitroanilide} (#4# mutant enzyme E296Q, 500 mM KCl in 250 mM Tris buffer (pH 7.5) <64>; #4# wild type enzyme, 500 mM KCl in 250 mM Tris buffer (pH 7.5) <64>) <64> 1.9 mM Alanine-4-nitroanilide 3.3.2.6 #4# mutant enzyme E296Q, 500 mM KCl in 250 mM Tris buffer (pH 7.5 Y Y ECO:0000006 Pubmed:18804029 BRENDA <64> Tholander, F.; Muroya, A.; Roques, B.P.; Fournie-Zaluski, M.C.; Thunnissen, M.M.; Haeggstroem, J.Z.: Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design. Chem. Biol. (2008) 15, 920-929. {Pubmed:18804029}; PENTACON Notes: wild type enzyme; Request ChEBI ID: alanine-4-nitroanilide; Pubchem ID: CID 150936 AAP 12/7/2011 1111 2000000762 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 1.5 {L-Arg-p-nitroanilide} (#4# wild type enzyme, 500 mM KCl in 250 mM Tris buffer (pH 7.5) <64>) <64> 1.5 mM L-Arg-p-nitroanilide 3.3.2.6 #4# wild type enzyme, 500 mM KCl in 250 mM Tris buffer (pH 7.5 Y Y ECO:0000006 Pubmed:18804029 BRENDA <64> Tholander, F.; Muroya, A.; Roques, B.P.; Fournie-Zaluski, M.C.; Thunnissen, M.M.; Haeggstroem, J.Z.: Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design. Chem. Biol. (2008) 15, 920-929. {Pubmed:18804029}; PENTACON Notes: Request ChEBI ID: L-Arg-p-nitroanilide; Pubchem ID: CID 7408187 AAP 12/7/2011 1111 2000000763 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 1.3 {Arg-Ser-Arg} (#4# wild type enzyme, 500 mM KCl in 250 mM Tris buffer (pH 7.5) <64>) <64> 1.3 mM Arg-Ser-Arg 3.3.2.6 #4# wild type enzyme, 500 mM KCl in 250 mM Tris buffer (pH 7.5 Y Y ECO:0000006 Pubmed:18804029 BRENDA <64> Tholander, F.; Muroya, A.; Roques, B.P.; Fournie-Zaluski, M.C.; Thunnissen, M.M.; Haeggstroem, J.Z.: Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design. Chem. Biol. (2008) 15, 920-929. {Pubmed:18804029}; PENTACON Notes: Request ChEBI ID: Arg-Ser-Arg AAP 12/7/2011 1111 2000000764 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 2.2 {L-Arg-p-nitroanilide} (#4# mutant enzyme E296Q, 500 mM KCl in 250 mM Tris buffer (pH 7.5) <64>) <64> 2.2 mM L-Arg-p-nitroanilide 3.3.2.6 #4# mutant enzyme E296Q, 500 mM KCl in 250 mM Tris buffer (pH 7.5 Y Y ECO:0000006 Pubmed:18804029 BRENDA <64> Tholander, F.; Muroya, A.; Roques, B.P.; Fournie-Zaluski, M.C.; Thunnissen, M.M.; Haeggstroem, J.Z.: Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design. Chem. Biol. (2008) 15, 920-929. {Pubmed:18804029}; PENTACON Notes: Mutant: E296Q; Request ChEBI ID: L-Arg-p-nitroanilide; Pubchem ID: CID 7408187 AAP 12/7/2011 1111 2000000765 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 1.9 {L-Ala-p-nitroanilide} (#4# mutant enzyme E296Q, 500 mM KCl in 250 mM Tris buffer (pH 7.5) <64>; #4# wild type enzyme, 500 mM KCl in 250 mM Tris buffer (pH 7.5) <64>) <64> 1.9 mM alanine-4-nitroanilide 3.3.2.6 #4# mutant enzyme E296Q, 500 mM KCl in 250 mM Tris buffer (pH 7.5 Y Y ECO:0000006 Pubmed:18804029 BRENDA <64> Tholander, F.; Muroya, A.; Roques, B.P.; Fournie-Zaluski, M.C.; Thunnissen, M.M.; Haeggstroem, J.Z.: Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design. Chem. Biol. (2008) 15, 920-929. {Pubmed:18804029}; PENTACON Notes: Mutant: E296Q; Request ChEBI ID: alanine-4-nitroanilide; Pubchem ID: CID 150936 AAP 12/7/2011 1111 2000000766 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 3 {L-Ala-p-nitroanilide} (#4# mutant enzyme D375A, 500 mM KCl in 250 mM Tris buffer (pH 7.5) <64>) <64> 3 mM alanine-4-nitroanilide 3.3.2.6 #4# mutant enzyme D375A, 500 mM KCl in 250 mM Tris buffer (pH 7.5 Y Y ECO:0000006 Pubmed:18804029 BRENDA <64> Tholander, F.; Muroya, A.; Roques, B.P.; Fournie-Zaluski, M.C.; Thunnissen, M.M.; Haeggstroem, J.Z.: Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design. Chem. Biol. (2008) 15, 920-929. {Pubmed:18804029}; PENTACON Notes: Mutant: D375A; Request ChEBI ID: alanine-4-nitroanilide; Pubchem ID: CID 150936 AAP 12/7/2011 1111 2000000767 Jodi P33261 1557 CYP2C19 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.018 {fenthion-sulfoxide} (#3# CYP2C19 <60>) <60> 0.018 mM fenthion-sulfoxide 1.14.14.1 #3# CYP2C19 <60> Y Y ECO:0000006 Pubmed:18845175 BRENDA <60> Leoni, C.; Buratti, F.M.; Testai, E.: The participation of human hepatic P450 isoforms, flavin-containing monooxygenases and aldehyde oxidase in the biotransformation of the insecticide fenthion. Toxicol. Appl. Pharmacol. (2008) 233, 343-352. {Pubmed:18845175}; PENTACON Notes: Request ChEBI ID: fenthion-sulfoxide; Pubchem ID: CID 19577 AAP 12/7/2011 1111 2000000768 Jodi P04798 1543 CYP1A1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.008 {fenthion} (#3# CYP1A1, sulfoxidation to fenthion-sulfoxide <60>) <60> 0.008 mM fenthion CHEBI:34761 1.14.14.1 #3# CYP1A1, sulfoxidation to fenthion-sulfoxide <60> Y Y ECO:0000006 Pubmed:18845175 BRENDA <60> Leoni, C.; Buratti, F.M.; Testai, E.: The participation of human hepatic P450 isoforms, flavin-containing monooxygenases and aldehyde oxidase in the biotransformation of the insecticide fenthion. Toxicol. Appl. Pharmacol. (2008) 233, 343-352. {Pubmed:18845175} AAP 12/7/2011 1111 2000000769 Jodi P05177 1544 CYP1A2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #62# 0.0016 {fenthion} (#62# desulfuration by recombinant human CYPs to fenthion-oxon <60>) <60> 0.0016 mM fenthion CHEBI:34761 1.14.14.1 #62# desulfuration by recombinant human CYPs to fenthion-oxon <60> Y Y ECO:0000006 Pubmed:18845175 BRENDA <60> Leoni, C.; Buratti, F.M.; Testai, E.: The participation of human hepatic P450 isoforms, flavin-containing monooxygenases and aldehyde oxidase in the biotransformation of the insecticide fenthion. Toxicol. Appl. Pharmacol. (2008) 233, 343-352. {Pubmed:18845175} AAP 12/7/2011 1111 2000000770 Jodi P05177 1544 CYP1A2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #62# 0.0022 {fenthion} (#62# sulfoxidation to fenthion-sulfoxide <60>) <60> 0.0022 mM fenthion CHEBI:34761 1.14.14.1 #62# sulfoxidation to fenthion-sulfoxide <60> Y Y ECO:0000006 Pubmed:18845175 BRENDA <60> Leoni, C.; Buratti, F.M.; Testai, E.: The participation of human hepatic P450 isoforms, flavin-containing monooxygenases and aldehyde oxidase in the biotransformation of the insecticide fenthion. Toxicol. Appl. Pharmacol. (2008) 233, 343-352. {Pubmed:18845175} AAP 12/7/2011 1111 2000000771 Jodi P20813 1555 CYP2B6 Homo sapiens 9606 Comment/biophysicochemical properties/KM #64# 0.01 {fenthion} (#64# sulfoxidation to fenthion-sulfoxide <60>) <60> 0.01 mM fenthion CHEBI:34761 1.14.14.1 #64# sulfoxidation to fenthion-sulfoxide <60> Y Y ECO:0000006 Pubmed:18845175 BRENDA <60> Leoni, C.; Buratti, F.M.; Testai, E.: The participation of human hepatic P450 isoforms, flavin-containing monooxygenases and aldehyde oxidase in the biotransformation of the insecticide fenthion. Toxicol. Appl. Pharmacol. (2008) 233, 343-352. {Pubmed:18845175} AAP 12/7/2011 1111 2000000772 Jodi P20813 1555 CYP2B6 Homo sapiens 9606 Comment/biophysicochemical properties/KM #64# 0.0027 {fenthion} (#64# desulfuration by recombinant human CYPs to fenthion-oxon <60>) <60> 0.0027 mM fenthion CHEBI:34761 1.14.14.1 #64# desulfuration by recombinant human CYPs to fenthion-oxon <60> Y Y ECO:0000006 Pubmed:18845175 BRENDA <60> Leoni, C.; Buratti, F.M.; Testai, E.: The participation of human hepatic P450 isoforms, flavin-containing monooxygenases and aldehyde oxidase in the biotransformation of the insecticide fenthion. Toxicol. Appl. Pharmacol. (2008) 233, 343-352. {Pubmed:18845175} AAP 12/7/2011 1111 2000000773 Jodi P33261 1557 CYP2C19 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0024 {fenthion} (#3# CYP2C19, desulfuration by recombinant human CYPs to fenthion-oxon <60>) <60> 0.0024 mM fenthion CHEBI:34761 1.14.14.1 #3# CYP2C19, desulfuration by recombinant human CYPs to fenthion-oxon <60> Y Y ECO:0000006 Pubmed:18845175 BRENDA <60> Leoni, C.; Buratti, F.M.; Testai, E.: The participation of human hepatic P450 isoforms, flavin-containing monooxygenases and aldehyde oxidase in the biotransformation of the insecticide fenthion. Toxicol. Appl. Pharmacol. (2008) 233, 343-352. {Pubmed:18845175} AAP 12/7/2011 1111 2000000774 Jodi P33261 1557 CYP2C19 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0044 {fenthion} (#3# CYP2C19, sulfoxidation to fenthion-sulfoxide <60>) <60> 0.0044 mM fenthion CHEBI:34761 1.14.14.1 #3# CYP2C19, sulfoxidation to fenthion-sulfoxide <60> Y Y ECO:0000006 Pubmed:18845175 BRENDA <60> Leoni, C.; Buratti, F.M.; Testai, E.: The participation of human hepatic P450 isoforms, flavin-containing monooxygenases and aldehyde oxidase in the biotransformation of the insecticide fenthion. Toxicol. Appl. Pharmacol. (2008) 233, 343-352. {Pubmed:18845175} AAP 12/7/2011 1111 2000000775 Jodi P11712 1559 CYP2C9 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.012 {fenthion} (#3# CYP2C9, desulfuration by recombinant human CYPs to fenthion-oxon <60>) <60> 0.012 mM fenthion CHEBI:34761 1.14.14.1 #3# CYP2C9, desulfuration by recombinant human CYPs to fenthion-oxon <60> Y Y ECO:0000006 Pubmed:18845175 BRENDA <60> Leoni, C.; Buratti, F.M.; Testai, E.: The participation of human hepatic P450 isoforms, flavin-containing monooxygenases and aldehyde oxidase in the biotransformation of the insecticide fenthion. Toxicol. Appl. Pharmacol. (2008) 233, 343-352. {Pubmed:18845175} AAP 12/7/2011 1111 2000000776 Jodi P11712 1559 CYP2C9 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.006 {fenthion} (#3# CYP2C9, sulfoxidation to fenthion-sulfoxide <60>) <60> 0.006 mM fenthion CHEBI:34761 1.14.14.1 #3# CYP2C9, sulfoxidation to fenthion-sulfoxide <60> Y Y ECO:0000006 Pubmed:18845175 BRENDA <60> Leoni, C.; Buratti, F.M.; Testai, E.: The participation of human hepatic P450 isoforms, flavin-containing monooxygenases and aldehyde oxidase in the biotransformation of the insecticide fenthion. Toxicol. Appl. Pharmacol. (2008) 233, 343-352. {Pubmed:18845175} AAP 12/7/2011 1111 2000000777 Jodi P08684 1576 CYP3A4 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.089 {fenthion} (#3# CYP3A4, desulfuration by recombinant human CYPs to fenthion-oxon <60>) <60> 0.089 mM fenthion CHEBI:34761 1.14.14.1 #3# CYP3A4, desulfuration by recombinant human CYPs to fenthion-oxon <60> Y Y ECO:0000006 Pubmed:18845175 BRENDA <60> Leoni, C.; Buratti, F.M.; Testai, E.: The participation of human hepatic P450 isoforms, flavin-containing monooxygenases and aldehyde oxidase in the biotransformation of the insecticide fenthion. Toxicol. Appl. Pharmacol. (2008) 233, 343-352. {Pubmed:18845175} AAP 12/7/2011 1111 2000000778 Jodi P08684 1576 CYP3A4 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.131 {fenthion} (#3# CYP3A4, sulfoxidation to fenthion-sulfoxide <60>) <60> 0.131 mM fenthion CHEBI:34761 1.14.14.1 #3# CYP3A4, sulfoxidation to fenthion-sulfoxide <60> Y Y ECO:0000006 Pubmed:18845175 BRENDA <60> Leoni, C.; Buratti, F.M.; Testai, E.: The participation of human hepatic P450 isoforms, flavin-containing monooxygenases and aldehyde oxidase in the biotransformation of the insecticide fenthion. Toxicol. Appl. Pharmacol. (2008) 233, 343-352. {Pubmed:18845175} AAP 12/7/2011 1111 2000000779 Jenn P18054 239 ALOX12 Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.0003 {arachidonate} <116> 0.0003 mM arachidonate CHEBI:32395 Y Y ECO:0000006 Pubmed:18972057 PENTACON Added by PENTACON AAP 2000000780 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.005 {arachidonate} <116> 0.005 mM arachidonate CHEBI:32395 1.13.11.33 Y Y ECO:0000006 Pubmed:18972057 BRENDA <116> Jacquot, C.; McGinley, C.M.; Plata, E.; Holman, T.R.; van der Donk, W.A.: Synthesis of 11-thialinoleic acid and 14-thialinoleic acid, inhibitors of soybean and human lipoxygenases. Org. Biomol. Chem. (2008) 6, 4242-4252. {Pubmed:18972057} AAP 12/7/2011 1111 2000000781 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.0062 {Linoleic acid} <116> 0.0062 mM Linoleic acid CHEBI:17351 1.13.11.33 Y Y ECO:0000006 Pubmed:18972057 BRENDA <116> Jacquot, C.; McGinley, C.M.; Plata, E.; Holman, T.R.; van der Donk, W.A.: Synthesis of 11-thialinoleic acid and 14-thialinoleic acid, inhibitors of soybean and human lipoxygenases. Org. Biomol. Chem. (2008) 6, 4242-4252. {Pubmed:18972057} AAP 12/7/2011 1111 2000000782 Chandra P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 21.4 {cholesterol} (#3# in cholesterol-lecithin vesicles <13>) <13> 21.4 mM cholesterol CHEBI:16113 2.3.1.43 #3# in cholesterol-lecithin vesicles <13> Y Y ECO:0000006 Pubmed:1901219 BRENDA <13> Collet, X.; Fielding, C.J.: Effects of inhibitors of N-linked oligosaccharide processing on the secretion, stability, and activity of lecithin:cholesterol acyltransferase. Biochemistry (1991) 30, 3228-3234. {Pubmed:1901219} AAP 12/7/2011 1111 2000000783 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.025 {3,5-dihydroxyphenylacetyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.025 mM 3,5-dihydroxyphenylacetyl-CoA 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545}; PENTACON Notes: Request ChEBI ID: 3,5-Dihydroxyphenylacetyl-CoA; Pubchem ID: CID 71448900 AAP 12/7/2011 1111 2000000784 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.01 {3,4-dihydroxyphenylacetyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.01 mM 3,4-dihydroxyphenylacetyl-CoA 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545}; PENTACON Notes: Request ChEBI ID: 3,4-dihydroxyphenylacetyl-CoA AAP 12/7/2011 1111 2000000785 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.041 {3-hydroxyphenylacetyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.041 mM 3-hydroxyphenylacetyl-CoA 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545}; PENTACON Notes: Request ChEBI ID: 3-HYDROXYPHENYLACETYL-COA, CID 25245569 AAP 12/7/2011 1111 2000000786 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.16 {3-hydroxyphenylacetyl-CoA} (#58# T69A mutant protein, pH7.5, 25°C <107>) <107> 0.16 mM 3-hydroxyphenylacetyl-CoA 3.1.2.20 #58# T69A mutant protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545}; PENTACON Notes: Mutant: T69A mutant protein, Request ChEBI ID: 3-HYDROXYPHENYLACETYL-COA; Pubchem ID: CID 25245569 AAP 12/7/2011 1111 2000000787 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.31 {3-hydroxyphenylacetyl-CoA} (#58# S83A mutant protein, pH7.5, 25°C <107>) <107> 0.31 mM 3-hydroxyphenylacetyl-CoA 3.1.2.20 #58# S83A mutant protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545}; PENTACON Notes: Mutant: S83A; Request ChEBI ID: 3-HYDROXYPHENYLACETYL-COA, CID 25245569 AAP 12/7/2011 1111 2000000788 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.3 {3-hydroxyphenylacetyl-CoA} (#58# N50A mutant protein, pH7.5, 25°C <107>) <107> 0.3 mM 3-hydroxyphenylacetyl-CoA 3.1.2.20 #58# N50A mutant protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545}; PENTACON Notes: Mutant: N50A mutant protein, Request ChEBI ID: 3-HYDROXYPHENYLACETYL-COA; Pubchem ID: CID 25245569 AAP 12/7/2011 1111 2000000789 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.12 {3-hydroxyphenylacetyl-CoA} (#58# K136A mutant protein, pH7.5, 25°C <107>) <107> 0.12 mM 3-hydroxyphenylacetyl-CoA 3.1.2.20 #58# K136A mutant protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545}; PENTACON Notes: Mutant: K136A; Request ChEBI ID: 3-HYDROXYPHENYLACETYL-COA, CID 25245569 AAP 12/7/2011 1111 2000000790 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.026 {3-hydroxyphenylacetyl-CoA} (#58# H56A mutant protein, pH7.5, 25°C <107>) <107> 0.026 mM 3-hydroxyphenylacetyl-CoA 3.1.2.20 #58# H56A mutant protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545}; PENTACON Notes: Mutant: H56A; Request ChEBI ID: 3-HYDROXYPHENYLACETYL-COA, CID 25245569 AAP 12/7/2011 1111 2000000791 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.9 {3-hydroxyphenylacetyl-CoA} (#58# H137A mutant protein, pH7.5, 25°C <107>) <107> 0.9 mM 3-hydroxyphenylacetyl-CoA 3.1.2.20 #58# H137A mutant protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545}; PENTACON Notes: Mutant: H137A; Request ChEBI ID: 3-HYDROXYPHENYLACETYL-COA, CID 25245569 AAP 12/7/2011 1111 2000000792 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.62 {3-hydroxyphenylacetyl-CoA} (#58# H134A mutant protein, pH7.5, 25°C <107>) <107> 0.62 mM 3-hydroxyphenylacetyl-CoA 3.1.2.20 #58# H134A mutant protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545}; PENTACON Notes: Mutant: H134A; Request ChEBI ID: 3-HYDROXYPHENYLACETYL-COA, CID 25245569 AAP 12/7/2011 1111 2000000793 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.36 {3-hydroxyphenylacetyl-CoA} (#58# D65N mutant protein, pH7.5, 25°C <107>) <107> 0.36 mM 3-hydroxyphenylacetyl-CoA 3.1.2.20 #58# D65N mutant protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545}; PENTACON Notes: Mutant: D65N; Request ChEBI ID: 3-HYDROXYPHENYLACETYL-COA, CID 25245569 AAP 12/7/2011 1111 2000000794 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.23 {3-hydroxyphenylacetyl-CoA} (#58# D65E mutant protein, pH7.5, 25°C <107>) <107> 0.23 mM 3-hydroxyphenylacetyl-CoA 3.1.2.20 #58# D65E mutant protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545}; PENTACON Notes: Mutant: D64E; Request ChEBI ID: 3-HYDROXYPHENYLACETYL-COA, CID 25245569 AAP 12/7/2011 1111 2000000795 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.22 {2-butenoyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.22 mM 2-butenoyl-CoA CHEBI:22961 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000796 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 2.9 {3-hydroxy-3-methylglutaryl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 2.9 mM 3-hydroxy-3-methylglutaryl-CoA CHEBI:11814 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000797 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.032 {3-Hydroxybenzoyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.032 mM 3-Hydroxybenzoyl-CoA CHEBI:15484 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000798 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.13 {4-chlorobenzoyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.13 mM 4-chlorobenzoyl-CoA CHEBI:15498 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000799 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.049 {4-hydroxyphenylacetyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.049 mM 4-hydroxyphenylacetyl-CoA CHEBI:28773 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000800 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.29 {acetyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.29 mM acetyl-CoA CHEBI:15351 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000801 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.02 {Arachidonoyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.02 mM Arachidonoyl-CoA CHEBI:15514 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000802 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.11 {beta-hydroxybutyryl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.11 mM beta-hydroxybutyryl-CoA CHEBI:37050 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000803 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.12 {beta-methylcrotonyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.12 mM beta-methylcrotonyl-CoA CHEBI:15486 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000804 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.18 {crotonyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.18 mM crotonyl-CoA CHEBI:15473 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000805 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.67 {Glutaryl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.67 mM Glutaryl-CoA CHEBI:15524 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000806 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.0099 {Lauroyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.0099 mM Lauroyl-CoA CHEBI:15521 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000807 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.31 {linoleoyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.31 mM linoleoyl-CoA CHEBI:15530 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000808 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.28 {malonyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.28 mM malonyl-CoA CHEBI:15531 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000809 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.21 {methylmalonyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.21 mM methylmalonyl-CoA CHEBI:16625 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000810 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.005 {myristoyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.005 mM myristoyl-CoA CHEBI:15532 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000811 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.009 {myristoyl-CoA} (#58# wild-type protein, pH7.5, 37°C <107>) <107> 0.009 mM myristoyl-CoA CHEBI:15532 3.1.2.20 #58# wild-type protein, pH7.5, 37°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000812 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.6 {n-Butyryl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.6 mM n-Butyryl-CoA CHEBI:15517 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000813 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.0049 {n-Decanoyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.0049 mM n-Decanoyl-CoA CHEBI:28493 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000814 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.07 {n-Hexanoyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.07 mM n-Hexanoyl-CoA CHEBI:27540 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000815 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.026 {n-Octanoyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.026 mM n-Octanoyl-CoA CHEBI:15533 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000816 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.016 {n-palmitoyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.016 mM n-palmitoyl-CoA CHEBI:15525 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000817 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.19 {n-propionyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.19 mM n-propionyl-CoA CHEBI:15539 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000818 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.009 {oleoyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.009 mM oleoyl-CoA CHEBI:15534 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000819 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.009 {Palmitoleoyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.009 mM Palmitoleoyl-CoA CHEBI:53152 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000820 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.24 {phenylacetyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.24 mM phenylacetyl-CoA CHEBI:15537 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000821 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.02 {stearoyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.02 mM stearoyl-CoA CHEBI:15541 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000822 Jenn Q9NPJ3 55856 ACOT13 Homo sapiens 9606 Comment/biophysicochemical properties/KM #58# 0.25 {tiglyl-CoA} (#58# wild-type protein, pH7.5, 25°C <107>) <107> 0.25 mM tiglyl-CoA CHEBI:15478 3.1.2.20 #58# wild-type protein, pH7.5, 25°C <107> Y Y ECO:0000006 Pubmed:19170545 BRENDA <107> Cao, J.; Xu, H.; Zhao, H.; Gong, W.; Dunaway-Mariano, D.: The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis. Biochemistry (2009) 48, 1293-1304. {Pubmed:19170545} AAP 12/7/2011 1111 2000000823 Jenn O15120 10555 AGPAT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0004 {acyl-CoA} (#4# pH 7.4, 37°C, recombinant <53>) <53> 0.0027 mM acyl-CoA CHEBI:17984 Y Y ECO:0000006 Pubmed:19318427 PENTACON Added by PENTACON; PENTACON Notes: pH 7.4, 37°C, recombinant AAP 2000000824 Jenn O15120 10555 AGPAT2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.002 {LPA} (#4# pH 7.4, 37°C, recombinant<53>) <53> 0.002 mM LPA CHEBI:52288 Y Y ECO:0000006 Pubmed:19318427 PENTACON Added by PENTACON; PENTACON Notes: pH 7.4, 37°C, recombinant AAP 2000000825 Christie Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/K0.5 #22# 0.214 {alpha-linolenoyl-CoA} (#22# 28°C, no cooperativity: Hill number 1.0 <64>) <64> 0.214 mM alpha-linolenoyl-CoA CHEBI:51985 2.3.1.23 #22# 28°C, no cooperativity: Hill number 1.0 <64> Y Y ECO:0000006 Pubmed:19351971 BRENDA <64> Jain, S.; Zhang, X.; Khandelwal, P.J.; Saunders, A.J.; Cummings, B.S.; Oelkers, P.: Characterization of human lysophospholipid acyltransferase 3. J. Lipid Res. (2009) 50, 1563-1570. {Pubmed:19351971} AAP 12/7/2011 1111 2000000826 Christie Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/K0.5 #22# 0.245 {Arachidonoyl-CoA} (#22# 37°C, cooperativity: Hill number 2.0 <64>) <64> 0.245 mM Arachidonoyl-CoA CHEBI:15514 2.3.1.23 #22# 37°C, cooperativity: Hill number 2.0 <64> Y Y ECO:0000006 Pubmed:19351971 BRENDA <64> Jain, S.; Zhang, X.; Khandelwal, P.J.; Saunders, A.J.; Cummings, B.S.; Oelkers, P.: Characterization of human lysophospholipid acyltransferase 3. J. Lipid Res. (2009) 50, 1563-1570. {Pubmed:19351971} AAP 12/7/2011 1111 2000000827 Christie Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/K0.5 #22# 0.0558 {Arachidonoyl-CoA} (#22# 28°C, cooperativity: Hill number 2.0 <64>) <64> 0.0558 mM Arachidonoyl-CoA CHEBI:15514 2.3.1.23 #22# 28°C, cooperativity: Hill number 2.0 <64> Y Y ECO:0000006 Pubmed:19351971 BRENDA <64> Jain, S.; Zhang, X.; Khandelwal, P.J.; Saunders, A.J.; Cummings, B.S.; Oelkers, P.: Characterization of human lysophospholipid acyltransferase 3. J. Lipid Res. (2009) 50, 1563-1570. {Pubmed:19351971} AAP 12/7/2011 1111 2000000828 Christie Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/K0.5 #22# 0.0131 {Lysophosphatidylcholine} (#22# cooperativity: Hill number 1.7 <64>) <64> 0.0131 mM lysophosphatidylcholine 16:0 CHEBI:64563 2.3.1.23 #22# cooperativity: Hill number 1.7 <64> Y Y ECO:0000006 Pubmed:19351971 BRENDA <64> Jain, S.; Zhang, X.; Khandelwal, P.J.; Saunders, A.J.; Cummings, B.S.; Oelkers, P.: Characterization of human lysophospholipid acyltransferase 3. J. Lipid Res. (2009) 50, 1563-1570. {Pubmed:19351971} AAP 12/7/2011 1111 2000000829 Christie Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/K0.5 #22# 0.0122 {oleoyl-CoA} (#22# 37°C, cooperativity: Hill number 1.6 <64>) <64> 0.0122 mM oleoyl-CoA CHEBI:15534 2.3.1.23 #22# 37°C, cooperativity: Hill number 1.6 <64> Y Y ECO:0000006 Pubmed:19351971 BRENDA <64> Jain, S.; Zhang, X.; Khandelwal, P.J.; Saunders, A.J.; Cummings, B.S.; Oelkers, P.: Characterization of human lysophospholipid acyltransferase 3. J. Lipid Res. (2009) 50, 1563-1570. {Pubmed:19351971} AAP 12/7/2011 1111 2000000830 Christie Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/K0.5 #22# 0.0465 {oleoyl-CoA} (#22# 28°C, cooperativity: Hill number 2.0 <64>) <64> 0.0465 mM oleoyl-CoA CHEBI:15534 2.3.1.23 #22# 28°C, cooperativity: Hill number 2.0 <64> Y Y ECO:0000006 Pubmed:19351971 BRENDA <64> Jain, S.; Zhang, X.; Khandelwal, P.J.; Saunders, A.J.; Cummings, B.S.; Oelkers, P.: Characterization of human lysophospholipid acyltransferase 3. J. Lipid Res. (2009) 50, 1563-1570. {Pubmed:19351971} AAP 12/7/2011 1111 2000000831 Christie Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/K0.5 #22# 0.0021 {stearoyl-CoA} (#22# 37°C, cooperativity: Hill number 3.7 <64>) <64> 0.0021 mM stearoyl-CoA CHEBI:15541 2.3.1.23 #22# 37°C, cooperativity: Hill number 3.7 <64> Y Y ECO:0000006 Pubmed:19351971 BRENDA <64> Jain, S.; Zhang, X.; Khandelwal, P.J.; Saunders, A.J.; Cummings, B.S.; Oelkers, P.: Characterization of human lysophospholipid acyltransferase 3. J. Lipid Res. (2009) 50, 1563-1570. {Pubmed:19351971} AAP 12/7/2011 1111 2000000832 Christie Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/K0.5 #22# 0.0051 {stearoyl-CoA} (#22# 28°C, cooperativity: Hill number 2.7 <64>) <64> 0.0051 mM stearoyl-CoA CHEBI:15541 2.3.1.23 #22# 28°C, cooperativity: Hill number 2.7 <64> Y Y ECO:0000006 Pubmed:19351971 BRENDA <64> Jain, S.; Zhang, X.; Khandelwal, P.J.; Saunders, A.J.; Cummings, B.S.; Oelkers, P.: Characterization of human lysophospholipid acyltransferase 3. J. Lipid Res. (2009) 50, 1563-1570. {Pubmed:19351971} AAP 12/7/2011 1111 2000000833 Christie Q6P1A2 10162 LPCAT3 Homo sapiens 9606 Comment/biophysicochemical properties/K0.5 #22# 0.232 {stearoyl-CoA} (#22# 37°C, cooperativity: Hill number 1.4 <64>) <64> 0.232 mM stearoyl-CoA CHEBI:15541 2.3.1.23 #22# 37°C, cooperativity: Hill number 1.4 <64> Y Y ECO:0000006 Pubmed:19351971 BRENDA <64> Jain, S.; Zhang, X.; Khandelwal, P.J.; Saunders, A.J.; Cummings, B.S.; Oelkers, P.: Characterization of human lysophospholipid acyltransferase 3. J. Lipid Res. (2009) 50, 1563-1570. {Pubmed:19351971} AAP 12/7/2011 1111 2000000834 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.022 {O2} (#2# with linoleic acid as substrate, in 25 mM Hepes buffer, pH 7.5, 25°C, in the presence of 12(S)-hydroperoxyeicosatetraenoic acid <103>) <103> 0.022 mM O2 CHEBI:15379 Linoleic acid CHEBI:17351 1.13.11.33 #2# with linoleic acid as substrate, in 25 mM Hepes buffer, pH 7.5, 25°C, in the presence of 12(S)-hydroperoxyeicosatetraenoic acid <103> Y Y ECO:0000006 Pubmed:19469483 BRENDA <103> Wecksler, A.T.; Jacquot, C.; van der Donk, W.A.; Holman, T.R.: Mechanistic investigations of human reticulocyte 15- and platelet 12-lipoxygenases with arachidonic acid. Biochemistry (2009) 48, 6259-6267. {Pubmed:19469483}; PENTACON Notes: Km is the concentration of oxygen consumed in the reaction, AA is the substrate AAP 12/7/2011 1111 2000000835 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.024 {O2} (#2# with arachidonic acid as substrate, in 25 mM Hepes buffer, pH 7.5, 25°C <103>) <103> 0.024 mM O2 CHEBI:15379 arachidonic acid CHEBI:15843 1.13.11.33 #2# with arachidonic acid as substrate, in 25 mM Hepes buffer, pH 7.5, 25°C <103> Y Y ECO:0000006 Pubmed:19469483 BRENDA <103> Wecksler, A.T.; Jacquot, C.; van der Donk, W.A.; Holman, T.R.: Mechanistic investigations of human reticulocyte 15- and platelet 12-lipoxygenases with arachidonic acid. Biochemistry (2009) 48, 6259-6267. {Pubmed:19469483}; PENTACON Notes: Km is the concentration of oxygen consumed in the reaction, AA is the substrate AAP 12/7/2011 1111 2000000836 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.0096 {O2} (#2# with linoleic acid as substrate, in 25 mM Hepes buffer, pH 7.5, 25°C <103>) <103> 0.0096 mM O2 CHEBI:15379 Linoleic acid CHEBI:17351 1.13.11.33 #2# with linoleic acid as substrate, in 25 mM Hepes buffer, pH 7.5, 25°C <103> Y Y ECO:0000006 Pubmed:19469483 BRENDA <103> Wecksler, A.T.; Jacquot, C.; van der Donk, W.A.; Holman, T.R.: Mechanistic investigations of human reticulocyte 15- and platelet 12-lipoxygenases with arachidonic acid. Biochemistry (2009) 48, 6259-6267. {Pubmed:19469483}; PENTACON Notes: Km is the concentration of oxygen consumed in the reaction, AA is the substrate AAP 12/7/2011 1111 2000000837 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.015 {O2} (#2# with arachidonic acid as substrate, in 25 mM Hepes buffer, pH 7.5, 25°C, in the presence of 12(S)-hydroperoxyeicosatetraenoic acid <103>) <103> 0.015 mM O2 CHEBI:15379 arachidonic acid CHEBI:15843 1.13.11.33 #2# with arachidonic acid as substrate, in 25 mM Hepes buffer, pH 7.5, 25°C, in the presence of 12(S)-hydroperoxyeicosatetraenoic acid <103> Y Y ECO:0000006 Pubmed:19469483 BRENDA <103> Wecksler, A.T.; Jacquot, C.; van der Donk, W.A.; Holman, T.R.: Mechanistic investigations of human reticulocyte 15- and platelet 12-lipoxygenases with arachidonic acid. Biochemistry (2009) 48, 6259-6267. {Pubmed:19469483}; PENTACON Notes: Km is the concentration of oxygen consumed in the reaction, AA is the substrate AAP 12/7/2011 1111 2000000838 Chandra P19440 2678 GGT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6,7# 1.09 {L-Glu-3-carboxy-4-nitroanilide} (#7# L-Cys-Gly, rat kidney enzyme <34>) <1,34> 1.09 mM L-Glu-3-carboxy-4-nitroanilide 2.3.2.2 #7# L-Cys-Gly, rat kidney enzyme <34> Y Y ECO:0000006 Pubmed:1978610 BRENDA <1> Yoshida, K.I.; Arai, K.; Kobayashi, N.; Saitoh, H.: Purification and properties of gamma-glutamyl transpeptidase from human testis. Andrologia (1990) 22, 239-246. {Pubmed:}; PENTACON Notes: Request ChEBI ID: gamma-glutamyl-3-carboxy-4-nitroanilide: CID 104545; Not a rat kidney enzyme as indicated in Secondary Source Notes, but a GGT isolated from human testis, results consistent with GGT1 AAP 12/7/2011 1111 2000000839 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 0.093 {arachidonic acid} <14> 0.093 nmol/min/mg arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:2459258 PENTACON Added by PENTACON AAP 2000000840 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 0.077 {Linoleic acid} <14> 0.077 nmol/min/mg Linoleic acid CHEBI:17351 Y Y ECO:0000006 Pubmed:2459258 PENTACON Added by PENTACON AAP 2000000841 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.0106 {arachidonic acid} <14> 0.0106 mM arachidonic acid CHEBI:15843 1.13.11.33 Y Y ECO:0000006 Pubmed:2459258 BRENDA <14> Burrall, B.A.; Cheung, M.; Chiu, A.; Goetzel, E.J.: Enzymatic properties of the 15-lipoxygenase of human cultured keratinocytes. J. Invest. Dermatol. (1988) 91, 294-297. {Pubmed:2459258} (c) AAP 12/7/2011 1111 2000000842 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.0095 {Linoleic acid} <14> 0.0095 mM Linoleic acid CHEBI:17351 1.13.11.33 Y Y ECO:0000006 Pubmed:2459258 BRENDA <14> Burrall, B.A.; Cheung, M.; Chiu, A.; Goetzel, E.J.: Enzymatic properties of the 15-lipoxygenase of human cultured keratinocytes. J. Invest. Dermatol. (1988) 91, 294-297. {Pubmed:2459258} (c) AAP 12/7/2011 1111 2000000843 Jenn P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/IC50 0.0005 {HgCl2} (#4# pH 7.8, 37°C <13>) <13> 0.0005 mM HgCl2 CHEBI:31823 leukotriene A4 CHEBI:15651 Y Y ECO:0000006 Pubmed:3038871 PENTACON Added by PENTACON; PENTACON Notes: pH 7.8, 37°C AAP 2000000844 Jenn P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3 {N-ethylmaleimide} (#4# pH 7.8, 37°C <13>) <13> 3 mM N-ethylmaleimide CHEBI:44485 leukotriene A4 CHEBI:15651 Y Y ECO:0000006 Pubmed:3038871 PENTACON Added by PENTACON; PENTACON Notes: pH 7.8, 37°C AAP 2000000845 Jenn P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/IC50 0.0007 {p-chloromercuribenzoic acid} (#4# pH 7.8, 37°C <13>) <13> 0.0007 mM p-chloromercuribenzoic acid CHEBI:28420 leukotriene A4 CHEBI:15651 Y Y ECO:0000006 Pubmed:3038871 PENTACON Added by PENTACON; PENTACON Notes: pH 7.8, 37°C AAP 2000000846 Jenn P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 2000-3000 {leukotriene A4} (#4# pH 7.8, 37°C <13>) <13> nmol/min/mg leukotriene A4 CHEBI:15651 Y Y ECO:0000006 Pubmed:3038871 PENTACON Added by PENTACON; PENTACON Notes: enzyme purified from two different sources; pH 7.8, 37°C AAP 2000000847 Jenn P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.013-0.014 {leukotriene A4} (#4# pH 7.8, 37°C <13>) <13> mM leukotriene A4 CHEBI:15651 3.3.2.6 #4# pH 7.8, 37°C <13> Y Y ECO:0000006 Pubmed:3038871 BRENDA <13> Ohishi, N.; Izumi, T.; Minami, M.; Kitamura, S.; Seyama, Y.; Ohkawa, S.; Terao, S.; Yotsumoto, H.; Takaku, F.; Shimizu, T.: Leukotriene A4 hydrolase in the human lung. Inactivation of the enzyme with leukotriene A4 isomers. J. Biol. Chem. (1987) 262, 10200-10205. {Pubmed:3038871}; PENTACON Notes: enzyme purified from two different sources AAP 12/7/2011 1111 2000000848 Jodi P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.063 {arachidonic acid} 0.063 mM arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:3070300 PENTACON Added by PENTACON AAP 2000000849 Jodi P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.077 {linoleic acid} 0.077 mM linoleic acid CHEBI:17351 Y Y ECO:0000006 Pubmed:3070300 PENTACON Added by PENTACON AAP 2000000850 Jodi P09917 240 ALOX5 Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.012 {arachidonic acid} <15> 0.012 mM arachidonic acid CHEBI:15843 ATP CHEBI:15422 1.13.11.34 Y Y ECO:0000006 Pubmed:3070300 BRENDA <15> Soberman, R.J.: 5- and 15(omega-6)-lipoxygenases from human polymorphonuclear leukocytes. Methods Enzymol. (1988) 163, 344-349. {Pubmed:3070300} (c) AAP 12/7/2011 1111 2000000851 Christie/Chandra P34913 2053 EPHX2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.055 {cis-2-methylstyrene oxide} (#6# cytosolic enzyme <12>) <12> 0.055 mM cis-2-methylstyrene oxide 3.3.2.10 #6# cytosolic enzyme <12> Y Y ECO:0000006 Pubmed:3169021 BRENDA <12> Schladt, L.; Thomas, H.; Hartmann, R.; Oesch, F.: Human liver cytosolic epoxide hydrolases. Eur. J. Biochem. (1988) 176, 715-723. {Pubmed:3169021} (c); PENTACON Notes: Request ChEBI ID:cis-2-methylstyrene oxide AAP 12/7/2011 1111 2000000852 Christie/Chandra P34913 2053 EPHX2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.089 {cis-1,2-dimethylstyrene oxide} (#6# cytosolic enzyme <12>) <12> 0.089 mM cis-1,2-dimethylstyrene oxide 3.3.2.10 #6# cytosolic enzyme <12> Y Y ECO:0000006 Pubmed:3169021 BRENDA <12> Schladt, L.; Thomas, H.; Hartmann, R.; Oesch, F.: Human liver cytosolic epoxide hydrolases. Eur. J. Biochem. (1988) 176, 715-723. {Pubmed:3169021} (c); PENTACON Notes: Request ChEBI ID:cis-1,2-dimethylstyrene oxide AAP 12/7/2011 1111 2000000853 Christie/Chandra P34913 2053 EPHX2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.358 {2,2-dimethylstyrene oxide} (#6# cytosolic enzyme <12>) <12> 0.358 mM 2,2-dimethylstyrene oxide 3.3.2.10 #6# cytosolic enzyme <12> Y Y ECO:0000006 Pubmed:3169021 BRENDA <12> Schladt, L.; Thomas, H.; Hartmann, R.; Oesch, F.: Human liver cytosolic epoxide hydrolases. Eur. J. Biochem. (1988) 176, 715-723. {Pubmed:3169021} (c) AAP 12/7/2011 1111 2000000854 Christie/Chandra P34913 2053 EPHX2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.517 {7,8-styrene oxide} (#6# cytosolic enzyme <12>) <12> 0.517 mM styrene oxide CHEBI:17907 3.3.2.10 #6# cytosolic enzyme <12> Y Y ECO:0000006 Pubmed:3169021 BRENDA <12> Schladt, L.; Thomas, H.; Hartmann, R.; Oesch, F.: Human liver cytosolic epoxide hydrolases. Eur. J. Biochem. (1988) 176, 715-723. {Pubmed:3169021} (c) AAP 12/7/2011 1111 2000000855 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 8.6 {arachidonic acid} <11> 8.6 nmol/min/mg arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:3337718 PENTACON Added by PENTACON; PENTACON Notes: 33°C, pH 7 AAP 2000000856 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.068 {arachidonic acid} <11> 0.068 mM arachidonic acid CHEBI:15843 1.13.11.33 Y Y ECO:0000006 Pubmed:3337718 BRENDA <11> Sigal, E.; Grunberger, D.; Cashman, J.R.; Craik, C.S.; Caughey, G.H.; Nadel, J.A.: Arachidonate 15-lipoxygenase from human eosinophil-enriched leukocytes: partial purification and properties. Biochem. Biophys. Res. Commun. (1988) 150, 376-383. {Pubmed:3337718} (c); PENTACON Notes: 33°C, pH 7 AAP 12/7/2011 1111 2000000857 Jenn P09917 240 ALOX5 Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.012 {Arachidonic acid} <15> 0.012 mM arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: ALOX5 prepared from single cell donor AAP 2000000858 Jenn P09917 240 ALOX5 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 1.72 {Arachidonic acid} <15> 1.72 nmol/min/mg arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: ALOX5 prepared from single cell donor AAP 2000000859 Jenn P09917 240 ALOX5 Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.023 {EPA} <15> 0.023 mM EPA CHEBI:36006 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: ALOX5 prepared from single cell donor AAP 2000000860 Jenn P09917 240 ALOX5 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 5.5 {EPA} <15> 5.5 nmol/min/mg EPA CHEBI:36006 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: ALOX5 prepared from single cell donor AAP 2000000861 Jenn P09917 240 ALOX5 Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.0175 {Arachidonic acid} <15> 0.0175 mM arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: ALOX5 prepared from multiple cell donors; pH 7.5 AAP 2000000862 Jenn P09917 240 ALOX5 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 5.6 {Arachidonic acid} <15> 5.6 nmol/min/mg arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: ALOX5 prepared from multiple cell donors; pH 7.5 AAP 2000000863 Jenn P09917 240 ALOX5 Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.0122 {Arachidonic acid} <15> 0.0122 mM arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: ALOX5 prepared from multiple cell donors AAP 2000000864 Jenn P09917 240 ALOX5 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 2.8 {Arachidonic acid} <15> 2.8 nmol/min/mg arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: ALOX5 prepared from multiple cell donors AAP 2000000865 Jenn P09917 240 ALOX5 Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.025 {EPA} <15> 0.025 mM EPA CHEBI:36006 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: ALOX5 prepared from multiple cell donors AAP 2000000866 Jenn P09917 240 ALOX5 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 5 {EPA} <15> 5 nmol/min/mg EPA CHEBI:36006 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: ALOX5 prepared from multiple cell donors AAP 2000000867 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 5.3 {arachidonic acid} <15> 5.3 nmol/min/mg arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: 22°C, pH 7.5. ALOX15 prepared from multiple cell donors AAP 2000000868 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 5.3 {arachidonic acid} <15> 5.3 nmol/min/mg arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: 22°C, pH 7.5. ALOX15 prepared from multiple cell donors AAP 2000000869 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 9.5 {Linoleic acid} <15> 9.5 nmol/min/mg Linoleic acid CHEBI:17351 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: 22°C, pH 7.5. ALOX15 prepared from multiple cell donors AAP 2000000870 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 10 {Linoleic acid} <15> 10 nmol/min/mg Linoleic acid CHEBI:17351 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: 22°C, pH 7.5. ALOX15 prepared from multiple cell donors AAP 2000000871 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.0634 {arachidonic acid} <15> 0.0634 mM arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: 22°C, pH 7.5. ALOX15 prepared from a single cell donor AAP 2000000872 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.083 {Linoleic acid} <15> 0.083 mM Linoleic acid CHEBI:17351 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: 22°C, pH 7.5. ALOX15 prepared from a single cell donor AAP 2000000873 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.0571 {arachidonic acid} <15> 0.0571 mM arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: 22°C, pH 6.5. ALOX15 prepared from a single cell donor AAP 2000000874 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 11.3 {arachidonic acid} <15> 11.3 nmol/min/mg arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: 22°C, pH 6.5. ALOX15 prepared from a single cell donor AAP 2000000875 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.0725 {Linoleic acid} <15> 0.0725 mM Linoleic acid CHEBI:17351 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: 22°C, pH 6.5. ALOX15 prepared from a single cell donor AAP 2000000876 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 30.8 {Linoleic acid} <15> 30.8 nmol/min/mg Linoleic acid CHEBI:17351 Y Y ECO:0000006 Pubmed:3920219 PENTACON Added by PENTACON; PENTACON Notes: 22°C, pH 6.5. ALOX15 prepared from a single cell donor AAP 2000000877 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.0631 {arachidonic acid} <15> 0.0631 mM arachidonic acid CHEBI:15843 1.13.11.33 Y Y ECO:0000006 Pubmed:3920219 BRENDA <15> Soberman, R.J.; Harper, T.W.; Betteridge, D.; Lewis, R.A.; Austen, K.F.: Characterization and separation of the arachidonic acid 5-lipoxygenase and linoleic acid omega-6 lipoxygenase (arachidonic acid 15-lipoxygenase) of human polymorphonuclear leukocytes. J. Biol. Chem. (1985) 260, 4508-4515. {Pubmed:3920219} (c); PENTACON Notes: 22°C, pH 7.5. ALOX15 prepared from multiple cell donors AAP 12/7/2011 1111 2000000878 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.0772 {Linoleic acid} <15> 0.0772 mM Linoleic acid CHEBI:17351 1.13.11.33 Y Y ECO:0000006 Pubmed:3920219 BRENDA <15> Soberman, R.J.; Harper, T.W.; Betteridge, D.; Lewis, R.A.; Austen, K.F.: Characterization and separation of the arachidonic acid 5-lipoxygenase and linoleic acid omega-6 lipoxygenase (arachidonic acid 15-lipoxygenase) of human polymorphonuclear leukocytes. J. Biol. Chem. (1985) 260, 4508-4515. {Pubmed:3920219} (c); PENTACON Notes: 22°C, pH 7.5. ALOX15 prepared from multiple cell donors AAP 12/7/2011 1111 2000000879 Chandra P19440 2678 GGT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 0.8 mM {gamma-glutamyl-p-nitroanilide} in the presence of glycylglycine (gamma-glutamyl acceptor); purified from kidney 0.8 mM gamma-L-Glutamyl-p-nitroanilide glycylglycine CHEBI:17201 Y Y ECO:0000006 Pubmed:4442 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: gamma-L-Glutamyl-p-nitroanilide: CID 16219428 AAP 2000000880 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.033 {Prostaglandin A1} <16> 0.033 mM Prostaglandin A1 CHEBI:15545 1.1.1.141 Y Y ECO:0000006 Pubmed:4822191 BRENDA <16> Schlegel, W.; Demers, L.M.; Hildebrandt-Stark, H.E.; Behrman, H.R.; Greep, R.O.: Partial purification of human placental 15-hydroxy-prostaglandin dehydrogenase: kinetic properties. Prostaglandins (1974) 5, 417-433. {Pubmed:4822191} AAP 12/7/2011 1111 2000000881 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.032 {Prostaglandin A2} <16> 0.032 mM Prostaglandin A2 CHEBI:27820 1.1.1.141 Y Y ECO:0000006 Pubmed:4822191 BRENDA <16> Schlegel, W.; Demers, L.M.; Hildebrandt-Stark, H.E.; Behrman, H.R.; Greep, R.O.: Partial purification of human placental 15-hydroxy-prostaglandin dehydrogenase: kinetic properties. Prostaglandins (1974) 5, 417-433. {Pubmed:4822191} AAP 12/7/2011 1111 2000000882 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.027 {prostaglandin E1} <16> 0.027 mM prostaglandin E1 CHEBI:15544 1.1.1.141 Y Y ECO:0000006 Pubmed:4822191 BRENDA <16> Schlegel, W.; Demers, L.M.; Hildebrandt-Stark, H.E.; Behrman, H.R.; Greep, R.O.: Partial purification of human placental 15-hydroxy-prostaglandin dehydrogenase: kinetic properties. Prostaglandins (1974) 5, 417-433. {Pubmed:4822191} AAP 12/7/2011 1111 2000000883 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.01 {prostaglandin E2} <16,24> 0.01 mM prostaglandin E2 CHEBI:15551 1.1.1.141 Y Y ECO:0000006 Pubmed:4822191 BRENDA <16> Schlegel, W.; Demers, L.M.; Hildebrandt-Stark, H.E.; Behrman, H.R.; Greep, R.O.: Partial purification of human placental 15-hydroxy-prostaglandin dehydrogenase: kinetic properties. Prostaglandins (1974) 5, 417-433. {Pubmed:4822191} AAP 12/7/2011 1111 2000000884 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.059 {prostaglandin F2alpha} <16> 0.059 mM prostaglandin F2alpha CHEBI:15553 1.1.1.141 Y Y ECO:0000006 Pubmed:4822191 BRENDA <16> Schlegel, W.; Demers, L.M.; Hildebrandt-Stark, H.E.; Behrman, H.R.; Greep, R.O.: Partial purification of human placental 15-hydroxy-prostaglandin dehydrogenase: kinetic properties. Prostaglandins (1974) 5, 417-433. {Pubmed:4822191} AAP 12/7/2011 1111 2000000885 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 1700 {leukotriene B4} 1700 nmol/min/mg leukotriene B4 CHEBI:15647 Y Y ECO:0000006 Pubmed:6490615 PENTACON Added by PENTACON; PENTACON Notes: 37°C AAP 2000000886 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 1100 {leukotriene B4} 1100 nmol/min/mg leukotriene B4 CHEBI:15647 Y Y ECO:0000006 Pubmed:6490615 PENTACON Added by PENTACON; PENTACON Notes: 2°C AAP 2000000887 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.022 {leukotriene A4} (#4# pH 7.7-8.0, 2°C <7>) <7> 0.022 mM leukotriene A4 CHEBI:15651 3.3.2.6 #4# pH 7.7-8.0, 2°C <7> Y Y ECO:0000006 Pubmed:6490615 BRENDA <7> Radmark, O.; Shimizu, T.; Jörnvall, H.; Samuelsson, B.: Leukotriene A4 hydrolase in human leukocytes. Purification and properties. J. Biol. Chem. (1984) 259, 12339-12345. {Pubmed:6490615} AAP 12/7/2011 1111 2000000888 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.023 {leukotriene A4} (#4# pH 7.7-8.0, 37°C <7>; #4# pH 8.0, 22°C, mutant Y378F <28,29>) <7,28,29> 0.023 mM leukotriene A4 CHEBI:15651 3.3.2.6 #4# pH 7.7-8.0, 37°C <7>; #4# pH 8.0, 22°C, mutant Y378F <28,29> Y Y ECO:0000006 Pubmed:6490615 BRENDA <7> Radmark, O.; Shimizu, T.; Jörnvall, H.; Samuelsson, B.: Leukotriene A4 hydrolase in human leukocytes. Purification and properties. J. Biol. Chem. (1984) 259, 12339-12345. {Pubmed:6490615} AAP 12/7/2011 1111 2000000889 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4,5# 0.02-0.03 {leukotriene A4} (#4,5# pH 7.7-7.8, 37°C <1,7>) <1,7> mM leukotriene A4 CHEBI:15651 3.3.2.6 #4,5# pH 7.7-7.8, 37°C <1,7> Y Y ECO:0000006 Pubmed:6490615 BRENDA <7> Radmark, O.; Shimizu, T.; Jörnvall, H.; Samuelsson, B.: Leukotriene A4 hydrolase in human leukocytes. Purification and properties. J. Biol. Chem. (1984) 259, 12339-12345. {Pubmed:6490615} AAP 12/7/2011 1111 2000000890 Christie P18054 239 ALOX12 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.024 {5,8,11,14,17-eicosapentaenoic acid} <22> 0.024 mM 5,8,11,14,17-eicosapentaenoic acid 1.13.11.31 Y Y ECO:0000006 Pubmed:6783111 BRENDA <22> Wallach, D.P.; Brown, V.R.: A novel preparation of human platelet lipoxygenase. Characteristics and inhibition by a variety of phenyl hydrazones and comparisons with other lipoxygenases. Biochim. Biophys. Acta (1981) 663, 361-372. {Pubmed:6783111} (c); PENTACON Notes: Request ChEBI ID: 5,8,11,14,17-eicosapentaenoic acid; Pubchem ID: CID 3209 AAP 12/7/2011 1111 2000000891 Christie P18054 239 ALOX12 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.079 {8,11,14-Eicosatrienoic acid} <22> 0.079 mM all-cis-icosa-8,11,14-trienoic acid CHEBI:53486 1.13.11.31 Y Y ECO:0000006 Pubmed:6783111 BRENDA <22> Wallach, D.P.; Brown, V.R.: A novel preparation of human platelet lipoxygenase. Characteristics and inhibition by a variety of phenyl hydrazones and comparisons with other lipoxygenases. Biochim. Biophys. Acta (1981) 663, 361-372. {Pubmed:6783111} (c) AAP 12/7/2011 1111 2000000892 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0013 {prostaglandin E1} (#4# at pH 7.0 <5>) <5,12> 0.0013 mM prostaglandin E1 CHEBI:15544 1.1.1.141 #4# at pH 7.0 <5> Y Y ECO:0000033 Pubmed:7132749 BRENDA <12> Jabarak, J.: Isolation and properties of an NAD+-dependent 15-hydroxyprostaglandin dehydrogenase from human placenta. Methods Enzymol. (1982) 86, 126-130. {Pubmed:7132749} (review) AAP 12/7/2011 1111 2000000893 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0048 {prostaglandin E1} (#4# at pH 9.0 <5>) <5,12> 0.0048 mM prostaglandin E1 CHEBI:15544 1.1.1.141 #4# at pH 9.0 <5> Y Y ECO:0000033 Pubmed:7132749 BRENDA <12> Jabarak, J.: Isolation and properties of an NAD+-dependent 15-hydroxyprostaglandin dehydrogenase from human placenta. Methods Enzymol. (1982) 86, 126-130. {Pubmed:7132749} (review) AAP 12/7/2011 1111 2000000894 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 3000 {Phosphatidylcholine} recombinant enzyme <19> 3000 nmol/min/mg Phosphatidylcholine CHEBI:49183 Y Y ECO:0000006 Pubmed:7798190 PENTACON Added by PENTACON; PENTACON Notes: recombinant enzyme AAP 2000000895 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 70000 {Phosphatidylethanolamine} ) recombinant enzyme 70000 nmol/min/mg Phosphatidylethanolamine CHEBI:16038 Y Y ECO:0000006 Pubmed:7798190 PENTACON Added by PENTACON; PENTACON Notes: recombinant enzyme AAP 2000000896 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 6300 {Phosphatidylcholine} (#8# natural PLA2 <19>) <19> 6300 nmol/min/mg Phosphatidylcholine CHEBI:49183 Y Y ECO:0000006 Pubmed:7798190 PENTACON Added by PENTACON; PENTACON Notes: natural PLA2 AAP 2000000897 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 145000 {Phosphatidylethanolamine} (#8# natural PLA2 <19>) <19> 145000 nmol/min/mg Phosphatidylethanolamine CHEBI:16038 Y Y ECO:0000006 Pubmed:7798190 PENTACON Added by PENTACON; PENTACON Notes: natural PLA2 AAP 2000000898 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/KM #8# 0.05 {Phosphatidylcholine} (#8# recombinant PLA2 <19>) <19> 0.05 mM Phosphatidylcholine CHEBI:49183 3.1.1.4 #8# recombinant PLA2 <19> Y Y ECO:0000006 Pubmed:7798190 BRENDA <19> Kawauchi, Y.; Takasaki, J.; Matsuura, Y.; Masuho, Y.: Preparation and characterization of human rheumatoid arthritic synovial fluid phospholipase A2 produced by recombinant baculovirus-infected cells. J. Biochem. (1994) 116, 82-87. {Pubmed:} AAP 12/7/2011 1111 2000000899 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/KM #8# 0.051 {Phosphatidylcholine} (#8# natural PLA2 <19>) <19> 0.051 mM Phosphatidylcholine CHEBI:49183 3.1.1.4 #8# natural PLA2 <19> Y Y ECO:0000006 Pubmed:7798190 BRENDA <19> Kawauchi, Y.; Takasaki, J.; Matsuura, Y.; Masuho, Y.: Preparation and characterization of human rheumatoid arthritic synovial fluid phospholipase A2 produced by recombinant baculovirus-infected cells. J. Biochem. (1994) 116, 82-87. {Pubmed:} AAP 12/7/2011 1111 2000000900 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/KM #8# 0.02 {Phosphatidylethanolamine} (#8# recombinant PLA2 <19>) <19> 0.02 mM Phosphatidylethanolamine CHEBI:16038 3.1.1.4 #8# recombinant PLA2 <19> Y Y ECO:0000006 Pubmed:7798190 BRENDA <19> Kawauchi, Y.; Takasaki, J.; Matsuura, Y.; Masuho, Y.: Preparation and characterization of human rheumatoid arthritic synovial fluid phospholipase A2 produced by recombinant baculovirus-infected cells. J. Biochem. (1994) 116, 82-87. {Pubmed:} AAP 12/7/2011 1111 2000000901 Jenn P14555 5320 PLA2G2A Homo sapiens 9606 Comment/biophysicochemical properties/KM #8# 0.024 {Phosphatidylethanolamine} (#8# natural PLA2 <19>) <19> 0.024 mM Phosphatidylethanolamine CHEBI:16038 3.1.1.4 #8# natural PLA2 <19> Y Y ECO:0000006 Pubmed:7798190 BRENDA <19> Kawauchi, Y.; Takasaki, J.; Matsuura, Y.; Masuho, Y.: Preparation and characterization of human rheumatoid arthritic synovial fluid phospholipase A2 produced by recombinant baculovirus-infected cells. J. Biochem. (1994) 116, 82-87. {Pubmed:} AAP 12/7/2011 1111 2000000902 Chandra P19440 2678 GGT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax WT Vmax 640 micromol/min/mg Glycylglycine CHEBI:17201 L-Glutamic acid gamma-(4-nitroanilide) Y Y ECO:0000006 Pubmed:7816801 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855 AAP 2000000903 Chandra P19440 2678 GGT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax WT Vmax 1100 micromol/min/mg L-Glutamic acid gamma-(4-nitroanilide) Glycylglycine CHEBI:17201 Y Y ECO:0000006 Pubmed:7816801 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855 AAP 2000000904 Chandra P19440 2678 GGT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 3.4 {Glycylglycine} (#6# recombinant mutant enzyme <65>) <65> 3.4 mM Glycylglycine CHEBI:17201 L-Glutamic acid gamma-(4-nitroanilide) 2.3.2.2 #6# recombinant mutant enzyme <65> Y Y ECO:0000006 Pubmed:7816801 BRENDA <65> Ikeda, Y.; Fujii, J.; Taniguchi, N.; Meister, A.: Expression of an active glycosylated human gamma-glutamyl transpeptidase mutant that lacks a membrane anchor domain. Proc. Natl. Acad. Sci. USA (1995) 92, 126-130. {Pubmed:7816801}; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855; Mutant:deltaSign AAP 12/7/2011 1111 2000000905 Chandra P19440 2678 GGT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6,21# 2.1 {L-Glu-4-nitroanilide} (#21# isoform II, hydrolase reaction <71>; #6# recombinant mutant enzyme <65>) <65,71> 2.1 mM L-Glutamic acid gamma-(4-nitroanilide) Glycylglycine CHEBI:17201 2.3.2.2 #21# isoform II, hydrolase reaction <71>; #6# recombinant mutant enzyme <65> Y Y ECO:0000006 Pubmed:7816801 BRENDA <65> Ikeda, Y.; Fujii, J.; Taniguchi, N.; Meister, A.: Expression of an active glycosylated human gamma-glutamyl transpeptidase mutant that lacks a membrane anchor domain. Proc. Natl. Acad. Sci. USA (1995) 92, 126-130. {Pubmed:7816801}; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855; Mutant:deltaSign AAP 12/7/2011 1111 2000000906 Chandra P19440 2678 GGT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6,7,17# 2.9-2.96 {Glycylglycine} (#6# recombinant wild-type enzyme <65>; #7# rat kidney enzyme <34>) <34,50,65> 2.9 mM Glycylglycine CHEBI:17201 L-Glutamic acid gamma-(4-nitroanilide) 2.3.2.2 #6# recombinant wild-type enzyme <65>; #7# rat kidney enzyme <34> Y Y ECO:0000006 Pubmed:7816801 BRENDA <65> Ikeda, Y.; Fujii, J.; Taniguchi, N.; Meister, A.: Expression of an active glycosylated human gamma-glutamyl transpeptidase mutant that lacks a membrane anchor domain. Proc. Natl. Acad. Sci. USA (1995) 92, 126-130. {Pubmed:7816801}; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855; Human protein, not from rat kidney as indicated in Secondary Source notes. AAP 12/7/2011 1111 2000000907 Chandra P19440 2678 GGT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1.5 {L-Glu-4-nitroanilide} (#6# recombinant wild-type <65>; #6# bile enzyme <46>) <46,65> 1.5 mM L-Glutamic acid gamma-(4-nitroanilide) Glycylglycine CHEBI:17201 2.3.2.2 #6# recombinant wild-type <65>; #6# bile enzyme <46> Y Y ECO:0000006 Pubmed:7816801 BRENDA <65> Ikeda, Y.; Fujii, J.; Taniguchi, N.; Meister, A.: Expression of an active glycosylated human gamma-glutamyl transpeptidase mutant that lacks a membrane anchor domain. Proc. Natl. Acad. Sci. USA (1995) 92, 126-130. {Pubmed:7816801}; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855 AAP 12/7/2011 1111 2000000908 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 406 {alanine-4-nitroanilide} 406 nmol/min/mg alanine-4-nitroanilide Y Y ECO:0000006 Pubmed:7893649 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: alanine-4-nitroanilide; Pubchem ID: CID 150936 AAP 2000000909 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 1439 {alanine-4-nitroanilide} 1439 nmol/min/mg alanine-4-nitroanilide Y Y ECO:0000006 Pubmed:7893649 PENTACON Added by PENTACON; PENTACON Notes: LTA4H modified with methyl methanethiosulfonate; Request ChEBI ID: alanine-4-nitroanilide; Pubchem ID: CID 150936 AAP 2000000910 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.47 {alanine-4-nitroanilide} (#4# pH 7.5, 25°C <27>) <27> 0.47 mM alanine-4-nitroanilide 3.3.2.6 #4# pH 7.5, 25°C <27> Y Y ECO:0000006 Pubmed:7893649 BRENDA <27> Mueller, M.J.; Samuelsson, B.; Haeggstrom, J.Z.: Chemical modification of leukotriene A4 hydrolase. Indications for essential tyrosyl and arginyl residues at the active site. Biochemistry (1995) 34, 3536-3543. {Pubmed:7893649}; PENTACON Notes: Request ChEBI ID: alanine-4-nitroanilide; Pubchem ID: CID 150936 AAP 12/7/2011 1111 2000000911 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 15480 {6-keto prostaglandin F1alpha} 15480 nmol/min/mg 6-oxo-prostaglandin F1alpha CHEBI:28158 Y Y ECO:0000006 Pubmed:8086429 PENTACON Added by PENTACON AAP 2000000912 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 24980 {NAD+} 24980 nmol/min/mg NAD(+) CHEBI:15846 Y Y ECO:0000006 Pubmed:8086429 PENTACON Added by PENTACON AAP 2000000913 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 21580 {prostaglandin A1} 21580 nmol/min/mg Prostaglandin A1 CHEBI:15545 Y Y ECO:0000006 Pubmed:8086429 PENTACON Added by PENTACON AAP 2000000914 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 13100 {prostaglandin A2} 13100 nmol/min/mg Prostaglandin A2 CHEBI:27820 Y Y ECO:0000006 Pubmed:8086429 PENTACON Added by PENTACON AAP 2000000915 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 22800 {prostaglandin E1} 22800 nmol/min/mg prostaglandin E1 CHEBI:15544 Y Y ECO:0000006 Pubmed:8086429 PENTACON Added by PENTACON AAP 2000000916 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 24600 {prostaglandin E2} 24600 nmol/min/mg prostaglandin E2 CHEBI:15551 Y Y ECO:0000006 Pubmed:8086429 PENTACON Added by PENTACON AAP 2000000917 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 22330 {prostaglandin F2alpha} 22330 nmol/min/mg prostaglandin F2alpha CHEBI:15553 Y Y ECO:0000006 Pubmed:8086429 PENTACON Added by PENTACON AAP 2000000918 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.063 {6-ketoprostaglandin F1alpha} (#4# recombinant enzyme expressed in E. coli <26>) <26> 0.063 mM 6-oxo-prostaglandin F1alpha CHEBI:28158 1.1.1.141 #4# recombinant enzyme expressed in E. coli <26> Y Y ECO:0000006 Pubmed:8086429 BRENDA <26> Ensoe, C.M.; Tai, H.H.: Bacterial expression and site-directed mutagenesis of two critical residues (tyrosine-151 and lysine-155) of human placental NAD+-dependent 15-hydroxyprostaglandin dehydrogenase. Biochim. Biophys. Acta (1994) 1208, 151-156. {Pubmed:8086429} AAP 12/7/2011 1111 2000000919 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.022 {NAD+} (#4# recombinant enzyme expressed in E. coli <26>; #4# 37°C, pH 7.5, V186K mutant <33>) <26,33> 0.022 mM NAD(+) CHEBI:15846 1.1.1.141 #4# recombinant enzyme expressed in E. coli <26>; #4# 37°C, pH 7.5, V186K mutant <33> Y Y ECO:0000006 Pubmed:8086429 BRENDA <26> Ensoe, C.M.; Tai, H.H.: Bacterial expression and site-directed mutagenesis of two critical residues (tyrosine-151 and lysine-155) of human placental NAD+-dependent 15-hydroxyprostaglandin dehydrogenase. Biochim. Biophys. Acta (1994) 1208, 151-156. {Pubmed:8086429} AAP 12/7/2011 1111 2000000920 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0045 {Prostaglandin A1} (#4# recombinant enzyme expressed in E. coli <26>) <26> 0.0045 mM Prostaglandin A1 CHEBI:15545 1.1.1.141 #4# recombinant enzyme expressed in E. coli <26> Y Y ECO:0000006 Pubmed:8086429 BRENDA <26> Ensoe, C.M.; Tai, H.H.: Bacterial expression and site-directed mutagenesis of two critical residues (tyrosine-151 and lysine-155) of human placental NAD+-dependent 15-hydroxyprostaglandin dehydrogenase. Biochim. Biophys. Acta (1994) 1208, 151-156. {Pubmed:8086429} AAP 12/7/2011 1111 2000000921 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.022 {Prostaglandin A2} (#4# recombinant enzyme expressed in E. coli <26>) <26> 0.022 mM Prostaglandin A2 CHEBI:27820 1.1.1.141 #4# recombinant enzyme expressed in E. coli <26> Y Y ECO:0000006 Pubmed:8086429 BRENDA <26> Ensoe, C.M.; Tai, H.H.: Bacterial expression and site-directed mutagenesis of two critical residues (tyrosine-151 and lysine-155) of human placental NAD+-dependent 15-hydroxyprostaglandin dehydrogenase. Biochim. Biophys. Acta (1994) 1208, 151-156. {Pubmed:8086429} AAP 12/7/2011 1111 2000000922 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0055 {prostaglandin E1} (#4# recombinant enzyme expressed in E. coli <26>) <26> 0.0055 mM prostaglandin E1 CHEBI:15544 1.1.1.141 #4# recombinant enzyme expressed in E. coli <26> Y Y ECO:0000006 Pubmed:8086429 BRENDA <26> Ensoe, C.M.; Tai, H.H.: Bacterial expression and site-directed mutagenesis of two critical residues (tyrosine-151 and lysine-155) of human placental NAD+-dependent 15-hydroxyprostaglandin dehydrogenase. Biochim. Biophys. Acta (1994) 1208, 151-156. {Pubmed:8086429} AAP 12/7/2011 1111 2000000923 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.0039 {prostaglandin E2} (#4# recombinant enzyme expressed in E. coli <26>) <26> 0.0039 mM prostaglandin E2 CHEBI:15551 1.1.1.141 #4# recombinant enzyme expressed in E. coli <26> Y Y ECO:0000006 Pubmed:8086429 BRENDA <26> Ensoe, C.M.; Tai, H.H.: Bacterial expression and site-directed mutagenesis of two critical residues (tyrosine-151 and lysine-155) of human placental NAD+-dependent 15-hydroxyprostaglandin dehydrogenase. Biochim. Biophys. Acta (1994) 1208, 151-156. {Pubmed:8086429} AAP 12/7/2011 1111 2000000924 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.04 {prostaglandin F2alpha} (#4# recombinant enzyme expressed in E. coli <26>) <26> 0.04 mM prostaglandin F2alpha CHEBI:15553 1.1.1.141 #4# recombinant enzyme expressed in E. coli <26> Y Y ECO:0000006 Pubmed:8086429 BRENDA <26> Ensoe, C.M.; Tai, H.H.: Bacterial expression and site-directed mutagenesis of two critical residues (tyrosine-151 and lysine-155) of human placental NAD+-dependent 15-hydroxyprostaglandin dehydrogenase. Biochim. Biophys. Acta (1994) 1208, 151-156. {Pubmed:8086429} AAP 12/7/2011 1111 2000000925 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 5600 {arachidonic acid} <26> 5600 nmol/min/mg arachidonic acid CHEBI:15843 Y Y ECO:0000006 Pubmed:8334154 PENTACON Added by PENTACON AAP 2000000926 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 10600 {Linoleic acid} <26> 10600 nmol/min/mg Linoleic acid CHEBI:17351 Y Y ECO:0000006 Pubmed:8334154 PENTACON Added by PENTACON AAP 2000000927 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.012 {arachidonic acid} <26> 0.012 mM arachidonic acid CHEBI:15843 1.13.11.33 Y Y ECO:0000006 Pubmed:8334154 BRENDA <26> Kuehn, H.; Barnett, J.; Grunberger, D.; Baecker, P.; Chow, J.; Nguyen, B.; Bursztyn-Pettegrew, H.; Chan, H.; Sigal, E.: Overexpression, purification and characterization of human recombinant 15-lipoxygenase. Biochim. Biophys. Acta (1993) 1169, 80-89. {Pubmed:8334154} (c) AAP 12/7/2011 1111 2000000928 Jenn P16050 246 ALOX15 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.003 {Linoleic acid} <26> 0.003 mM Linoleic acid CHEBI:17351 1.13.11.33 Y Y ECO:0000006 Pubmed:8334154 BRENDA <26> Kuehn, H.; Barnett, J.; Grunberger, D.; Baecker, P.; Chow, J.; Nguyen, B.; Bursztyn-Pettegrew, H.; Chan, H.; Sigal, E.: Overexpression, purification and characterization of human recombinant 15-lipoxygenase. Biochim. Biophys. Acta (1993) 1169, 80-89. {Pubmed:8334154} (c) AAP 12/7/2011 1111 2000000929 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM .00968 {(5Z,8E,10E,12S)-12-hydroxy-5,8,10-heptadecatrienoic acid} 0.00968 mM 12-hydroxy-5,8,10-heptadecatrienoic acid Y Y ECO:0000006 Pubmed:8508808 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID:12-hydroxy-5,8,10-heptadecatrienoic acid; Pubchem ID: CID 5283141 AAP 2000000930 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM .102 {NAD+} 0.102 mM NAD(+) CHEBI:15846 Y Y ECO:0000006 Pubmed:8508808 PENTACON Added by PENTACON AAP 2000000931 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.00765 {(5Z,8E,10E,12S)-12-hydroxy-5,8,10-heptadecatrienoic acid} <24> 0.00765 mM 12-hydroxy-5,8,10-heptadecatrienoic acid 1.1.1.141 Y Y ECO:0000006 Pubmed:8508808 BRENDA <24> Höhl, W.; Stahl, B.; Mundkowski, R.; Hofmann, U.; Meese, C.O.; Kuhlmann, U.; Schlegel, W.: Mass determination of 15-hydroxyprostaglandin dehydrogenase from human placenta and kinetic studies with (5Z,8E,10E,12S)-12-hydroxy-5,8,10,-heptadecatrienoic acid as substrate. Eur. J. Biochem. (1993) 214, 67-73. {Pubmed:8508808}; PENTACON Notes: Request ChEBI ID:12-hydroxy-5,8,10-heptadecatrienoic acid; Pubchem ID: CID 5283141 AAP 12/7/2011 1111 2000000932 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.117 {NAD+} <24> 0.117 mM NAD(+) CHEBI:15846 1.1.1.141 Y Y ECO:0000006 Pubmed:8508808 BRENDA <24> Höhl, W.; Stahl, B.; Mundkowski, R.; Hofmann, U.; Meese, C.O.; Kuhlmann, U.; Schlegel, W.: Mass determination of 15-hydroxyprostaglandin dehydrogenase from human placenta and kinetic studies with (5Z,8E,10E,12S)-12-hydroxy-5,8,10,-heptadecatrienoic acid as substrate. Eur. J. Biochem. (1993) 214, 67-73. {Pubmed:8508808} AAP 12/7/2011 1111 2000000933 Christie P15428 3248 HPGD Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.01 {prostaglandin E2} <16,24> 0.01 mM prostaglandin E2 CHEBI:15551 1.1.1.141 Y Y ECO:0000033 Pubmed:8508808 BRENDA <24> Höhl, W.; Stahl, B.; Mundkowski, R.; Hofmann, U.; Meese, C.O.; Kuhlmann, U.; Schlegel, W.: Mass determination of 15-hydroxyprostaglandin dehydrogenase from human placenta and kinetic studies with (5Z,8E,10E,12S)-12-hydroxy-5,8,10,-heptadecatrienoic acid as substrate. Eur. J. Biochem. (1993) 214, 67-73. {Pubmed:8508808} AAP 12/7/2011 1111 2000000934 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.023 {leukotriene A4} (#4# pH 7.7-8.0, 37°C <7>; #4# pH 8.0, 22°C, mutant Y378F <28,29>) <7,28,29> 0.023 mM leukotriene A4 CHEBI:15651 3.3.2.6 #4# pH 7.7-8.0, 37°C <7>; #4# pH 8.0, 22°C, mutant Y378F <28,29> Y Y ECO:0000006 Pubmed:8650196 BRENDA <28> Mueller, M.J.; Blomster, M.; Oppermann, U.C.; Jornvall, H.; Samuelsson, B.; Haeggstrom, J.Z.: Leukotriene A4 hydrolase: protection from mechanism-based inactivation by mutation of tyrosine-378. Proc. Natl. Acad. Sci. USA (1996) 93, 5931-5935. {Pubmed:8650196}; PENTACON Notes: Mutant: Y378F AAP 12/7/2011 1111 2000000935 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.006 {leukotriene A4} (#4# pH 8.0, 22°C, wild-type enzyme <28,29>) <28,29> 0.006 mM leukotriene A4 CHEBI:15651 3.3.2.6 #4# pH 8.0, 22°C, wild-type enzyme <28,29> Y Y ECO:0000006 Pubmed:8650196 BRENDA <28> Mueller, M.J.; Blomster, M.; Oppermann, U.C.; Jornvall, H.; Samuelsson, B.; Haeggstrom, J.Z.: Leukotriene A4 hydrolase: protection from mechanism-based inactivation by mutation of tyrosine-378. Proc. Natl. Acad. Sci. USA (1996) 93, 5931-5935. {Pubmed:8650196} AAP 12/7/2011 1111 2000000936 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.023 {leukotriene A4} (#4# pH 7.7-8.0, 37°C <7>; #4# pH 8.0, 22°C, mutant Y378F <28,29>) <7,28,29> 0.023 mM leukotriene A4 CHEBI:15651 3.3.2.6 #4# pH 7.7-8.0, 37°C <7>; #4# pH 8.0, 22°C, mutant Y378F <28,29> Y Y ECO:0000006 Pubmed:8798687 BRENDA <29> Mueller, M.J.; Andberg, M.B.; Samuelsson, B.; Haeggstrom, J.Z.: Leukotriene A4 hydrolase, mutation of tyrosine 378 allows conversion of leukotriene A4 into an isomer of leukotriene B4. J. Biol. Chem. (1996) 271, 24345-24348. {Pubmed:8798687}; PENTACON Notes: Mutant: Y378F AAP 12/7/2011 1111 2000000937 Christie P09960 4048 LTA4H Homo sapiens 9606 Comment/biophysicochemical properties/KM #4# 0.006 {leukotriene A4} (#4# pH 8.0, 22°C, wild-type enzyme <28,29>) <28,29> 0.006 mM leukotriene A4 CHEBI:15651 3.3.2.6 #4# pH 8.0, 22°C, wild-type enzyme <28,29> Y Y ECO:0000006 Pubmed:8798687 BRENDA <29> Mueller, M.J.; Andberg, M.B.; Samuelsson, B.; Haeggstrom, J.Z.: Leukotriene A4 hydrolase, mutation of tyrosine 378 allows conversion of leukotriene A4 into an isomer of leukotriene B4. J. Biol. Chem. (1996) 271, 24345-24348. {Pubmed:8798687} AAP 12/7/2011 1111 2000000938 Chandra P19440 2678 GGT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 5.5 5.5 micromol/min/mg L-Glutamic acid gamma-(4-nitroanilide) H2O Y Y ECO:0000006 Pubmed:8827453 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855; hydrolysis reaction AAP 2000000939 Chandra P19440 2678 GGT1 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 1200 1200 micromol/min/mg L-Glutamic acid gamma-(4-nitroanilide) glycylglycine CHEBI:17201 Y Y ECO:0000006 Pubmed:8827453 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855; transpeptidation AAP 2000000940 Chandra P19440 2678 GGT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM 10 10 mM Glycylglycine CHEBI:17201 L-Glutamic acid gamma-(4-nitroanilide) Y Y ECO:0000006 Pubmed:8827453 PENTACON Added by PENTACON; PENTACON Notes: recombinant wild-type, transpeptidation AAP 2000000941 Chandra P19440 2678 GGT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 0.008 {L-Glu-4-nitroanilide} (#6# hydrolase reaction <67>) <67> 0.008 mM L-Glutamic acid gamma-(4-nitroanilide) H2O 2.3.2.2 #6# hydrolase reaction <67> Y Y ECO:0000006 Pubmed:8827453 BRENDA <67> Ikeda, Y.; Fujii, J.; Taniguchi, N.: Effects of substitutions of the conserved histidine residues in human gamma-glutamyl transpeptidase. J. Biochem. (1996) 119, 1166-1170. {Pubmed:8827453}; PENTACON Notes: Request ChEBI ID:L-Glutamic acid gamma-(4-nitroanilide): CID 57369855 AAP 12/7/2011 1111 2000000942 Chandra P19440 2678 GGT1 Homo sapiens 9606 Comment/biophysicochemical properties/KM #6# 1.4 {L-Glu-4-nitroanilide} (#6# recombinant wild-type, transpeptidation <67>) <67> 1.4 mM L-Glutamic acid gamma-(4-nitroanilide) glycylglycine CHEBI:17201 2.3.2.2 #6# recombinant wild-type, transpeptidation <67> Y Y ECO:0000006 Pubmed:8827453 BRENDA <67> Ikeda, Y.; Fujii, J.; Taniguchi, N.: Effects of substitutions of the conserved histidine residues in human gamma-glutamyl transpeptidase. J. Biochem. (1996) 119, 1166-1170. {Pubmed:8827453}; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855 AAP 12/7/2011 1111 2000000943 Jenn P08684 1576 CYP3A4 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 0.00749 {Quinine} (#2# recombinant CYP3A4 <1>) <1> 0.00749 nmol/min/mg Quinine CHEBI:15854 Y Y ECO:0000006 Pubmed:8968357 PENTACON Added by PENTACON; PENTACON Notes: recombinant CYP3A4 AAP 2000000944 Jenn P33261 1557 CYP2C19 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 0.000196 {Quinine} (#2# recombinant CYP2C19 <1>) <1> 0.000196 nmol/min/mg Quinine CHEBI:15854 Y Y ECO:0000006 Pubmed:8968357 PENTACON Added by PENTACON; PENTACON Notes: recombinant CYP2C19 AAP 2000000945 Jenn P33261 1557 CYP2C19 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.046 {Quinine} (#2# recombinant CYP2C19 <1>) <1> 0.046 mM Quinine CHEBI:15854 1.14.13.67 #2# recombinant CYP2C19 <1> Y Y ECO:0000006 Pubmed:8968357 BRENDA <1> Zhao, X.J.; Yokoyama, H.; Chiba, K.; Wanwimolruk, S.; Ishizaki, T.: Identification of human cytochrome P450 isoforms involved in the hydroxylation of quinine by human liver microsomes and nine recombinant human cytochromes P450. J. Pharmacol. Exp. Ther. (1996) 279, 1327-1334. {Pubmed:8968357} AAP 12/7/2011 1111 2000000946 Jenn P08684 1576 CYP3A4 Homo sapiens 9606 Comment/biophysicochemical properties/KM #2# 0.114 {Quinine} (#2# recombinant CYP3A4 <1>) <1> 0.114 mM Quinine CHEBI:15854 1.14.13.67 #2# recombinant CYP3A4 <1> Y Y ECO:0000006 Pubmed:8968357 BRENDA <1> Zhao, X.J.; Yokoyama, H.; Chiba, K.; Wanwimolruk, S.; Ishizaki, T.: Identification of human cytochrome P450 isoforms involved in the hydroxylation of quinine by human liver microsomes and nine recombinant human cytochromes P450. J. Pharmacol. Exp. Ther. (1996) 279, 1327-1334. {Pubmed:8968357} AAP 12/7/2011 1111 2000000947 Jenn Q99487 5051 PAFAH2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 1700 {1-decanoyl-2-(4-nitrophenylglutaryl) phosphate} <6> 1700 nmol/min/mg 1-decanoyl-2-(4-nitrophenylglutaryl) phosphate Y Y ECO:0000006 Pubmed:9494101 PENTACON Added by PENTACON; PENTACON Notes: Request ChEBI ID: 1-decanoyl-2-(4-nitrophenylglutaryl) phosphate AAP 2000000948 Jenn Q99487 5051 PAFAH2 Homo sapiens 9606 Comment/biophysicochemical properties/Vmax 35000 {Platelet activating factor} <6> 35000 nmol/min/mg Platelet activating factor CHEBI:44811 Y Y ECO:0000006 Pubmed:9494101 PENTACON Added by PENTACON AAP 2000000949 Jenn Q99487 5051 PAFAH2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #8# 0.01 {1-decanoyl-2-(4-nitrophenylglutaryl) phosphate} <6> 0.01 mM 1-decanoyl-2-(4-nitrophenylglutaryl) phosphate 3.1.1.4 Y Y ECO:0000006 Pubmed:9494101 BRENDA <6> Rice, S.Q.J.; Southan, C.; Boyd, H.F.; Terrett, J.A.; MacPhee, C.H.; Moores, K.; Gloger, I.S.; Tew, D.G.: Expression, purification and characterization of a human serine-dependent phospholipase A2 with high specificity for oxidized phospholipids and platelet activating factor. Biochem. J. (1998) 330, 1309-1315. {Pubmed:9494101}; PENTACON Notes: Request ChEBI ID: 1-decanoyl-2-(4-nitrophenylglutaryl) phosphate AAP 12/7/2011 1111 2000000950 Jenn Q99487 5051 PAFAH2 Homo sapiens 9606 Comment/biophysicochemical properties/KM #8# 0.042 {Platelet activating factor} <6> 0.042 mM Platelet activating factor CHEBI:44811 3.1.1.4 Y Y ECO:0000006 Pubmed:9494101 BRENDA <6> Rice, S.Q.J.; Southan, C.; Boyd, H.F.; Terrett, J.A.; MacPhee, C.H.; Moores, K.; Gloger, I.S.; Tew, D.G.: Expression, purification and characterization of a human serine-dependent phospholipase A2 with high specificity for oxidized phospholipids and platelet activating factor. Biochem. J. (1998) 330, 1309-1315. {Pubmed:9494101} AAP 12/7/2011 1111 2000000951 Jenn Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.04 {leukotriene A4} (#3# pH 7.4, 25°C <6>) <6> 0.04 mM leukotriene A4 CHEBI:15651 Y Y ECO:0000006 Pubmed:9554994 PENTACON Added by PENTACON; PENTACON Notes: pH 7.4, 25°C AAP 2000000952 Jenn Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/Vmax #3# 14000 {leukotriene A4} (#3# pH 7.4, 25°C <6>) <6> 14000 nmol/min/mg leukotriene A4 CHEBI:15651 Y Y ECO:0000006 Pubmed:9554994 PENTACON Added by PENTACON; PENTACON Notes: pH 7.4, 25°C AAP 2000000953 Jenn Q16873 4056 LTC4S Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.0004 {glutathione} (#3# pH 7.4, 25°C <6>) <6> 0.0004 mM glutathione CHEBI:16856 4.4.1.20 #3# pH 7.4, 25°C <6> Y Y ECO:0000006 Pubmed:9554994 BRENDA <6> Gupta, N.; Gresser, M.J.; Ford-Hutchinson, A.W.: Kinetic mechanism of glutathione conjugation to leukotriene A4 by leukotriene C4 synthase. Biochim. Biophys. Acta (1998) 1391, 157-168. {Pubmed:9554994} (c) AAP 12/7/2011 1111 2000000954 Jenn P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.00055 {1,2-bis-(1-pyrenebutanoyl)-sn-glycero-3-phosphocholine} (#3# phospholipase activity of recombinant enzyme devoid of sialic acid, expressed in baby hamster kidney cells <47>) <47> 0.00055 mM 1,2-bis-(1-pyrenebutanoyl)-sn-glycero-3-phosphocholine 2.3.1.43 #3# phospholipase activity of recombinant enzyme devoid of sialic acid, expressed in baby hamster kidney cells <47> Y Y ECO:0000006 Pubmed:9555945 BRENDA <47> Lacko, A.G.; Reason, A.J.; Nuckolls, C.; Kudchodkar, B.J.; Nair, M.P.; Sundarrajan, G.; Pritchard, P.H.; Morris, H.R.; Dell, A.: Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties. J. Lipid Res. (1998) 39, 807-820. {Pubmed:9555945}; PENTACON Notes: Request ChEBI ID: 1,2-bis-(1-pyrenebutanoyl)-sn-glycero-3-phosphocholine AAP 12/7/2011 1111 2000000955 Jenn P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.00014 {1,2-bis-(1-pyrenebutanoyl)-sn-glycero-3-phosphocholine} (#3# phospholipase activity <47>) <47> 0.00014 mM 1,2-bis-(1-pyrenebutanoyl)-sn-glycero-3-phosphocholine 2.3.1.43 #3# phospholipase activity <47> Y Y ECO:0000006 Pubmed:9555945 BRENDA <47> Lacko, A.G.; Reason, A.J.; Nuckolls, C.; Kudchodkar, B.J.; Nair, M.P.; Sundarrajan, G.; Pritchard, P.H.; Morris, H.R.; Dell, A.: Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties. J. Lipid Res. (1998) 39, 807-820. {Pubmed:9555945}; PENTACON Notes: Request ChEBI ID: 1,2-bis-(1-pyrenebutanoyl)-sn-glycero-3-phosphocholine AAP 12/7/2011 1111 2000000956 Jenn P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.00034 {1,2-bis-(1-pyrenebutanoyl)-sn-glycero-3-phosphocholine} (#3# recombinant enzyme devoid of sialic acid, expressed in baby hamster kidney cells <47>) <47> 0.00034 mM 1,2-bis-(1-pyrenebutanoyl)-sn-glycero-3-phosphocholine 2.3.1.43 #3# recombinant enzyme devoid of sialic acid, expressed in baby hamster kidney cells <47> Y Y ECO:0000006 Pubmed:9555945 BRENDA <47> Lacko, A.G.; Reason, A.J.; Nuckolls, C.; Kudchodkar, B.J.; Nair, M.P.; Sundarrajan, G.; Pritchard, P.H.; Morris, H.R.; Dell, A.: Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties. J. Lipid Res. (1998) 39, 807-820. {Pubmed:9555945}; PENTACON Notes: Request ChEBI ID: 1,2-bis-(1-pyrenebutanoyl)-sn-glycero-3-phosphocholine AAP 12/7/2011 1111 2000000957 Jenn P04180 3931 LCAT Homo sapiens 9606 Comment/biophysicochemical properties/KM #3# 0.00019 {1,2-bis-(1-pyrenebutanoyl)-sn-gycero-3-phosphocholine} (#3# phospholipase activity of recombinant enzyme expressed in baby hamster kidney cells <47>) <47> 0.00019 mM 1,2-bis-(1-pyrenebutanoyl)-sn-gycero-3-phosphocholine 2.3.1.43 #3# phospholipase activity of recombinant enzyme expressed in baby hamster kidney cells <47> Y Y ECO:0000006 Pubmed:9555945 BRENDA <47> Lacko, A.G.; Reason, A.J.; Nuckolls, C.; Kudchodkar, B.J.; Nair, M.P.; Sundarrajan, G.; Pritchard, P.H.; Morris, H.R.; Dell, A.: Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties. J. Lipid Res. (1998) 39, 807-820. {Pubmed:9555945}; PENTACON Notes: Request ChEBI ID: 1,2-bis-(1-pyrenebutanoyl)-sn-glycero-3-phosphocholine AAP 12/7/2011 1111 2000000958 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin; IC50: 750.0 nM; Cyclooxygenase-2; CHEBI:100173 (indomethacin) 750 nM indomethacin CHEBI:100173 arachidonate CHEBI:32395 17638 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000959 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 10; IC50: 60.0 nM; Cyclooxygenase-2; CHEBI:258373 60 nM Indomethacin derivative, 10 CHEBI:258373 arachidonate CHEBI:32395 22957 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000960 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 11; IC50: 75.0 nM; Cyclooxygenase-2; CHEBI:258629 75 nM Indomethacin derivative, 11 CHEBI:258629 arachidonate CHEBI:32395 22958 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000961 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 12; IC50: 50.0 nM; Cyclooxygenase-2; CHEBI:258602 50 nM Indomethacin derivative, 12 CHEBI:258602 arachidonate CHEBI:32395 22959 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000962 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 13; IC50: 120.0 nM; Cyclooxygenase-2; CHEBI:258273 120 nM Indomethacin derivative, 13 CHEBI:258273 arachidonate CHEBI:32395 22960 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000963 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 14; IC50: 60.0 nM; Cyclooxygenase-2; CHEBI:258615 60 nM Indomethacin derivative, 14 CHEBI:258615 arachidonate CHEBI:32395 22961 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000964 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 15; IC50: 50.0 nM; Cyclooxygenase-2; CHEBI:258787 50 nM Indomethacin derivative, 15 CHEBI:258787 arachidonate CHEBI:32395 22962 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000965 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 16; IC50: >16500 nM; Cyclooxygenase-2; CHEBI:258316 nM Indomethacin derivative, 16 CHEBI:258316 arachidonate CHEBI:32395 22963 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000966 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 17; IC50: >16500 nM; Cyclooxygenase-2; CHEBI:258289 nM Indomethacin derivative, 17 CHEBI:258289 arachidonate CHEBI:32395 22964 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000967 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 18; IC50: 700.0 nM; Cyclooxygenase-2; CHEBI:258695 700 nM Indomethacin derivative, 18 CHEBI:258695 arachidonate CHEBI:32395 22965 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000968 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 19; IC50: 60.0 nM; Cyclooxygenase-2; CHEBI:258321 60 nM Indomethacin derivative, 19 CHEBI:258321 arachidonate CHEBI:32395 22966 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000969 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 20; IC50: 50.0 nM; Cyclooxygenase-2; CHEBI:258407 50 nM Indomethacin derivative, 20 CHEBI:258407 arachidonate CHEBI:32395 22967 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000970 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 21; IC50: >66000 nM; Cyclooxygenase-2; CHEBI:258849 nM Indomethacin derivative, 21 CHEBI:258849 arachidonate CHEBI:32395 22968 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000971 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 22; IC50: >66000 nM; Cyclooxygenase-2; CHEBI:258881 nM Indomethacin derivative, 22 CHEBI:258881 arachidonate CHEBI:32395 22969 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000972 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 23; IC50: 2500.0 nM; Cyclooxygenase-2; CHEBI:258967 2500 nM Indomethacin derivative, 23 CHEBI:258967 arachidonate CHEBI:32395 22970 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000973 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 4; IC50: 700.0 nM; Cyclooxygenase-2; CHEBI:259092 700 nM Indomethacin derivative, 4 CHEBI:259092 arachidonate CHEBI:32395 22951 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000974 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 5; IC50: 250.0 nM; Cyclooxygenase-2; CHEBI:216294 250 nM Indomethacin derivative, 5 CHEBI:216294 arachidonate CHEBI:32395 22952 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000975 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 6; IC50: 250.0 nM; Cyclooxygenase-2; CHEBI:133478 250 nM Indomethacin derivative, 6 CHEBI:133478 arachidonate CHEBI:32395 22953 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000976 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 7; IC50: 120.0 nM; Cyclooxygenase-2; CHEBI:258213 120 nM Indomethacin derivative, 7 CHEBI:258213 arachidonate CHEBI:32395 22954 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000977 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 8; IC50: 40.0 nM; Cyclooxygenase-2; CHEBI:258372 40 nM Indomethacin derivative, 8 CHEBI:258372 arachidonate CHEBI:32395 22955 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000978 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin derivative, 9; IC50: 300.0 nM; Cyclooxygenase-2; CHEBI:258406 300 nM Indomethacin derivative, 9 CHEBI:258406 arachidonate CHEBI:32395 22956 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000979 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Meclofenamic acid; IC50: 50.0 nM; Cyclooxygenase-2; CHEBI:110531 50 nM Meclofenamic acid CHEBI:110531 arachidonate CHEBI:32395 22971 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000980 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Meclofenamic acid derivative, 24; IC50: 5500.0 nM; Cyclooxygenase-2; CHEBI:348088 5500 nM Meclofenamic acid derivative, 24 CHEBI:348088 arachidonate CHEBI:32395 22972 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000981 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Meclofenamic acid derivative, 25; IC50: 60.0 nM; Cyclooxygenase-2; CHEBI:348823 60 nM Meclofenamic acid derivative, 25 CHEBI:348823 arachidonate CHEBI:32395 22973 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000982 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Meclofenamic acid derivative, 26; IC50: 600.0 nM; Cyclooxygenase-2; CHEBI:349120 600 nM Meclofenamic acid derivative, 26 CHEBI:349120 arachidonate CHEBI:32395 22974 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000983 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Meclofenamic acid derivative, 27; IC50: 150.0 nM; Cyclooxygenase-2; CHEBI:348276 150 nM Meclofenamic acid derivative, 27 CHEBI:348276 arachidonate CHEBI:32395 22975 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000984 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Meclofenamic acid derivative, 28; IC50: 1000.0 nM; Cyclooxygenase-2; CHEBI:348010 1000 nM Meclofenamic acid derivative, 28 CHEBI:348010 arachidonate CHEBI:32395 22976 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000985 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Meclofenamic acid derivative, 29; IC50: 200.0 nM; Cyclooxygenase-2; CHEBI:347576 200 nM Meclofenamic acid derivative, 29 CHEBI:347576 arachidonate CHEBI:32395 22977 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000986 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Meclofenamic acid derivative, 30; IC50: 4500.0 nM; Cyclooxygenase-2; CHEBI:348179 4500 nM Meclofenamic acid derivative, 30 CHEBI:348179 arachidonate CHEBI:32395 22978 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000987 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Meclofenamic acid derivative, 31; IC50: 70.0 nM; Cyclooxygenase-2; CHEBI:348140 70 nM Meclofenamic acid derivative, 31 CHEBI:348140 arachidonate CHEBI:32395 22979 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000988 Christie P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Meclofenamic acid derivative, 32; IC50: 400.0 nM; Cyclooxygenase-2; CHEBI:347888 400 nM Meclofenamic acid derivative, 32 CHEBI:347888 arachidonate CHEBI:32395 22980 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:10639181 BindingDB AAP 10/25/2013 10/25/2013 2000000989 Chandra P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/Km 3alpha-androsteanediol oxidation; Km: 32000.0 nM; 17-beta-Hydroxysteroid Dehydrogenase 5 (17-beta-HSD5, AKR1C3) 32000 nM 5alpha-androstane-3alpha,17beta-diol CHEBI:36713 Y Y ECO:0000006 PubMed:14996743 PENTACON Added by PENTACON AAP 2000000990 Chandra P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/Km Androsterone reduction; Km: 15900.0 nM; 17-beta-Hydroxysteroid Dehydrogenase 5 (17-beta-HSD5, AKR1C3) 15900 nM androsterone CHEBI:16032 Y Y ECO:0000006 PubMed:14996743 PENTACON Added by PENTACON AAP 2000000991 Chandra P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/Km 5a-DHT reduction; Km: 7200.0 nM; 17-beta-Hydroxysteroid Dehydrogenase 5 (17-beta-HSD5, AKR1C3) 7200 nM 17beta-hydroxy-5alpha-androstan-3-one CHEBI:16330 Y Y ECO:0000006 PubMed:14996743 PENTACON Added by PENTACON AAP 2000000992 Chandra P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/Ki Flufenamic acid; Ki: 140.0 nM; 17-beta-Hydroxysteroid Dehydrogenase 5 (17-beta-HSD5, AKR1C3); CHEBI:129860 (flufenamic acid) 140 nM flufenamic acid CHEBI:129860 5alpha-androstane-3alpha,17beta-diol CHEBI:36713 17636 pH: 7; temp: 30.00 C Y Y ECO:0000006 PubMed:14996743 BindingDB AAP 10/25/2013 10/25/2013 2000000993 Chandra P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/Ki Flufenamic acid; Ki: 3100.0 nM; 17-beta-Hydroxysteroid Dehydrogenase 5 (17-beta-HSD5, AKR1C3); CHEBI:129860 (flufenamic acid) 3100 nM flufenamic acid CHEBI:129860 androsterone CHEBI:16032 17636 pH: 7; temp: 30.00 C Y Y ECO:0000006 PubMed:14996743 BindingDB AAP 10/25/2013 10/25/2013 2000000994 Chandra P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/Ki Indomethacin; Ki: 270.0 nM; 17-beta-Hydroxysteroid Dehydrogenase 5 (17-beta-HSD5, AKR1C3); CHEBI:100173 (indomethacin) 270 nM indomethacin CHEBI:100173 5alpha-androstane-3alpha,17beta-diol CHEBI:36713 17638 pH: 7; temp: 30.00 C Y Y ECO:0000006 PubMed:14996743 BindingDB AAP 10/25/2013 10/25/2013 2000000995 Chandra P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/Ki Indomethacin; Ki: 2100.0 nM; 17-beta-Hydroxysteroid Dehydrogenase 5 (17-beta-HSD5, AKR1C3); CHEBI:100173 (indomethacin) 2100 nM indomethacin CHEBI:100173 androsterone CHEBI:16032 17638 pH: 7; temp: 30.00 C Y Y ECO:0000006 PubMed:14996743 BindingDB AAP 10/25/2013 10/25/2013 2000000996 Chandra P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/Km 2.9 micromolar for testosterone 2900 nM testosterone CHEBI:17347 Y Y ECO:0000006 PubMed:17166832 PENTACON Added by PENTACON AAP 2000000997 Chandra P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 EM-1396; IC50: 13.0 nM; 17-beta-Hydroxysteroid Dehydrogenase 5 (17-beta-HSD5, AKR1C3); 13 nM EM-1396 testosterone CHEBI:17347 17287 pH: 6; temp: 22.00 C Y Y ECO:0000006 PubMed:17166832 BindingDB PENTACON Notes: Request ChEBI ID: EM-1396 AAP 10/25/2013 10/25/2013 2000000998 Chandra P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 EM-1404; IC50: 3.2 nM; 17-beta-Hydroxysteroid Dehydrogenase 5 (17-beta-HSD5, AKR1C3); 3.2 nM EM-1404 testosterone CHEBI:17347 17285 pH: 6; temp: 22.00 C Y Y ECO:0000006 PubMed:17166832 BindingDB PENTACON Notes: Request ChEBI ID: EM-1404 AAP 10/25/2013 10/25/2013 2000000999 Chandra P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/Ki EM-1404; Ki: 6.9 nM; 17-beta-Hydroxysteroid Dehydrogenase 5 (17-beta-HSD5, AKR1C3); 6.9 nM EM-1404 testosterone CHEBI:17347 17285 pH: 7.5; temp: 37.00 C Y Y ECO:0000006 PubMed:17166832 BindingDB PENTACON Notes: Request ChEBI ID: EM-1404 AAP 10/25/2013 10/25/2013 2000001000 Chandra P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 EM-1424; IC50: 9.5 nM; 17-beta-Hydroxysteroid Dehydrogenase 5 (17-beta-HSD5, AKR1C3); 9.5 nM EM-1424 testosterone CHEBI:17347 17286 pH: 6; temp: 22.00 C Y Y ECO:0000006 PubMed:17166832 BindingDB PENTACON Notes: Request ChEBI ID: EM-1424 AAP 10/25/2013 10/25/2013 2000001001 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6a; IC50: 77.0 nM; Prostacyclin (IP) Receptor; 77 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6a 23953 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6a; binding activity assay AAP 10/25/2013 10/25/2013 2000001002 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/EC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6b; EC50: 66.0 nM; Prostacyclin (IP) Receptor; 66 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6b 23955 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6b; functional assay AAP 10/25/2013 10/25/2013 2000001003 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6b; IC50: 561.0 nM; Prostacyclin (IP) Receptor; 561 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6b 23955 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6b; binding activity assay AAP 10/25/2013 10/25/2013 2000001004 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/EC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6c; EC50: 138.0 nM; Prostacyclin (IP) Receptor; 138 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6c 23956 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID:5-(4-phenylbenzyl)oxazole-4-carboxamide, 6c; functional assay AAP 10/25/2013 10/25/2013 2000001005 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6c; IC50: 721.0 nM; Prostacyclin (IP) Receptor; 721 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6c 23956 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID:5-(4-phenylbenzyl)oxazole-4-carboxamide, 6c; binding assay AAP 10/25/2013 10/25/2013 2000001006 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/EC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6d; EC50: 278.0 nM; Prostacyclin (IP) Receptor; 278 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6d 23957 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6d; functional assay AAP 10/25/2013 10/25/2013 2000001007 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6d; IC50: 1230.0 nM; Prostacyclin (IP) Receptor; 1230 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6d 23957 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6d; binding assay AAP 10/25/2013 10/25/2013 2000001008 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/EC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6e; EC50: 2133.0 nM; Prostacyclin (IP) Receptor; 2133 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6e 23958 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6e; functional assay AAP 10/25/2013 10/25/2013 2000001009 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6e; IC50: 7160.0 nM; Prostacyclin (IP) Receptor; 7160 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6e 23958 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6e; binding assay AAP 10/25/2013 10/25/2013 2000001010 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6f; IC50: 331.0 nM; Prostacyclin (IP) Receptor; 331 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6f 23959 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6f; binding assay AAP 10/25/2013 10/25/2013 2000001011 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/EC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6f; EC50: 358.0 nM; Prostacyclin (IP) Receptor; 358 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6f 23959 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6f; functional assay AAP 10/25/2013 10/25/2013 2000001012 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/EC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6g; EC50: 51.0 nM; Prostacyclin (IP) Receptor; 51 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6g 23960 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6g; functional assay AAP 10/25/2013 10/25/2013 2000001013 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6g; IC50: 53.0 nM; Prostacyclin (IP) Receptor; 53 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6g 23960 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6g; binding assay AAP 10/25/2013 10/25/2013 2000001014 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/EC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6h; EC50: 296.0 nM; Prostacyclin (IP) Receptor; 296 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6h 23961 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6h; functional assay AAP 10/25/2013 10/25/2013 2000001015 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6h; IC50: 916.0 nM; Prostacyclin (IP) Receptor; 916 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6h 23961 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6h; binding assay AAP 10/25/2013 10/25/2013 2000001016 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/EC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6i; EC50: 831.0 nM; Prostacyclin (IP) Receptor; 831 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6i 23962 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6i; functional assay AAP 10/25/2013 10/25/2013 2000001017 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6i; IC50: 4200.0 nM; Prostacyclin (IP) Receptor; 4200 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6i 23962 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6i; binding assay AAP 10/25/2013 10/25/2013 2000001018 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/EC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6j; EC50: 16.0 nM; Prostacyclin (IP) Receptor; 16 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6j 23963 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6j; functional assay AAP 10/25/2013 10/25/2013 2000001019 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6j; IC50: 476.0 nM; Prostacyclin (IP) Receptor; 476 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6j 23963 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6j; binding assay AAP 10/25/2013 10/25/2013 2000001020 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/EC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6k; EC50: 1005.0 nM; Prostacyclin (IP) Receptor; 1005 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6k 23964 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6k; functional assay AAP 10/25/2013 10/25/2013 2000001021 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6k; IC50: 7600.0 nM; Prostacyclin (IP) Receptor; 7600 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6k 23964 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6k; binding assay AAP 10/25/2013 10/25/2013 2000001022 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/EC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6l; EC50: 741.0 nM; Prostacyclin (IP) Receptor; 741 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6l 23965 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6l; functional assay AAP 10/25/2013 10/25/2013 2000001023 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6l; IC50: 4950.0 nM; Prostacyclin (IP) Receptor; 4950 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6l 23965 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6l; binding assay AAP 10/25/2013 10/25/2013 2000001024 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/EC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6m; EC50: 476.0 nM; Prostacyclin (IP) Receptor; 476 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6m 23966 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6m; functional assay AAP 10/25/2013 10/25/2013 2000001025 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6m; IC50: 4710.0 nM; Prostacyclin (IP) Receptor; 4710 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6m 23966 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6m; binding assay AAP 10/25/2013 10/25/2013 2000001026 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/EC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6n; EC50: 828.0 nM; Prostacyclin (IP) Receptor; 828 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6n 23967 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6n; functional assay AAP 10/25/2013 10/25/2013 2000001027 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6n; IC50: 3480.0 nM; Prostacyclin (IP) Receptor; 3480 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6n 23967 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6n; binding assay AAP 10/25/2013 10/25/2013 2000001028 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/EC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6o; EC50: 3306.0 nM; Prostacyclin (IP) Receptor; 3306 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6o 23968 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6o; functional assay AAP 10/25/2013 10/25/2013 2000001029 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6o; IC50: 12200.0 nM; Prostacyclin (IP) Receptor; 12200 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6o 23968 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6o; binding assay AAP 10/25/2013 10/25/2013 2000001030 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/EC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6p; EC50: 3584.0 nM; Prostacyclin (IP) Receptor; 3584 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6p 23969 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6p; functional assay AAP 10/25/2013 10/25/2013 2000001031 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6p; IC50: 12400.0 nM; Prostacyclin (IP) Receptor; 12400 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6p 23969 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6p; binding assay AAP 10/25/2013 10/25/2013 2000001032 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/EC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6q; EC50: 3306.0 nM; Prostacyclin (IP) Receptor; 3306 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6q 23970 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6q; functional assay AAP 10/25/2013 10/25/2013 2000001033 Jodi P43119 5739 PTGIR Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6q; IC50: 34100.0 nM; Prostacyclin (IP) Receptor; 34100 nM 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6q 23970 pH: 7.4; temp: 22.00 C Y Y ECO:0000006 PubMed:17239589 BindingDB PENTACON Notes: Request ChEBI ID: 5-(4-phenylbenzyl)oxazole-4-carboxamide, 6q; binding assay AAP 10/25/2013 10/25/2013 2000001034 Chandra P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 alpha-substituted indomethacin ethanolamide, 14; IC50: 250.0 nM; Cyclooxygenase-2; CHEBI:133883 250 nM alpha-substituted indomethacin ethanolamide, 14 CHEBI:133883 22574 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:17656360 BindingDB AAP 10/25/2013 10/25/2013 2000001035 Chandra P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 alpha-substituted indomethacin ethanolamide, 15; IC50: 1000.0 nM; Cyclooxygenase-2; CHEBI:133523 1000 nM alpha-substituted indomethacin ethanolamide, 15 CHEBI:133523 22575 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:17656360 BindingDB AAP 10/25/2013 10/25/2013 2000001036 Chandra P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 alpha-substituted indomethacin ethanolamide, 16; IC50: 440.0 nM; Cyclooxygenase-2; CHEBI:133480 440 nM alpha-substituted indomethacin ethanolamide, 16 CHEBI:133480 22576 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:17656360 BindingDB AAP 10/25/2013 10/25/2013 2000001037 Chandra P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 alpha-substituted indomethacin ethanolamide, 17; IC50: 85.0 nM; Cyclooxygenase-2; CHEBI:133518 85 nM alpha-substituted indomethacin ethanolamide, 17 CHEBI:133518 22577 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:17656360 BindingDB AAP 10/25/2013 10/25/2013 2000001038 Chandra P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 alpha-substituted indomethacin ethanolamide, 6; IC50: 170.0 nM; Cyclooxygenase-2; CHEBI:133605 170 nM alpha-substituted indomethacin ethanolamide, 6 CHEBI:133605 22569 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:17656360 BindingDB AAP 10/25/2013 10/25/2013 2000001039 Chandra P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 alpha-substituted indomethacin ethanolamide, 7; IC50: 270.0 nM; Cyclooxygenase-2; CHEBI:133693 270 nM alpha-substituted indomethacin ethanolamide, 7 CHEBI:133693 22571 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:17656360 BindingDB AAP 10/25/2013 10/25/2013 2000001040 Chandra P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 alpha-substituted indomethacin ethanolamide, 8; IC50: 100.0 nM; Cyclooxygenase-2; CHEBI:133692 100 nM alpha-substituted indomethacin ethanolamide, 8 CHEBI:133692 22572 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:17656360 BindingDB AAP 10/25/2013 10/25/2013 2000001041 Chandra P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 alpha-substituted indomethacin ethanolamide, 9; IC50: 280.0 nM; Cyclooxygenase-2; CHEBI:134429 280 nM alpha-substituted indomethacin ethanolamide, 9 CHEBI:134429 22573 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:17656360 BindingDB AAP 10/25/2013 10/25/2013 2000001042 Chandra P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 thiazolidinone derivative, 7; IC50: 262000.0 nM; Cyclooxygenase-2; 262000 nM thiazolidinone derivative, 7 arachidonic acid CHEBI:15843 22342 pH: 8; temp: 37.00 C Y Y ECO:0000006 PubMed:18311898 BindingDB PENTACON Notes: Request ChEBI ID: thiazolidinone derivative, 7 AAP 10/25/2013 10/25/2013 2000001043 Jenn O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indeno[1,2-c]pyridazin-5-one; IC50: 3800.0 nM; Prostaglandin D Synthase; 3800 nM Indeno[1,2-c]pyridazin-5-one monochlorobimane CHEBI:52158 21629 pH: 7.2; temp: 22.00 C Y Y ECO:0000006 PubMed:18341273 BindingDB PENTACON Notes: Request ChEBI ID: Indeno[1,2-c]pyridazin-5-one, CHEMBL125044 AAP 10/25/2013 10/25/2013 2000001044 Jenn O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Methoxynaphthalen-1-yl, 8; IC50: 12400.0 nM; Prostaglandin D Synthase; 12400 nM Methoxynaphthalen-1-yl, 8 monochlorobimane CHEBI:52158 21620 pH: 7.2; temp: 22.00 C Y Y ECO:0000006 PubMed:18341273 BindingDB PENTACON Notes: Request ChEBI ID: Methoxynaphthalen-1-yl, 8, Chembl ID: CHEMBL260489 AAP 10/25/2013 10/25/2013 2000001045 Jenn O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Phenol, 11; IC50: 17400.0 nM; Prostaglandin D Synthase; 17400 nM Phenol, 11 monochlorobimane CHEBI:52158 21623 pH: 7.2; temp: 22.00 C Y Y ECO:0000006 PubMed:18341273 BindingDB PENTACON Notes: Request ChEBI ID: Phenol, 11 Chembl ID: CHEMBL261678 AAP 10/25/2013 10/25/2013 2000001046 Jenn O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Phenylisothiazole-5-carboxamide, 15; IC50: 75.0 nM; Prostaglandin D Synthase; 75 nM Phenylisothiazole-5-carboxamide, 15 monochlorobimane CHEBI:52158 21627 pH: 7.2; temp: 22.00 C Y Y ECO:0000006 PubMed:18341273 BindingDB PENTACON Notes: Request ChEBI ID: Phenylisothiazole-5-carboxamide, 15,Chembl ID: CHEMBL258506 AAP 10/25/2013 10/25/2013 2000001047 Jenn O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Phenylpyridazine-3-carboxylate, 7; IC50: 45000.0 nM; Prostaglandin D Synthase; 45000 nM Phenylpyridazine-3-carboxylate, 7 monochlorobimane CHEBI:52158 21619 pH: 7.2; temp: 22.00 C Y Y ECO:0000006 PubMed:18341273 BindingDB PENTACON Notes: Request ChEBI ID: Phenylpyridazine-3-carboxylate, 7, Pubchem ID: CID 24776310 AAP 10/25/2013 10/25/2013 2000001048 Jenn O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Pyrazol-5-amine, 5; IC50: 33000.0 nM; Prostaglandin D Synthase; 33000 nM Pyrazol-5-amine, 5 monochlorobimane CHEBI:52158 21617 pH: 7.2; temp: 22.00 C Y Y ECO:0000006 PubMed:18341273 BindingDB PENTACON Notes: Request ChEBI ID: Pyrazol-5-amine, 5, Chembl ID: CHEMBL405844 AAP 10/25/2013 10/25/2013 2000001049 Jenn O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Pyrazole, 1; IC50: 890000.0 nM; Prostaglandin D Synthase; 890000 nM Pyrazole, 1 monochlorobimane CHEBI:52158 21615 pH: 7.2; temp: 22.00 C Y Y ECO:0000006 PubMed:18341273 BindingDB PENTACON Notes: Request ChEBI ID: Pyrazole, 1, Chembl ID: CHEMBL406105 AAP 10/25/2013 10/25/2013 2000001050 Jenn O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Pyrazole, 9; IC50: 26400.0 nM; Prostaglandin D Synthase; 26400 nM Pyrazole, 9 monochlorobimane CHEBI:52158 21621 pH: 7.2; temp: 22.00 C Y Y ECO:0000006 PubMed:18341273 BindingDB PENTACON Notes: Request ChEBI ID: Pyrazole, 9, Chembl ID: CHEMBL408265 AAP 10/25/2013 10/25/2013 2000001051 Jenn O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Pyrazolylisoxazole, 14; IC50: 920.0 nM; Prostaglandin D Synthase; 920 nM Pyrazolylisoxazole, 14 monochlorobimane CHEBI:52158 21626 pH: 7.2; temp: 22.00 C Y Y ECO:0000006 PubMed:18341273 BindingDB PENTACON Notes: Request ChEBI ID: Pyrazolylisoxazole, 14 Chembl ID: CHEMBL265720 AAP 10/25/2013 10/25/2013 2000001052 Jenn O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Pyrazolylthiazole, 13; IC50: 21.0 nM; Prostaglandin D Synthase; 21 nM Pyrazolylthiazole, 13 monochlorobimane CHEBI:52158 21625 pH: 7.2; temp: 22.00 C Y Y ECO:0000006 PubMed:18341273 BindingDB PENTACON Notes: Request ChEBI ID: Pyrazolylthiazole, 13, Chembl ID: CHEMBL261777 AAP 10/25/2013 10/25/2013 2000001053 Jenn O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Pyridine-3-carboxylate; IC50: 1500.0 nM; Prostaglandin D Synthase; 1500 nM Pyridine-3-carboxylate monochlorobimane CHEBI:52158 21628 pH: 7.2; temp: 22.00 C Y Y ECO:0000006 PubMed:18341273 BindingDB PENTACON Notes: Request ChEBI ID: Pyridine-3-carboxylate AAP 10/25/2013 10/25/2013 2000001054 Jenn O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Pyridine, 10; IC50: 34700.0 nM; Prostaglandin D Synthase; 34700 nM Pyridine, 10 monochlorobimane CHEBI:52158 21622 pH: 7.2; temp: 22.00 C Y Y ECO:0000006 PubMed:18341273 BindingDB PENTACON Notes: Request ChEBI ID: Pyridine, 10, Chembl ID: CHEMBL260289 AAP 10/25/2013 10/25/2013 2000001055 Jenn O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Thiazole, 4; IC50: 994.0 nM; Prostaglandin D Synthase; 994 nM Thiazole, 4 monochlorobimane CHEBI:52158 21616 pH: 7.2; temp: 22.00 C Y Y ECO:0000006 PubMed:18341273 BindingDB PENTACON Notes: Request ChEBI ID: Thiazole, 4, Chembl ID: CHEMBL264951 AAP 10/25/2013 10/25/2013 2000001056 Jenn O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Thiazylamino,ol 12; IC50: 138.0 nM; Prostaglandin D Synthase; 138 nM Thiazolylamino, 12 monochlorobimane CHEBI:52158 21624 pH: 7.2; temp: 22.00 C Y Y ECO:0000006 PubMed:18341273 BindingDB PENTACON Notes: Request ChEBI ID: Thiazolylamino, 12, Chembl ID: CHEMBL258467 AAP 10/25/2013 10/25/2013 2000001057 Jenn O60760 27306 HPGDS Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Tranilast; IC50: 11600.0 nM; Prostaglandin D Synthase; 11600 nM Tranilast monochlorobimane CHEBI:52158 21613 pH: 7.2; temp: 22.00 C Y Y ECO:0000006 PubMed:18341273 BindingDB PENTACON Notes: Request CHebi ID: Tranilast Chembl ID: CHEMBL415324 AAP 10/25/2013 10/25/2013 2000001058 Jenn P42330 8644 AKR1C3 Homo sapiens 9606 Comment/biophysicochemical properties/Ki 3,5-dichlorosalicylic acid; Ki: 94000.0 nM; 17-beta-Hydroxysteroid Dehydrogenase 5 (17-beta-HSD5, AKR1C3); CHEBI:560901 94000 nM 3,5-dichlorosalicylic acid NADP CHEBI:25523 26269 pH: 7.4; temp: 25.00 C Y Y ECO:0000006 PubMed:18620380 BindingDB PENTACON Notes: Request ChEBI ID: 3,5-dichlorosalicylic acid Chembl ID: CHEMBL449129 AAP 10/25/2013 10/25/2013 2000001059 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: <3e+2 nM; Cyclooxygenase-2 (COX-2); nM Celecoxib CHEBI:41423 arachidonic acid CHEBI:15843 91683 Y Y ECO:0000006 PubMed:18951238 BindingDB AAP 10/25/2013 10/25/2013 2000001060 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: >1.00e+5 nM; Cyclooxygenase-1 (COX-1); nM Celecoxib CHEBI:41423 arachidonic acid CHEBI:15843 91683 Y Y ECO:0000006 PubMed:18951238 BindingDB AAP 10/25/2013 10/25/2013 2000001061 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin; IC50: 260.0 nM; Cyclooxygenase-1 (COX-1); CHEBI:100173 (indomethacin) 260 nM indomethacin CHEBI:100173 arachidonic acid CHEBI:15843 17638 Y Y ECO:0000006 PubMed:18951238 BindingDB AAP 10/25/2013 10/25/2013 2000001062 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Indomethacin; IC50: 2630.0 nM; Cyclooxygenase-2 (COX-2); CHEBI:100173 (indomethacin) 2630 nM indomethacin CHEBI:100173 arachidonic acid CHEBI:15843 17638 Y Y ECO:0000006 PubMed:18951238 BindingDB AAP 10/25/2013 10/25/2013 2000001063 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Pyrazolyl benzenesulfonamide derivative, 7a; IC50: 1350.0 nM; Cyclooxygenase-2 (COX-2); 1350 nM Pyrazolyl benzenesulfonamide derivative, 7a arachidonic acid CHEBI:15843 91678 Y Y ECO:0000006 PubMed:18951238 BindingDB PENTACON Notes: Request ChEBI ID: Pyrazolyl benzenesulfonamide derivative, 7a Pubchem ID: CID 57411990 AAP 10/25/2013 10/25/2013 2000001064 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Pyrazolyl benzenesulfonamide derivative, 7a; IC50: 83620.0 nM; Cyclooxygenase-1 (COX-1); 83620 nM Pyrazolyl benzenesulfonamide derivative, 7a arachidonic acid CHEBI:15843 91678 Y Y ECO:0000006 PubMed:18951238 BindingDB PENTACON Notes: Request ChEBI ID: Pyrazolyl benzenesulfonamide derivative, 7a Pubchem ID: CID 57411990 AAP 10/25/2013 10/25/2013 2000001065 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Pyrazolyl benzenesulfonamide derivative, 7b; IC50: 1260.0 nM; Cyclooxygenase-2 (COX-2); 1260 nM Pyrazolyl benzenesulfonamide derivative, 7b arachidonic acid CHEBI:15843 91679 Y Y ECO:0000006 PubMed:18951238 BindingDB PENTACON Notes: Request ChEBI ID: Pyrazolyl benzenesulfonamide derivative, 7b, Pubchem ID: CID 57411991 AAP 10/25/2013 10/25/2013 2000001066 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Pyrazolyl benzenesulfonamide derivative, 7b; IC50: 76410.0 nM; Cyclooxygenase-1 (COX-1); 76410 nM Pyrazolyl benzenesulfonamide derivative, 7b arachidonic acid CHEBI:15843 91679 Y Y ECO:0000006 PubMed:18951238 BindingDB PENTACON Notes: Request ChEBI ID: Pyrazolyl benzenesulfonamide derivative, 7b, Pubchem ID: CID 57411991 AAP 10/25/2013 10/25/2013 2000001067 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Pyrazolyl benzenesulfonamide derivative, 9a; IC50: 780.0 nM; Cyclooxygenase-2 (COX-2); 780 nM Pyrazolyl benzenesulfonamide derivative, 9a arachidonic acid CHEBI:15843 91684 Y Y ECO:0000006 PubMed:18951238 BindingDB PENTACON Notes: Request ChEBI ID: Pyrazolyl benzenesulfonamide derivative, 9a, Pubchem ID: CID 25227547 AAP 10/25/2013 10/25/2013 2000001068 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Pyrazolyl benzenesulfonamide derivative, 9a; IC50: >1.00e+5 nM; Cyclooxygenase-1 (COX-1); nM Pyrazolyl benzenesulfonamide derivative, 9a arachidonic acid CHEBI:15843 91684 Y Y ECO:0000006 PubMed:18951238 BindingDB PENTACON Notes: Request ChEBI ID: Pyrazolyl benzenesulfonamide derivative, 9a, Pubchem ID: CID 25227547 AAP 10/25/2013 10/25/2013 2000001069 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Pyrazolyl benzenesulfonamide derivative, 9b; IC50: 920.0 nM; Cyclooxygenase-2 (COX-2); 920 nM Pyrazolyl benzenesulfonamide derivative, 9b arachidonic acid CHEBI:15843 91685 Y Y ECO:0000006 PubMed:18951238 BindingDB PENTACON Notes: Request ChEBI ID: Pyrazolyl benzenesulfonamide derivative, 9b, Pubchem ID: CID 25227548 AAP 10/25/2013 10/25/2013 2000001070 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Pyrazolyl benzenesulfonamide derivative, 9b; IC50: 94220.0 nM; Cyclooxygenase-1 (COX-1); 94220 nM Pyrazolyl benzenesulfonamide derivative, 9b arachidonic acid CHEBI:15843 91685 Y Y ECO:0000006 PubMed:18951238 BindingDB PENTACON Notes: Request ChEBI ID: Pyrazolyl benzenesulfonamide derivative, 9b, Pubchem ID: CID 25227548 AAP 10/25/2013 10/25/2013 2000001071 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 5a; IC50: 210.0 nM; Cyclooxygenase-2 (COX-2); 210 nM 3-benzyl-2-(4-methylsulfonylphenyl)-1,3- oxazolidine-4(5H)-one, COX inhibitor, 5a arachidonic acid CHEBI:15843 93103 Y Y ECO:0000006 Zarghi, A.; Arefi, H.; Dadrass, O.G.; Torabi S.: Design and synthesis of new 2-aryl, 3-benzyl-(1,3-oxazolidine or 1,3-thiazolidine)-4-ones as selective cyclooxygenase (COX-2) inhibitors. Medicinal Chemistry Research (2012); 19(8):782-793. BindingDB PENTACON Notes: Request ChEBI ID: 3-benzyl-2-(4-methylsulfonylphenyl)-1,3- oxazolidine-4(5H)-one AAP 10/25/2013 10/25/2013 2000001072 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 5a; IC50: >1.00e+5 nM; Cyclooxygenase-1 (COX-1); nM 3-benzyl-2-(4-methylsulfonylphenyl)-1,3- oxazolidine-4(5H)-one, COX inhibitor, 5a arachidonic acid CHEBI:15843 93103 Y Y ECO:0000006 Zarghi, A.; Arefi, H.; Dadrass, O.G.; Torabi S.: Design and synthesis of new 2-aryl, 3-benzyl-(1,3-oxazolidine or 1,3-thiazolidine)-4-ones as selective cyclooxygenase (COX-2) inhibitors. Medicinal Chemistry Research (2012); 19(8):782-793. BindingDB PENTACON Notes: Request ChEBI ID: 3-benzyl-2-(4-methylsulfonylphenyl)-1,3- oxazolidine-4(5H)-one AAP 10/25/2013 10/25/2013 2000001073 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 5b; IC50: 320.0 nM; Cyclooxygenase-2 (COX-2); 320 nM 3-Benzyl-2-(4-methylsulfonylphenyl)-1,3-thiazolidine 4(5H)-one, COX inhibitor, 5b arachidonic acid CHEBI:15843 93104 Y Y ECO:0000006 Zarghi, A.; Arefi, H.; Dadrass, O.G.; Torabi S.: Design and synthesis of new 2-aryl, 3-benzyl-(1,3-oxazolidine or 1,3-thiazolidine)-4-ones as selective cyclooxygenase (COX-2) inhibitors. Medicinal Chemistry Research (2012); 19(8):782-793. BindingDB PENTACON Notes: Request ChEBI ID: 3-Benzyl-2-(4-methylsulfonylphenyl)-1,3-thiazolidine 4(5H)-one AAP 10/25/2013 10/25/2013 2000001074 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 5b; IC50: >1.00e+5 nM; Cyclooxygenase-1 (COX-1); nM 3-Benzyl-2-(4-methylsulfonylphenyl)-1,3-thiazolidine 4(5H)-one, COX inhibitor, 5b arachidonic acid CHEBI:15843 93104 Y Y ECO:0000006 Zarghi, A.; Arefi, H.; Dadrass, O.G.; Torabi S.: Design and synthesis of new 2-aryl, 3-benzyl-(1,3-oxazolidine or 1,3-thiazolidine)-4-ones as selective cyclooxygenase (COX-2) inhibitors. Medicinal Chemistry Research (2012); 19(8):782-793. BindingDB PENTACON Notes: Request ChEBI ID: 3-Benzyl-2-(4-methylsulfonylphenyl)-1,3-thiazolidine 4(5H)-one AAP 10/25/2013 10/25/2013 2000001075 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 8; IC50: 270.0 nM; Cyclooxygenase-2 (COX-2); 270 nM 3-Benzyl-5-methyl-2-(4-methylsufonylphenyl)-1,3-oxazolidine 4(5H)-one, COX inhibitor, 8 arachidonic acid CHEBI:15843 93105 Y Y ECO:0000006 Zarghi, A.; Arefi, H.; Dadrass, O.G.; Torabi S.: Design and synthesis of new 2-aryl, 3-benzyl-(1,3-oxazolidine or 1,3-thiazolidine)-4-ones as selective cyclooxygenase (COX-2) inhibitors. Medicinal Chemistry Research (2012); 19(8):782-793. BindingDB PENTACON Notes: Request ChEBI ID: 3-Benzyl-5-methyl-2-(4-methylsufonylphenyl)-1,3-oxazolidine 4(5H)-one AAP 10/25/2013 10/25/2013 2000001076 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 8; IC50: 85900.0 nM; Cyclooxygenase-1 (COX-1); 85900 nM 3-Benzyl-5-methyl-2-(4-methylsufonylphenyl)-1,3-oxazolidine 4(5H)-one, COX inhibitor, 8 arachidonic acid CHEBI:15843 93105 Y Y ECO:0000006 Zarghi, A.; Arefi, H.; Dadrass, O.G.; Torabi S.: Design and synthesis of new 2-aryl, 3-benzyl-(1,3-oxazolidine or 1,3-thiazolidine)-4-ones as selective cyclooxygenase (COX-2) inhibitors. Medicinal Chemistry Research (2012); 19(8):782-793. BindingDB PENTACON Notes: Request ChEBI ID: 3-Benzyl-5-methyl-2-(4-methylsufonylphenyl)-1,3-oxazolidine 4(5H)-one AAP 10/25/2013 10/25/2013 2000001077 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 9; IC50: 340.0 nM; Cyclooxygenase-2 (COX-2); 340 nM 3-Benzyl-5-methyl-2-(4-methylsufonylphenyl)-1,3-thiazolidine 4(5H)-one, COX inhibitor, 9 arachidonic acid CHEBI:15843 93106 Y Y ECO:0000006 Zarghi, A.; Arefi, H.; Dadrass, O.G.; Torabi S.: Design and synthesis of new 2-aryl, 3-benzyl-(1,3-oxazolidine or 1,3-thiazolidine)-4-ones as selective cyclooxygenase (COX-2) inhibitors. Medicinal Chemistry Research (2012); 19(8):782-793. BindingDB PENTACON Notes: Request ChEBI ID: 3-Benzyl-5-methyl-2-(4-methylsufonylphenyl)-1,3-thiazolidine 4(5H)-one AAP 10/25/2013 10/25/2013 2000001078 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 9; IC50: 75600.0 nM; Cyclooxygenase-1 (COX-1); 75600 nM 3-Benzyl-5-methyl-2-(4-methylsufonylphenyl)-1,3-thiazolidine 4(5H)-one, COX inhibitor, 9 arachidonic acid CHEBI:15843 93106 Y Y ECO:0000006 Zarghi, A.; Arefi, H.; Dadrass, O.G.; Torabi S.: Design and synthesis of new 2-aryl, 3-benzyl-(1,3-oxazolidine or 1,3-thiazolidine)-4-ones as selective cyclooxygenase (COX-2) inhibitors. Medicinal Chemistry Research (2012); 19(8):782-793. BindingDB PENTACON Notes: Request ChEBI ID: 3-Benzyl-5-methyl-2-(4-methylsufonylphenyl)-1,3-thiazolidine 4(5H)-one AAP 10/25/2013 10/25/2013 2000001079 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 2a; IC50: 350 nM; Cyclooxygenase-2 (COX-2); 350 nM 2-(4-Methylsulfonylphenyl)-3-phenyl-1,3-benzdiazinan-4-one, COX inhibitor, 2a arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-Methylsulfonylphenyl)-3-phenyl-1,3-benzdiazinan-4-one AAP 2000001080 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 2a; IC50: 99800 nM; Cyclooxygenase-1 (COX-1); 99800 nM 2-(4-Methylsulfonylphenyl)-3-phenyl-1,3-benzdiazinan-4-one, COX inhibitor, 2a arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-Methylsulfonylphenyl)-3-phenyl-1,3-benzdiazinan-4-one AAP 2000001081 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 2b; IC50: 70 nM; Cyclooxygenase-2 (COX-2); 70 nM 3-(4-Fluorophenyl)-2-(4-methylsulfonylphenyl)-1,3-benzdiazinan-4-one, COX inhibitor, 2b arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Fluorophenyl)-2-(4-methylsulfonylphenyl)-1,3-benzdiazinan-4-one AAP 2000001082 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 2b; IC50: 40100 nM; Cyclooxygenase-1 (COX-1); 40100 nM 3-(4-Fluorophenyl)-2-(4-methylsulfonylphenyl)-1,3-benzdiazinan-4-one, COX inhibitor, 2b arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Fluorophenyl)-2-(4-methylsulfonylphenyl)-1,3-benzdiazinan-4-one AAP 2000001083 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 2c; IC50: 170 nM; Cyclooxygenase-2 (COX-2); 170 nM 3-(4-Chlorophenyl)-2-(4-methylsulfonylphenyl)-1,3-benzdiazinan-4-one, COX inhibitor, 2c arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Chlorophenyl)-2-(4-methylsulfonylphenyl)-1,3-benzdiazinan-4-one AAP 2000001084 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 2c; IC50: 17700 nM; Cyclooxygenase-1 (COX-1); 17700 nM 3-(4-Chlorophenyl)-2-(4-methylsulfonylphenyl)-1,3-benzdiazinan-4-one, COX inhibitor, 2c arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Chlorophenyl)-2-(4-methylsulfonylphenyl)-1,3-benzdiazinan-4-one AAP 2000001085 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 2d; IC50: 100 nM; Cyclooxygenase-2 (COX-2); 100 nM 3-(4-Methylphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzdiazinan-4-one, COX inhibitor, 2d arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Methylphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzdiazinan-4-one AAP 2000001086 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 2d; IC50: 37200 nM; Cyclooxygenase-1 (COX-1); 37200 nM 3-(4-Methylphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzdiazinan-4-one, COX inhibitor, 2d arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Methylphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzdiazinan-4-one AAP 2000001087 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 2e; IC50: 70 nM; Cyclooxygenase-2 (COX-2); 70 nM 3-(4-Methoxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzdiazinan-4-one, COX inhibitor, 2e arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Methoxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzdiazinan-4-one AAP 2000001088 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 2e; IC50: 33400 nM; Cyclooxygenase-1 (COX-1); 33400 nM 3-(4-Methoxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzdiazinan-4-one, COX inhibitor, 2e arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Methoxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzdiazinan-4-one AAP 2000001089 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 4a; IC50: 120 nM; Cyclooxygenase-2 (COX-2); 120 nM 3-(4-Methylsulfonylphenyl)-2-phenyl-1,3-benzdiazinan-4- one, COX inhibitor, 4a arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Methylsulfonylphenyl)-2-phenyl-1,3-benzdiazinan-4- one AAP 2000001090 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 4a; IC50: 24100 nM; Cyclooxygenase-1 (COX-1); 24100 nM 3-(4-Methylsulfonylphenyl)-2-phenyl-1,3-benzdiazinan-4- one, COX inhibitor, 4a arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Methylsulfonylphenyl)-2-phenyl-1,3-benzdiazinan-4- one AAP 2000001091 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 4b; IC50: 90 nM; Cyclooxygenase-2 (COX-2); 90 nM 2-(4-Fluorophenyl)-3-(4-methylsulfonylphenyl)-1,3- benzdiazinan-4-one, COX inhibitor, 4b arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-Fluorophenyl)-3-(4-methylsulfonylphenyl)-1,3- benzdiazinan-4-one AAP 2000001092 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 4b; IC50: 31800 nM; Cyclooxygenase-1 (COX-1); 31800 nM 2-(4-Fluorophenyl)-3-(4-methylsulfonylphenyl)-1,3- benzdiazinan-4-one, COX inhibitor, 4b arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-Fluorophenyl)-3-(4-methylsulfonylphenyl)-1,3- benzdiazinan-4-one AAP 2000001093 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 4c; IC50: 220 nM; Cyclooxygenase-2 (COX-2); 220 nM 2-(4-Chlorophenyl)-3-(4-methylsulfonylphenyl)-1,3- benzdiazinan-4-one, COX inhibitor, 4c arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-Chlorophenyl)-3-(4-methylsulfonylphenyl)-1,3- benzdiazinan-4-one AAP 2000001094 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 4c; IC50: 20900 nM; Cyclooxygenase-1 (COX-1); 20900 nM 2-(4-Chlorophenyl)-3-(4-methylsulfonylphenyl)-1,3- benzdiazinan-4-one, COX inhibitor, 4c arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-Chlorophenyl)-3-(4-methylsulfonylphenyl)-1,3- benzdiazinan-4-one AAP 2000001095 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 4d; IC50: 110 nM; Cyclooxygenase-2 (COX-2); 110 nM 2-(4-Methylphenyl)-3-(4-methylsulfonylphenyl)-1,3- benzdiazinan-4-one, COX inhibitor, 4d arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-Methylphenyl)-3-(4-methylsulfonylphenyl)-1,3- benzdiazinan-4-one AAP 2000001096 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 4d; IC50: 24100 nM; Cyclooxygenase-1 (COX-1); 24100 nM 2-(4-Methylphenyl)-3-(4-methylsulfonylphenyl)-1,3- benzdiazinan-4-one, COX inhibitor, 4d arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-Methylphenyl)-3-(4-methylsulfonylphenyl)-1,3- benzdiazinan-4-one AAP 2000001097 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 4e; IC50: 110 nM; Cyclooxygenase-2 (COX-2); 110 nM 2-(4-Methoxyphenyl)-3-(4-methylsulfonylphenyl)-1,3- benzdiazinan-4-one, COX inhibitor, 4e arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-Methoxyphenyl)-3-(4-methylsulfonylphenyl)-1,3- benzdiazinan-4-one AAP 2000001098 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 COX inhibitor, 4e; IC50: 29700 nM; Cyclooxygenase-1 (COX-1); 29700 nM 2-(4-Methoxyphenyl)-3-(4-methylsulfonylphenyl)-1,3- benzdiazinan-4-one, COX inhibitor, 4e arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-Methoxyphenyl)-3-(4-methylsulfonylphenyl)-1,3- benzdiazinan-4-one AAP 2000001099 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 60.0 nM; Cyclooxygenase-2 (COX-2); CHEBI:118694 (celecoxib) 60 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON Added by PENTACON AAP 2000001100 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 24300.0 nM; Cyclooxygenase-1 (COX-1); CHEBI:118694 (celecoxib) 24300 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:22076641 PENTACON Added by PENTACON AAP 2000001101 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 60.0 nM; Cyclooxygenase-2 (COX-2); CHEBI:118694 (celecoxib) 60 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:21886896 PENTACON Added by PENTACON AAP 2000001102 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 24300.0 nM; Cyclooxygenase-1 (COX-1); CHEBI:118694 (celecoxib) 24300 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:21886896 PENTACON Added by PENTACON AAP 2000001103 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-[4-(Methylsulfonyl)phenyl]-5-phenylimidazolidine-2,4-dione (5-[4-(Methylsulfonyl)phenyl]-5-phenylhydantoin, Cox Inhibitor, 4; IC50: 77 nM; Cyclooxygenase-2 (COX-2); 77 nM 5-[4-(Methylsulfonyl)phenyl]-5-phenylimidazolidine-2,4-dione (5-[4-(Methylsulfonyl)phenyl]-5-phenylhydantoin arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:21886896 PENTACON PENTACON Notes: Request ChEBI ID: 5-[4-(Methylsulfonyl)phenyl]-5-phenylimidazolidine-2,4-dione (5-[4-(Methylsulfonyl)phenyl]-5-phenylhydantoin' AAP 2000001104 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-[4-(Methylsulfonyl)phenyl]-5-phenylimidazolidine-2,4-dione (5-[4-(Methylsulfonyl)phenyl]-5-phenylhydantoin, Cox Inhibitor 4; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); nM 5-[4-(Methylsulfonyl)phenyl]-5-phenylimidazolidine-2,4-dione (5-[4-(Methylsulfonyl)phenyl]-5-phenylhydantoin arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:21886896 PENTACON PENTACON Notes: Request ChEBI ID: 5-[4-(Methylsulfonyl)phenyl]-5-phenylimidazolidine-2,4-dione (5-[4-(Methylsulfonyl)phenyl]-5-phenylhydantoin' AAP 2000001105 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-Methyl-5-[4-(methylsulfonyl)phenyl]-5-phenylimidazolidine-2,4-dione (N-3-Methyl-5-(4-(methylsulfonyl)phenyl)-5-phenylhydantoin, Cox Inhibitor, 5; IC50: 81 nM; Cyclooxygenase-2 (COX-2); 81 nM 5-[4-(Methylsulfonyl)phenyl]-5-phenylimidazolidine-2,4-dione (5-[4-(Methylsulfonyl)phenyl]-5-phenylhydantoin arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:21886896 PENTACON PENTACON Notes: Request ChEBI ID: 5-[4-(Methylsulfonyl)phenyl]-5-phenylimidazolidine-2,4-dione (5-[4-(Methylsulfonyl)phenyl]-5-phenylhydantoin' AAP 2000001106 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-Methyl-5-[4-(methylsulfonyl)phenyl]-5-phenylimidazolidine-2,4-dione (N-3-Methyl-5-(4-(methylsulfonyl)phenyl)-5-phenylhydantoin, Cox Inhibitor 5; IC50: 22690 nM; Cyclooxygenase-1 (COX-1); 22690 nM 3-Methyl-5-[4-(methylsulfonyl)phenyl]-5-phenylimidazolidine-2,4-dione (N-3-Methyl-5-(4-(methylsulfonyl)phenyl)-5-phenylhydantoin arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:21886896 PENTACON PENTACON Notes: Request ChEBI ID: 3-Methyl-5-[4-(methylsulfonyl)phenyl]-5-phenylimidazolidine-2,4-dione (N-3-Methyl-5-(4-(methylsulfonyl)phenyl)-5-phenylhydantoin AAP 2000001107 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-Ethyl-5-[4-(methylsulfonyl)phenyl]-5-phenylimidazolidine-2,4-dione (N-3-Ethyl-5-(4-(methylsulfonyl)phenyl)-5-phenylhydantoin, Cox Inhibitor, 6; IC50: 98 nM; Cyclooxygenase-2 (COX-2); 98 nM 3-Ethyl-5-[4-(methylsulfonyl)phenyl]-5-phenylimidazolidine-2,4-dione (N-3-Ethyl-5-(4-(methylsulfonyl)phenyl)-5-phenylhydantoin arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:21886896 PENTACON PENTACON Notes: Request ChEBI ID:3-Ethyl-5-[4-(methylsulfonyl)phenyl]-5-phenylimidazolidine-2,4-dione (N-3-Ethyl-5-(4-(methylsulfonyl)phenyl)-5-phenylhydantoin AAP 2000001108 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-Ethyl-5-[4-(methylsulfonyl)phenyl]-5-phenylimidazolidine-2,4-dione (N-3-Ethyl-5-(4-(methylsulfonyl)phenyl)-5-phenylhydantoin, Cox Inhibitor 6; IC50: 20210 nM; Cyclooxygenase-1 (COX-1); 20210 nM 3-Ethyl-5-[4-(methylsulfonyl)phenyl]-5-phenylimidazolidine-2,4-dione (N-3-Ethyl-5-(4-(methylsulfonyl)phenyl)-5-phenylhydantoin arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:21886896 PENTACON PENTACON Notes: Request ChEBI ID: 3-Ethyl-5-[4-(methylsulfonyl)phenyl]-5-phenylimidazolidine-2,4-dione (N-3-Ethyl-5-(4-(methylsulfonyl)phenyl)-5-phenylhydantoin AAP 2000001109 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-[4-(Methylsulfonyl)phenyl]-5-phenyl-3-propylimidazolidine-2,4-dione (5-(4-(Methylsulfonyl)phenyl)-5-phenyl-N-3-propyl-hydantoin, Cox Inhibitor, 7; IC50: 171 nM; Cyclooxygenase-2 (COX-2); 171 nM 5-[4-(Methylsulfonyl)phenyl]-5-phenyl-3-propylimidazolidine-2,4-dione (5-(4-(Methylsulfonyl)phenyl)-5-phenyl-N-3-propyl-hydantoin arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:21886896 PENTACON PENTACON Notes: Request ChEBI ID: 5-[4-(Methylsulfonyl)phenyl]-5-phenyl-3-propylimidazolidine-2,4-dione (5-(4-(Methylsulfonyl)phenyl)-5-phenyl-N-3-propyl-hydantoin AAP 2000001110 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-[4-(Methylsulfonyl)phenyl]-5-phenyl-3-propylimidazolidine-2,4-dione (5-(4-(Methylsulfonyl)phenyl)-5-phenyl-N-3-propyl-hydantoin, Cox Inhibitor 7; IC50: 12010 nM; Cyclooxygenase-1 (COX-1); 12010 nM 5-[4-(Methylsulfonyl)phenyl]-5-phenyl-3-propylimidazolidine-2,4-dione (5-(4-(Methylsulfonyl)phenyl)-5-phenyl-N-3-propyl-hydantoin arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:21886896 PENTACON PENTACON Notes: Request ChEBI ID: 5-[4-(Methylsulfonyl)phenyl]-5-phenyl-3-propylimidazolidine-2,4-dione (5-(4-(Methylsulfonyl)phenyl)-5-phenyl-N-3-propyl-hydantoin AAP 2000001111 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-[4-(Methylsulfonyl)phenyl]-5-phenyl-3-(prop-2-en-1-yl)imidazolidine-2,4-dione (N-3-Allyl-5-(4-(methylsulfonyl)phenyl)-5-phenylhydantoin, Cox Inhibitor, 8; IC50: 99 nM; Cyclooxygenase-2 (COX-2); 99 nM 5-[4-(Methylsulfonyl)phenyl]-5-phenyl-3-(prop-2-en-1-yl)imidazolidine-2,4-dione (N-3-Allyl-5-(4-(methylsulfonyl)phenyl)-5-phenylhydantoin arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:21886896 PENTACON PENTACON Notes: Request ChEBI ID: 5-[4-(Methylsulfonyl)phenyl]-5-phenyl-3-(prop-2-en-1-yl)imidazolidine-2,4-dione (N-3-Allyl-5-(4-(methylsulfonyl)phenyl)-5-phenylhydantoin AAP 2000001112 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 5-[4-(Methylsulfonyl)phenyl]-5-phenyl-3-(prop-2-en-1-yl)imidazolidine-2,4-dione (N-3-Allyl-5-(4-(methylsulfonyl)phenyl)-5-phenylhydantoin, Cox Inhibitor 8; IC50:14960 nM; Cyclooxygenase-1 (COX-1); 14960 nM 5-[4-(Methylsulfonyl)phenyl]-5-phenyl-3-(prop-2-en-1-yl)imidazolidine-2,4-dione (N-3-Allyl-5-(4-(methylsulfonyl)phenyl)-5-phenylhydantoin arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:21886896 PENTACON PENTACON Notes: Request ChEBI ID: 5-[4-(Methylsulfonyl)phenyl]-5-phenyl-3-(prop-2-en-1-yl)imidazolidine-2,4-dione (N-3-Allyl-5-(4-(methylsulfonyl)phenyl)-5-phenylhydantoin AAP 2000001113 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 60.0 nM; Cyclooxygenase-2 (COX-2); CHEBI:118694 (celecoxib) 60 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20650641 PENTACON Added by PENTACON AAP 2000001114 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 24300.0 nM; Cyclooxygenase-1 (COX-1); CHEBI:118694 (celecoxib) 24300 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20650641 PENTACON Added by PENTACON AAP 2000001115 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-(Acetamido)phenyl)-8-benzoyl-quinoline-4-carboxylic acid, Cox Inhibitor 5a; IC50: 80 nM; Cyclooxygenase-2 (COX-2); 80 nM 2-(4-(Acetamido)phenyl)-8-benzoyl-quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20650641 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-(Acetamido)phenyl)-8-benzoyl-quinoline-4-carboxylic acid AAP 2000001116 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-(Acetamido)phenyl)-8-benzoyl-quinoline-4-carboxylic acid, Cox Inhibitor 5a; IC50: 9200 nM; Cyclooxygenase-1 (COX-1); 9200 nM 2-(4-(Acetamido)phenyl)-8-benzoyl-quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20650641 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-(Acetamido)phenyl)-8-benzoyl-quinoline-4-carboxylic acid AAP 2000001117 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-(Acetamido)phenyl)-6-benzoyl-quioline-4-carboxylic acid, Cox Inhibitor 5b; IC50: 85 nM; Cyclooxygenase-2 (COX-2); 85 nM 2-(4-(Acetamido)phenyl)-6-benzoyl-quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20650641 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-(Acetamido)phenyl)-6-benzoyl-quinoline-4-carboxylic acid AAP 2000001118 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-(Acetamido)phenyl)-6-benzoyl-quinoline-4-carboxylic acid, Cox Inhibitor 5b; IC50: 21800 nM; Cyclooxygenase-1 (COX-1); 21800 nM 2-(4-(Acetamido)phenyl)-6-benzoyl-quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20650641 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-(Acetamido)phenyl)-6-benzoyl-quinoline-4-carboxylic acid AAP 2000001119 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 8-Benzoyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid, Cox Inhibitor 6a; IC50: 69 nM; Cyclooxygenase-2 (COX-2); 69 nM 8-Benzoyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20650641 PENTACON PENTACON Notes: Request ChEBI ID: 8-Benzoyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid AAP 2000001120 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 8-Benzoyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid, Cox Inhibitor 6a; IC50: 15900 nM; Cyclooxygenase-1 (COX-1); 15900 nM 8-Benzoyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20650641 PENTACON PENTACON Notes: Request ChEBI ID: 8-Benzoyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid AAP 2000001121 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 6-Benzoyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid, Cox Inhibitor 6b; IC50: 77 nM; Cyclooxygenase-2 (COX-2); 77 nM 6-Benzoyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20650641 PENTACON PENTACON Notes: Request ChEBI ID: 6-Benzoyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid AAP 2000001122 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 6-Benzoyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid, Cox Inhibitor 6b; IC50: 24400 nM; Cyclooxygenase-1 (COX-1); 24400 nM 6-Benzoyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20650641 PENTACON PENTACON Notes: Request ChEBI ID: 6-Benzoyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid AAP 2000001123 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-(Azido)phenyl)-8-benzoyl-quinoline-4-carboxylic acid, Cox Inhibitor 8a; IC50: 57 nM; Cyclooxygenase-2 (COX-2); 57 nM 2-(4-(Azido)phenyl)-8-benzoyl-quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20650641 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-(Azido)phenyl)-8-benzoyl-quinoline-4-carboxylic acid AAP 2000001124 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-(Azido)phenyl)-8-benzoyl-quinoline-4-carboxylic acid, Cox Inhibitor 8a; IC50: 65550 nM; Cyclooxygenase-1 (COX-1); 65550 nM 2-(4-(Azido)phenyl)-8-benzoyl-quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20650641 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-(Azido)phenyl)-8-benzoyl-quinoline-4-carboxylic acid AAP 2000001125 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-(Azido)phenyl)-6-benzoyl-quinoline-4-carboxylic acid, Cox Inhibitor 8b; IC50: 77 nM; Cyclooxygenase-2 (COX-2); 77 nM 2-(4-(Azido)phenyl)-6-benzoyl-quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20650641 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-(Azido)phenyl)-6-benzoyl-quinoline-4-carboxylic acid AAP 2000001126 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-(Azido)phenyl)-6-benzoyl-quinoline-4-carboxylic acid, Cox Inhibitor 8b; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); nM 2-(4-(Azido)phenyl)-6-benzoyl-quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20650641 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-(Azido)phenyl)-6-benzoyl-quinoline-4-carboxylic acid AAP 2000001127 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-carboxyl quinoline, Cox Inhibitor A; IC50: 91 nM; Cyclooxygenase-2 (COX-2); 91 nM 4-carboxyl quinoline arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20650641 PENTACON PENTACON Notes: Request ChEBI ID: 4-carboxyl quinoline AAP 2000001128 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-carboxyl quinoline, Cox Inhibitor A; IC50: 13400 nM; Cyclooxygenase-1 (COX-1); 13400 nM 4-carboxyl quinoline arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20650641 PENTACON PENTACON Notes: Request ChEBI ID: 4-carboxyl quinoline AAP 2000001129 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 60.0 nM; Cyclooxygenase-2 (COX-2); CHEBI:118694 (celecoxib) 60 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20061161 PENTACON Added by PENTACON AAP 2000001130 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 24300.0 nM; Cyclooxygenase-1 (COX-1); CHEBI:118694 (celecoxib) 24300 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20061161 PENTACON Added by PENTACON AAP 2000001131 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-(methylsulfonyl)phenyl)-3-phenylquinoline, Cox Inhibitor 4; IC50: 110 nM; Cyclooxygenase-2 (COX-2); 110 nM 2-(4-(methylsulfonyl)phenyl)-3-phenylquinoline arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20061161 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-(methylsulfonyl)phenyl)-3-phenylquinoline AAP 2000001132 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-(methylsulfonyl)phenyl)-3-phenylquinoline, Cox Inhibitor 4; IC50: 33500 nM; Cyclooxygenase-1 (COX-1); 33500 nM 2-(4-(methylsulfonyl)phenyl)-3-phenylquinoline arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20061161 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-(methylsulfonyl)phenyl)-3-phenylquinoline AAP 2000001133 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-methyl-2-(4-methylsulfonyl)phenyl)-3-phenylquinoline, Cox Inhibitor 5; IC50: 110 nM; Cyclooxygenase-2 (COX-2); 110 nM 4-methyl-2-(4-methylsulfonyl)phenyl)-3-phenylquinoline arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20061161 PENTACON PENTACON Notes: Request ChEBI ID: 4-methyl-2-(4-methylsulfonyl)phenyl)-3-phenylquinoline AAP 2000001134 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-methyl-2-(4-methylsulfonyl)phenyl)-3-phenylquinoline, Cox Inhibitor 5; IC50: 13300 nM; Cyclooxygenase-1 (COX-1); 13300 nM 4-methyl-2-(4-methylsulfonyl)phenyl)-3-phenylquinoline arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20061161 PENTACON PENTACON Notes: Request ChEBI ID:4-methyl-2-(4-methylsulfonyl)phenyl)-3-phenylquinoline AAP 2000001135 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3,4-diphenyl-2-(4-methylsulfonyl)phenyl)-quinoline, Cox Inhibitor 6; IC50: 130 nM; Cyclooxygenase-2 (COX-2); 130 nM 3,4-diphenyl-2-(4-methylsulfonyl)phenyl)-quinoline arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20061161 PENTACON PENTACON Notes: Request ChEBI ID: 3,4-diphenyl-2-(4-methylsulfonyl)phenyl)-quinoline AAP 2000001136 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3,4-diphenyl-2-(4-methylsulfonyl)phenyl)-quinoline, Cox Inhibitor 6; IC50: 10200 nM; Cyclooxygenase-1 (COX-1); 10200 nM 3,4-diphenyl-2-(4-methylsulfonyl)phenyl)-quinoline arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20061161 PENTACON PENTACON Notes: Request ChEBI ID:3,4-diphenyl-2-(4-methylsulfonyl)phenyl)-quinoline AAP 2000001137 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-amino-2-(4-(methylsulfonyl)phenyl)-3-phenylquinoline, Cox Inhibitor 7; IC50: 80 nM; Cyclooxygenase-2 (COX-2); 80 nM 4-amino-2-(4-(methylsulfonyl)phenyl)-3-phenylquinoline arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20061161 PENTACON PENTACON Notes: Request ChEBI ID: 4-amino-2-(4-(methylsulfonyl)phenyl)-3-phenylquinoline AAP 2000001138 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-amino-2-(4-(methylsulfonyl)phenyl)-3-phenylquinoline, Cox Inhibitor 7; IC50: 14400 nM; Cyclooxygenase-1 (COX-1); 14400 nM 4-amino-2-(4-(methylsulfonyl)phenyl)-3-phenylquinoline arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20061161 PENTACON PENTACON Notes: Request ChEBI ID: 4-amino-2-(4-(methylsulfonyl)phenyl)-3-phenylquinoline AAP 2000001139 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-(methylsulfonyl)phenyl)-3-phenylquinoline-4-carboxylic acid, Cox Inhibitor 8; IC50: 70 nM; Cyclooxygenase-2 (COX-2); 70 nM 2-(4-(methylsulfonyl)phenyl)-3-phenylquinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20061161 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-(methylsulfonyl)phenyl)-3-phenylquinoline-4-carboxylic acid AAP 2000001140 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-(methylsulfonyl)phenyl)-3-phenylquinoline-4-carboxylic acid, Cox Inhibitor 8; IC50: 48100 nM; Cyclooxygenase-1 (COX-1); 48100 nM 2-(4-(methylsulfonyl)phenyl)-3-phenylquinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20061161 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-(methylsulfonyl)phenyl)-3-phenylquinoline-4-carboxylic acid AAP 2000001141 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 60.0 nM; Cyclooxygenase-2 (COX-2); CHEBI:118694 (celecoxib) 60 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19596198 PENTACON Added by PENTACON AAP 2000001142 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 24300.0 nM; Cyclooxygenase-1 (COX-1); CHEBI:118694 (celecoxib) 24300 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19596198 PENTACON Added by PENTACON AAP 2000001143 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-Methylsulfonylphenyl)-3-phenyl-1,3-benzthiazinan-4-one, Cox Inhibitor 7a; IC50: 120 nM; Cyclooxygenase-2 (COX-2); 120 nM 2-(4-Methylsulfonylphenyl)-3-phenyl-1,3-benzthiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19596198 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-Methylsulfonylphenyl)-3-phenyl-1,3-benzthiazinan-4-one AAP 2000001144 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-Methylsulfonylphenyl)-3-phenyl-1,3-benzthiazinan-4-one, Cox Inhibitor 7a; IC50: 16500 nM; Cyclooxygenase-1 (COX-1); 16500 nM 2-(4-Methylsulfonylphenyl)-3-phenyl-1,3-benzthiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19596198 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-Methylsulfonylphenyl)-3-phenyl-1,3-benzthiazinan-4-one AAP 2000001145 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-Fluorophenyl)-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one, Cox Inhibitor 7b; IC50: 50 nM; Cyclooxygenase-2 (COX-2); 50 nM 3-(4-Fluorophenyl)-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19596198 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Fluorophenyl)-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one AAP 2000001146 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-Fluorophenyl)-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one, Cox Inhibitor 7b; IC50: 12950 nM; Cyclooxygenase-1 (COX-1); 12950 nM 3-(4-Fluorophenyl)-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19596198 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Fluorophenyl)-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one AAP 2000001147 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-Methylphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one, Cox Inhibitor 7c; IC50: 60.0 nM; Cyclooxygenase-2 (COX-2); 60 nM 3-(4-Methylphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19596198 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Methylphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one AAP 2000001148 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-Methylphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one, Cox Inhibitor 7c; IC50: 16120 nM; Cyclooxygenase-1 (COX-1); 16120 nM 3-(4-Methylphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19596198 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Methylphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one AAP 2000001149 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-Methoxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one, Cox Inhibitor 7d; IC50: 110 nM; Cyclooxygenase-2 (COX-2); 110 nM 3-(4-Methoxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19596198 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Methoxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one AAP 2000001150 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-Methoxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one, Cox Inhibitor 7d; IC50: 14840 nM; Cyclooxygenase-1 (COX-1); 14840 nM 3-(4-Methoxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19596198 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Methoxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one AAP 2000001151 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-Benzyl-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one, Cox Inhibitor 7e; IC50: 70 nM; Cyclooxygenase-2 (COX-2); 70 nM 3-Benzyl-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19596198 PENTACON PENTACON Notes: Request ChEBI ID:3-Benzyl-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one AAP 2000001152 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-Benzyl-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one, Cox Inhibitor 7e; IC50: 15800 nM; Cyclooxygenase-1 (COX-1); 15800 nM 3-Benzyl-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19596198 PENTACON PENTACON Notes: Request ChEBI ID:3-Benzyl-2-(4-methylsulfonylphenyl)-1,3-benzthiazinan-4-one AAP 2000001153 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-Methylsulfonylphenyl)-3-phenethyl-1,3-benzthiazinan-4-one, Cox Inhibitor 7f; IC50: 80 nM; Cyclooxygenase-2 (COX-2); 80 nM 2-(4-Methylsulfonylphenyl)-3-phenethyl-1,3-benzthiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19596198 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-Methylsulfonylphenyl)-3-phenethyl-1,3-benzthiazinan-4-one AAP 2000001154 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-Methylsulfonylphenyl)-3-phenethyl-1,3-benzthiazinan-4-one, Cox Inhibitor 7f; IC50: 15910 nM; Cyclooxygenase-1 (COX-1); 15910 nM 2-(4-Methylsulfonylphenyl)-3-phenethyl-1,3-benzthiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19596198 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-Methylsulfonylphenyl)-3-phenethyl-1,3-benzthiazinan-4-one AAP 2000001155 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 60.0 nM; Cyclooxygenase-2 (COX-2); CHEBI:118694 (celecoxib) 60 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19560931 PENTACON Added by PENTACON AAP 2000001156 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 24300.0 nM; Cyclooxygenase-1 (COX-1); CHEBI:118694 (celecoxib) 24300 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19560931 PENTACON Added by PENTACON AAP 2000001157 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-(methylsulfonyl)phenyl)-quinoline-4-carboxylic acid, Cox Inhibitor 4; IC50: 91 nM; Cyclooxygenase-2 (COX-2); 91 nM 2-(4-(methylsulfonyl)phenyl)-quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19560931 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-(methylsulfonyl)phenyl)-quinoline-4-carboxylic acid AAP 2000001158 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-(methylsulfonyl)phenyl)-quinoline-4-carboxylic acid, Cox Inhibitor 4; IC50: 13400 nM; Cyclooxygenase-1 (COX-1); 13400 nM 2-(4-(methylsulfonyl)phenyl)-quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19560931 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-(methylsulfonyl)phenyl)-quinoline-4-carboxylic acid AAP 2000001159 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 8-Methyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid, Cox Inhibitor 9a; IC50: 86 nM; Cyclooxygenase-2 (COX-2); 86 nM 8-Methyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19560931 PENTACON PENTACON Notes: Request ChEBI ID: 8-Methyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid AAP 2000001160 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 8-Methyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid, Cox Inhibitor 9a; IC50: 14200 nM; Cyclooxygenase-1 (COX-1); 14200 nM 8-Methyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19560931 PENTACON PENTACON Notes: Request ChEBI ID: 8-Methyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid AAP 2000001161 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 7,8-Dimethyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid, Cox Inhibitor 9b; IC50: 75 nM; Cyclooxygenase-2 (COX-2); 75 nM 7,8-Dimethyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19560931 PENTACON PENTACON Notes: Request ChEBI ID:7,8-Dimethyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid AAP 2000001162 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 7,8-Dimethyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid, Cox Inhibitor 9b; IC50: 14500 nM; Cyclooxygenase-1 (COX-1); 14500 nM 7,8-Dimethyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19560931 PENTACON PENTACON Notes: Request ChEBI ID: 7,8-Dimethyl-2-(4-(methylsulfonyl)phenyl)quinoline-4-carboxylic acid AAP 2000001163 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-(Methylsulfonyl)phenyl)-8-phenyl-quinoline-4-carboxylic acid, Cox Inhibitor 9c; IC50: 71 nM; Cyclooxygenase-2 (COX-2); 71 nM 2-(4-(Methylsulfonyl)phenyl)-8-phenyl-quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19560931 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-(Methylsulfonyl)phenyl)-8-phenyl-quinoline-4-carboxylic acid AAP 2000001164 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-(Methylsulfonyl)phenyl)-8-phenyl-quinoline-4-carboxylic acid, Cox Inhibitor 9c; IC50: 14700 nM; Cyclooxygenase-1 (COX-1); 14700 nM 2-(4-(Methylsulfonyl)phenyl)-8-phenyl-quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19560931 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-(Methylsulfonyl)phenyl)-8-phenyl-quinoline-4-carboxylic acid AAP 2000001165 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-(Methylsulfonyl)phenyl)benzo[h]quinoline-4-carboxylic acid, Cox Inhibitor 9d; IC50: 54 nM; Cyclooxygenase-2 (COX-2); 54 nM 2-(4-(Methylsulfonyl)phenyl)benzo[h]quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19560931 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-(Methylsulfonyl)phenyl)benzo[h]quinoline-4-carboxylic acid AAP 2000001166 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 2-(4-(Methylsulfonyl)phenyl)benzo[h]quinoline-4-carboxylic acid, Cox Inhibitor 9d; IC50: 17600 nM; Cyclooxygenase-1 (COX-1); 17600 nM 2-(4-(Methylsulfonyl)phenyl)benzo[h]quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19560931 PENTACON PENTACON Notes: Request ChEBI ID: 2-(4-(Methylsulfonyl)phenyl)benzo[h]quinoline-4-carboxylic acid AAP 2000001167 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 7,8,9,10-Tetrahydro-2-(4-(methylsulfonyl)phenyl)benzo[h]quinoline-4-carboxylic acid, Cox Inhibitor 9e; IC50: 43 nM; Cyclooxygenase-2 (COX-2); 43 nM 7,8,9,10-Tetrahydro-2-(4-(methylsulfonyl)phenyl)benzo[h]quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19560931 PENTACON PENTACON Notes: Request ChEBI ID: 7,8,9,10-Tetrahydro-2-(4-(methylsulfonyl)phenyl)benzo[h]quinoline-4-carboxylic acid AAP 2000001168 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 7,8,9,10-Tetrahydro-2-(4-(methylsulfonyl)phenyl)benzo[h]quinoline-4-carboxylic acid, Cox Inhibitor 9e; IC50: 22100 nM; Cyclooxygenase-1 (COX-1); 22100 nM 7,8,9,10-Tetrahydro-2-(4-(methylsulfonyl)phenyl)benzo[h]quinoline-4-carboxylic acid arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19560931 PENTACON PENTACON Notes: Request ChEBI ID: 7,8,9,10-Tetrahydro-2-(4-(methylsulfonyl)phenyl)benzo[h]quinoline-4-carboxylic acid AAP 2000001169 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 60.0 nM; Cyclooxygenase-2 (COX-2); CHEBI:118694 (celecoxib) 60 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19447036 PENTACON Added by PENTACON AAP 2000001170 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 24300.0 nM; Cyclooxygenase-1 (COX-1); CHEBI:118694 (celecoxib) 24300 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19447036 PENTACON Added by PENTACON AAP 2000001171 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-benzyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one, Cox Inhibitor 11a; IC50: 60.0 nM; Cyclooxygenase-2 (COX-2); 60 nM 3-benzyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19447036 PENTACON PENTACON Notes: Request ChEBI ID: 3-benzyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one AAP 2000001172 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-benzyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one, Cox Inhibitor 11a; IC50: 17150 nM; Cyclooxygenase-1 (COX-1); 17150 nM 3-benzyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19447036 PENTACON PENTACON Notes: Request ChEBI ID: 3-benzyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one AAP 2000001173 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-phenethyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one, Cox Inhibitor 11b; IC50: 70 nM; Cyclooxygenase-2 (COX-2); 70 nM 3-phenethyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19447036 PENTACON PENTACON Notes: Request ChEBI ID: 3-phenethyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one AAP 2000001174 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-phenethyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one, Cox Inhibitor 11b; IC50: 15980 nM; Cyclooxygenase-1 (COX-1); 15980 nM 3-phenethyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19447036 PENTACON PENTACON Notes: Request ChEBI ID: 3-phenethyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one AAP 2000001175 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-propyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one, Cox Inhibitor 11d; IC50: 110 nM; Cyclooxygenase-2 (COX-2); 110 nM 3-propyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19447036 PENTACON PENTACON Notes: Request ChEBI ID: 3-propyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one AAP 2000001176 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-propyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one, Cox Inhibitor 11d; IC50: 14120 nM; Cyclooxygenase-1 (COX-1); 14120 nM 3-propyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19447036 PENTACON PENTACON Notes: Request ChEBI ID: 3-propyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one AAP 2000001177 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-butyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one, Cox Inhibitor 11e; IC50: 80 nM; Cyclooxygenase-2 (COX-2); 80 nM 3-butyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19447036 PENTACON PENTACON Notes: Request ChEBI ID: 3-butyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one AAP 2000001178 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-butyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one, Cox Inhibitor 11e; IC50: 14800 nM; Cyclooxygenase-1 (COX-1); 14800 nM 3-butyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19447036 PENTACON PENTACON Notes: Request ChEBI ID: 3-butyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one AAP 2000001179 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-pentyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one, Cox Inhibitor 11f; IC50: 80 nM; Cyclooxygenase-2 (COX-2); 80 nM 3-pentyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19447036 PENTACON PENTACON Notes: Request ChEBI ID: 3-pentyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one AAP 2000001180 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-pentyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one, Cox Inhibitor 11f; IC50: 14910 nM; Cyclooxygenase-1 (COX-1); 14910 nM 3-pentyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:19447036 PENTACON PENTACON Notes: Request ChEBI ID: 3-pentyl-2-(4-methyl sulfonylphenyl)-1,3-thiazinan-4-one AAP 2000001181 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 60.0 nM; Cyclooxygenase-2 (COX-2); CHEBI:118694 (celecoxib) 60 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:18226898 PENTACON Added by PENTACON AAP 2000001182 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 24300.0 nM; Cyclooxygenase-1 (COX-1); CHEBI:118694 (celecoxib) 24300 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:18226898 PENTACON Added by PENTACON AAP 2000001183 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 1-(4-methylsulfonylpheny)-3-(4-hydroxyphenyl) urea, Cox Inhibitor 4a; IC50: 170 nM; Cyclooxygenase-2 (COX-2); 170 nM 1-(4-methylsulfonylpheny)-3-(4-hydroxyphenyl) urea arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:18226898 PENTACON PENTACON Notes: Request ChEBI ID: 1-(4-methylsulfonylpheny)-3-(4-hydroxyphenyl) urea AAP 2000001184 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 1-(4-methylsulfonylpheny)-3-(4-hydroxyphenyl) urea, Cox Inhibitor 4a; IC50: 9200 nM; Cyclooxygenase-1 (COX-1); 9200 nM 1-(4-methylsulfonylpheny)-3-(4-hydroxyphenyl) urea arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:18226898 PENTACON PENTACON Notes: Request ChEBI ID: 1-(4-methylsulfonylpheny)-3-(4-hydroxyphenyl) urea AAP 2000001185 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 1-(4-methylsulfonylpheny)-3-(4-fluorophenyl) urea, Cox Inhibitor 4b; IC50: 130 nM; Cyclooxygenase-2 (COX-2); 130 nM 1-(4-methylsulfonylpheny)-3-(4-fluorophenyl) urea arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:18226898 PENTACON PENTACON Notes: Request ChEBI ID: 1-(4-methylsulfonylpheny)-3-(4-fluorophenyl) urea AAP 2000001186 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 1-(4-methylsulfonylpheny)-3-(4-fluorophenyl) urea, Cox Inhibitor 4b; IC50: 21800 nM; Cyclooxygenase-1 (COX-1); 21800 nM 1-(4-methylsulfonylpheny)-3-(4-fluorophenyl) urea arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:18226898 PENTACON PENTACON Notes: Request ChEBI ID: 1-(4-methylsulfonylpheny)-3-(4-fluorophenyl) urea AAP 2000001187 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 1-(4-methylsulfonylpheny)-3-(4-chlorophenyl) urea, Cox Inhibitor 4c; IC50: 270 nM; Cyclooxygenase-2 (COX-2); 270 nM 1-(4-methylsulfonylpheny)-3-(4-chlorophenyl) urea arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:18226898 PENTACON PENTACON Notes: Request ChEBI ID: 1-(4-methylsulfonylpheny)-3-(4-chlorophenyl) urea AAP 2000001188 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 1-(4-methylsulfonylpheny)-3-(4-chlorophenyl) urea, Cox Inhibitor 4c; IC50: 21500 nM; Cyclooxygenase-1 (COX-1); 21500 nM 1-(4-methylsulfonylpheny)-3-(4-chlorophenyl) urea arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:18226898 PENTACON PENTACON Notes: Request ChEBI ID: 1-(4-methylsulfonylpheny)-3-(4-chlorophenyl) urea AAP 2000001189 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 1-(4-methylsulfonylpheny)-3-(4-methylphenyl) urea, Cox Inhibitor 4d; IC50: 330 nM; Cyclooxygenase-2 (COX-2); 330 nM 1-(4-methylsulfonylpheny)-3-(4-methylphenyl) urea arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:18226898 PENTACON PENTACON Notes: Request ChEBI ID: 1-(4-methylsulfonylpheny)-3-(4-methylphenyl) urea AAP 2000001190 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 1-(4-methylsulfonylpheny)-3-(4-methylphenyl) urea, Cox Inhibitor 4d; IC50: 12500 nM; Cyclooxygenase-1 (COX-1); 12500 nM 1-(4-methylsulfonylpheny)-3-(4-methylphenyl) urea arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:18226898 PENTACON PENTACON Notes: Request ChEBI ID: 1-(4-methylsulfonylpheny)-3-(4-methylphenyl) urea AAP 2000001191 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 1-(4-methylsulfonylpheny)-3-(4-methoxyphenyl) urea, Cox Inhibitor 4e; IC50: 110 nM; Cyclooxygenase-2 (COX-2); 110 nM 1-(4-methylsulfonylpheny)-3-(4-methoxyphenyl) urea arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:18226898 PENTACON PENTACON Notes: Request ChEBI ID:1-(4-methylsulfonylpheny)-3-(4-methoxyphenyl) urea AAP 2000001192 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 1-(4-methylsulfonylpheny)-3-(4-methoxyphenyl) urea, Cox Inhibitor 4e; IC50: 22400 nM; Cyclooxygenase-1 (COX-1); 22400 nM 1-(4-methylsulfonylpheny)-3-(4-methoxyphenyl) urea arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:18226898 PENTACON PENTACON Notes: Request ChEBI ID: 1-(4-methylsulfonylpheny)-3-(4-methoxyphenyl) urea AAP 2000001193 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 60.0 nM; Cyclooxygenase-2 (COX-2); CHEBI:118694 (celecoxib) 60 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON Added by PENTACON AAP 2000001194 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 24300.0 nM; Cyclooxygenase-1 (COX-1); CHEBI:118694 (celecoxib) 24300 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON Added by PENTACON AAP 2000001195 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-(Methylsulfonyl)phenyl)-2,3-diphenylprop-2-en-1-one, Cox Inhibitor 3a; IC50: 110 nM; Cyclooxygenase-2 (COX-2); 110 nM (E)-1-(4-(Methylsulfonyl)phenyl)-2,3-diphenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-(Methylsulfonyl)phenyl)-2,3-diphenylprop-2-en-1-one AAP 2000001196 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-(Methylsulfonyl)phenyl)-2,3-diphenylprop-2-en-1-one, Cox Inhibitor 3a; IC50: 13270 nM; Cyclooxygenase-1 (COX-1); 13270 nM (E)-1-(4-(Methylsulfonyl)phenyl)-2,3-diphenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-(Methylsulfonyl)phenyl)-2,3-diphenylprop-2-en-1-one AAP 2000001197 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (Z)-1-(4-(Methylsulfonyl)phenyl)-2,3-diphenylprop-2-en-1-one, Cox Inhibitor 3b; IC50: 70 nM; Cyclooxygenase-2 (COX-2); 70 nM (Z)-1-(4-(Methylsulfonyl)phenyl)-2,3-diphenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (Z)-1-(4-(Methylsulfonyl)phenyl)-2,3-diphenylprop-2-en-1-one AAP 2000001198 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (Z)-1-(4-(Methylsulfonyl)phenyl)-2,3-diphenylprop-2-en-1-one, Cox Inhibitor 3b; IC50: 14270 nM; Cyclooxygenase-1 (COX-1); 14270 nM (Z)-1-(4-(Methylsulfonyl)phenyl)-2,3-diphenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (Z)-1-(4-(Methylsulfonyl)phenyl)-2,3-diphenylprop-2-en-1-one AAP 2000001199 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-3-(4-Fluorophenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one, Cox Inhibitor 4a; IC50: 190 nM; Cyclooxygenase-2 (COX-2); 190 nM (E)-3-(4-Fluorophenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (E)-3-(4-Fluorophenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one AAP 2000001200 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-3-(4-Fluorophenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one, Cox Inhibitor 4a; IC50: 12590 nM; Cyclooxygenase-1 (COX-1); 12590 nM (E)-3-(4-Fluorophenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (E)-3-(4-Fluorophenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one AAP 2000001201 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (Z)-3-(4-Fluorophenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one, Cox Inhibitor 4b; IC50: 160 nM; Cyclooxygenase-2 (COX-2); 160 nM (Z)-3-(4-Fluorophenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (Z)-3-(4-Fluorophenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one AAP 2000001202 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (Z)-3-(4-Fluorophenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one, Cox Inhibitor 4b; IC50: 30940 nM; Cyclooxygenase-1 (COX-1); 30940 nM (Z)-3-(4-Fluorophenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (Z)-3-(4-Fluorophenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one AAP 2000001203 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-p-tolylprop-2-en-1-one, Cox Inhibitor 5a; IC50: 280 nM; Cyclooxygenase-2 (COX-2); 280 nM (E)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-p-tolylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID:(E)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-p-tolylprop-2-en-1-one AAP 2000001204 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-p-tolylprop-2-en-1-one, Cox Inhibitor 5a; IC50: 10370 nM; Cyclooxygenase-1 (COX-1); 10370 nM (E)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-p-tolylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-p-tolylprop-2-en-1-one AAP 2000001205 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (Z)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-p-tolylprop-2-en-1-one, Cox Inhibitor 5b; IC50: 210 nM; Cyclooxygenase-2 (COX-2); 210 nM (Z)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-p-tolylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (Z)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-p-tolylprop-2-en-1-one AAP 2000001206 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (Z)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-p-tolylprop-2-en-1-one, Cox Inhibitor 5b; IC50: 12210 nM; Cyclooxygenase-1 (COX-1); 12210 nM (Z)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-p-tolylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (Z)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-p-tolylprop-2-en-1-one AAP 2000001207 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-3-(4-Methoxyphenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one, Cox Inhibitor 6a; IC50: 220 nM; Cyclooxygenase-2 (COX-2); 220 nM (E)-3-(4-Methoxyphenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (E)-3-(4-Methoxyphenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one AAP 2000001208 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-3-(4-Methoxyphenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one, Cox Inhibitor 6a; IC50: 10680 nM; Cyclooxygenase-1 (COX-1); 10680 nM (E)-3-(4-Methoxyphenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (E)-3-(4-Methoxyphenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one AAP 2000001209 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (Z)-3-(4-Methoxyphenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one, Cox Inhibitor 6b; IC50: 210 nM; Cyclooxygenase-2 (COX-2); 210 nM (Z)-3-(4-Methoxyphenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (Z)-3-(4-Methoxyphenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one AAP 2000001210 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (Z)-3-(4-Methoxyphenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one, Cox Inhibitor 6b; IC50: 18380 nM; Cyclooxygenase-1 (COX-1); 18380 nM (Z)-3-(4-Methoxyphenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (Z)-3-(4-Methoxyphenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one AAP 2000001211 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-3-(4-Hydroxyphenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one, Cox Inhibitor 7; IC50: 80 nM; Cyclooxygenase-2 (COX-2); 80 nM (E)-3-(4-Hydroxyphenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (E)-3-(4-Hydroxyphenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one AAP 2000001212 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-3-(4-Hydroxyphenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one, Cox Inhibitor 7; IC50: 14420 nM; Cyclooxygenase-1 (COX-1); 14420 nM (E)-3-(4-Hydroxyphenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (E)-3-(4-Hydroxyphenyl)-1-(4-(methylsulfonyl)phenyl)-2-phenylprop-2-en-1-one AAP 2000001213 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-(thiophen-2-yl)prop-2-en-1-one, Cox Inhibitor 8a; IC50: 130 nM; Cyclooxygenase-2 (COX-2); 130 nM (E)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-(thiophen-2-yl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-(thiophen-2-yl)prop-2-en-1-one AAP 2000001214 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-(thiophen-2-yl)prop-2-en-1-one, Cox Inhibitor 8a; IC50: 13120 nM; Cyclooxygenase-1 (COX-1); 13120 nM (E)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-(thiophen-2-yl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-(thiophen-2-yl)prop-2-en-1-one AAP 2000001215 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E & Z)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-(pyridin-4-yl)prop-2-en-1-one, Cox Inhibitor 9; IC50: 70 nM; Cyclooxygenase-2 (COX-2); 70 nM (E & Z)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-(pyridin-4-yl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (E & Z)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-(pyridin-4-yl)prop-2-en-1-one AAP 2000001216 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E & Z)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-(pyridin-4-yl)prop-2-en-1-one, Cox Inhibitor 9; IC50: 12370 nM; Cyclooxygenase-1 (COX-1); 12370 nM (E & Z)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-(pyridin-4-yl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:20691338 PENTACON PENTACON Notes: Request ChEBI ID: (E & Z)-1-(4-(Methylsulfonyl)phenyl)-2-phenyl-3-(pyridin-4-yl)prop-2-en-1-one AAP 2000001217 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 60.0 nM; Cyclooxygenase-2 (COX-2); CHEBI:118694 (celecoxib) 60 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17822894 PENTACON Added by PENTACON AAP 2000001218 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Celecoxib; IC50: 24300.0 nM; Cyclooxygenase-1 (COX-1); CHEBI:118694 (celecoxib) 24300 nM celecoxib CHEBI:118694 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17822894 PENTACON Added by PENTACON AAP 2000001219 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-hydroxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one, Cox Inhibitor 5a; IC50: 20 nM; Cyclooxygenase-2 (COX-2); 20 nM 3-(4-hydroxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17822894 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-hydroxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one AAP 2000001220 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-hydroxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one, Cox Inhibitor 5a; IC50: 96100 nM; Cyclooxygenase-1 (COX-1); 96100 nM 3-(4-hydroxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17822894 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-hydroxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one AAP 2000001221 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-fluorophenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one, Cox Inhibitor 5b; IC50: 120 nM; Cyclooxygenase-2 (COX-2); 120 nM 3-(4-fluorophenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17822894 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-fluorophenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one AAP 2000001222 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-fluorophenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one, Cox Inhibitor 5b; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); nM 3-(4-fluorophenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17822894 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-fluorophenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one AAP 2000001223 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-methylphenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one, Cox Inhibitor 5c; IC50: 150 nM; Cyclooxygenase-2 (COX-2); 150 nM 3-(4-methylphenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17822894 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-methylphenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one AAP 2000001224 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-methylphenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one, Cox Inhibitor 5c; IC50: 53900 nM; Cyclooxygenase-1 (COX-1); 53900 nM 3-(4-methylphenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17822894 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-methylphenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one AAP 2000001225 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-methoxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one, Cox Inhibitor 5d; IC50: 160 nM; Cyclooxygenase-2 (COX-2); 160 nM 3-(4-methoxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17822894 PENTACON PENTACON Notes: Request ChEBI ID:3-(4-methoxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one AAP 2000001226 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-methoxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one, Cox Inhibitor 5d; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); nM 3-(4-methoxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17822894 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-methoxyphenyl)-2-(4-methylsulfonylphenyl)-1,3-thiazolidine-4-one AAP 2000001227 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Rofecoxib; IC50: 430 nM; Cyclooxygenase-2 (COX-2); CHEBI:8887 (rofecoxib) 430 nM rofecoxib CHEBI:8887 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17706175 PENTACON Added by PENTACON AAP 2000001228 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Rofecoxib; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); CHEBI:8887 (rofecoxib) nM rofecoxib CHEBI:8887 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17706175 PENTACON Added by PENTACON AAP 2000001229 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 acetylsalicylic acid; IC50: 2400 nM; Cyclooxygenase-2 (COX-2); CHEBI:15365 (acetylsalicylic acid) 2400 nM acetylsalicylic acid CHEBI:15365 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17706175 PENTACON Added by PENTACON AAP 2000001230 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 acetylsalicylic acid; IC50: 350 nM; Cyclooxygenase-1 (COX-1); CHEBI:15365 (acetylsalicylic acid) 350 nM acetylsalicylic acid CHEBI:15365 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17706175 PENTACON Added by PENTACON AAP 2000001231 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-Acetylsulfonamido)phenyl]-3-phenyl-2(5H)furanone, Cox Inhibitor 8a; IC50: 320 nM; Cyclooxygenase-2 (COX-2); 320 nM 4-[4-(N-Acetylsulfonamido)phenyl]-3-phenyl-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17706175 PENTACON PENTACON Notes: Request ChEBI ID: 4-[4-(N-Acetylsulfonamido)phenyl]-3-phenyl-2(5H)furanone AAP 2000001232 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-Acetylsulfonamido)phenyl]-3-phenyl-2(5H)furanone, Cox Inhibitor 8a; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); nM 4-[4-(N-Acetylsulfonamido)phenyl]-3-phenyl-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17706175 PENTACON PENTACON Notes: Request ChEBI ID: 4-[4-(N-Acetylsulfonamido)phenyl]-3-phenyl-2(5H)furanone AAP 2000001233 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-flourophenyl)-2(5H)furanone, Cox Inhibitor 8b; IC50: 1030 nM; Cyclooxygenase-2 (COX-2); 1030 nM 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-flourophenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17706175 PENTACON PENTACON Notes: Request ChEBI ID: 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-flourophenyl)-2(5H)furanone AAP 2000001234 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-flourophenyl)-2(5H)furanone, Cox Inhibitor 8b; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); nM 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-flourophenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17706175 PENTACON PENTACON Notes: Request ChEBI ID: 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-flourophenyl)-2(5H)furanone AAP 2000001235 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-chlorophenyl)-2(5H)furanone, Cox Inhibitor 8c; IC50: 4480 nM; Cyclooxygenase-2 (COX-2); 4480 nM 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-chlorophenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17706175 PENTACON PENTACON Notes: Request ChEBI ID: 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-chlorophenyl)-2(5H)furanone AAP 2000001236 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-chlorophenyl)-2(5H)furanone, Cox Inhibitor 8c; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); nM 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-chlorophenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17706175 PENTACON PENTACON Notes: Request ChEBI ID: 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-chlorophenyl)-2(5H)furanone AAP 2000001237 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-methylphenyl)-2(5H)furanone, Cox Inhibitor 8d; IC50: 4850 nM; Cyclooxygenase-2 (COX-2); 4850 nM 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-methylphenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17706175 PENTACON PENTACON Notes: Request ChEBI ID: 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-methylphenyl)-2(5H)furanone AAP 2000001238 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-methylphenyl)-2(5H)furanone, Cox Inhibitor 8d; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); nM 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-methylphenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17706175 PENTACON PENTACON Notes: Request ChEBI ID: 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-methylphenyl)-2(5H)furanone AAP 2000001239 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-methoxylphenyl)-2(5H)furanone, Cox Inhibitor 8e; IC50: 9970 nM; Cyclooxygenase-2 (COX-2); 9970 nM 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-methoxylphenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17706175 PENTACON PENTACON Notes: Request ChEBI ID: 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-methoxylphenyl)-2(5H)furanone AAP 2000001240 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-methoxylphenyl)-2(5H)furanone, Cox Inhibitor 8e; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); nM 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-methoxylphenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed:17706175 PENTACON PENTACON Notes: Request ChEBI ID: 4-[4-(N-Acetylsulfonamido)phenyl]-3-(4-methoxylphenyl)-2(5H)furanone AAP 2000001241 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Rofecoxib; IC50: 500 nM; Cyclooxygenase-2 (COX-2); CHEBI:8887 (rofecoxib) 500 nM rofecoxib CHEBI:8887 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 17067801 PENTACON Added by PENTACON AAP 2000001242 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Rofecoxib; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); CHEBI:8887 (rofecoxib) nM rofecoxib CHEBI:8887 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 17067801 PENTACON Added by PENTACON AAP 2000001243 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-(4-Methylsulfonamidophenyl)-3-phenyl-2(5H)furanone, Cox Inhibitor 11a; IC50: 1700 nM; Cyclooxygenase-2 (COX-2); 1700 nM 4-(4-Methylsulfonamidophenyl)-3-phenyl-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 17067801 PENTACON PENTACON Notes: Request ChEBI ID: 4-(4-Methylsulfonamidophenyl)-3-phenyl-2(5H)furanone AAP 2000001244 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-(4-Methylsulfonamidophenyl)-3-phenyl-2(5H)furanone, Cox Inhibitor 11a; IC50: 31600 nM; Cyclooxygenase-1 (COX-1); 31600 nM 4-(4-Methylsulfonamidophenyl)-3-phenyl-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 17067801 PENTACON PENTACON Notes: Request ChEBI ID: 4-(4-Methylsulfonamidophenyl)-3-phenyl-2(5H)furanone AAP 2000001245 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-Fluorophenyl)-4-(4-methylsulfonamidophenyl)- 2(5H)furanone, Cox Inhibitor 11b; IC50: 3200 nM; Cyclooxygenase-2 (COX-2); 3200 nM 3-(4-Fluorophenyl)-4-(4-methylsulfonamidophenyl)- 2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 17067801 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Fluorophenyl)-4-(4-methylsulfonamidophenyl)- 2(5H)furanone AAP 2000001246 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-Fluorophenyl)-4-(4-methylsulfonamidophenyl)- 2(5H)furanone, Cox Inhibitor 11b; IC50: 10000 nM; Cyclooxygenase-1 (COX-1); 10000 nM 3-(4-Fluorophenyl)-4-(4-methylsulfonamidophenyl)- 2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 17067801 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Fluorophenyl)-4-(4-methylsulfonamidophenyl)- 2(5H)furanone AAP 2000001247 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-Chlorophenyl)-4-(4-methylsulfonamidophenyl)-2(5H)furanone, Cox Inhibitor 11c; IC50: 800 nM; Cyclooxygenase-2 (COX-2); 800 nM 3-(4-Chlorophenyl)-4-(4-methylsulfonamidophenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 17067801 PENTACON PENTACON Notes: Request ChEBI ID:3-(4-Chlorophenyl)-4-(4-methylsulfonamidophenyl)-2(5H)furanone AAP 2000001248 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-Chlorophenyl)-4-(4-methylsulfonamidophenyl)-2(5H)furanone, Cox Inhibitor 11c; IC50: 31500 nM; Cyclooxygenase-1 (COX-1); 31500 nM 3-(4-Chlorophenyl)-4-(4-methylsulfonamidophenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 17067801 PENTACON PENTACON Notes: Request ChEBI ID:3-(4-Chlorophenyl)-4-(4-methylsulfonamidophenyl)-2(5H)furanone AAP 2000001249 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-Bromophenyl)-4-(4-methylsulfonamidophenyl)- 2(5H)furanone, Cox Inhibitor 11d; IC50: 3200 nM; Cyclooxygenase-2 (COX-2); 3200 nM 3-(4-Bromophenyl)-4-(4-methylsulfonamidophenyl)- 2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 17067801 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Bromophenyl)-4-(4-methylsulfonamidophenyl)- 2(5H)furanone AAP 2000001250 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-Bromophenyl)-4-(4-methylsulfonamidophenyl)- 2(5H)furanone, Cox Inhibitor 11d; IC50: 35500 nM; Cyclooxygenase-1 (COX-1); 35500 nM 3-(4-Bromophenyl)-4-(4-methylsulfonamidophenyl)- 2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 17067801 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Bromophenyl)-4-(4-methylsulfonamidophenyl)- 2(5H)furanone AAP 2000001251 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-Methylphenyl)-4-(4-methylsulfonamidophenyl)-2(5H)furanone, Cox Inhibitor 11e; IC50: 900 nM; Cyclooxygenase-2 (COX-2); 900 nM 3-(4-Methylphenyl)-4-(4-methylsulfonamidophenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 17067801 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Methylphenyl)-4-(4-methylsulfonamidophenyl)-2(5H)furanone AAP 2000001252 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Request ChEBI ID: 3-(4-Methylphenyl)-4-(4-methylsulfonamidophenyl)-2(5H)furanone, Cox Inhibitor 11e; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); nM 3-(4-Methylphenyl)-4-(4-methylsulfonamidophenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 17067801 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Methylphenyl)-4-(4-methylsulfonamidophenyl)-2(5H)furanone AAP 2000001253 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-Methoxyphenyl)-4-(4-methylsulfonamidophenyl)-2(5H)furanone, Cox Inhibitor 11f; IC50: 31500 nM; Cyclooxygenase-2 (COX-2); 31500 nM 3-(4-Methoxyphenyl)-4-(4-methylsulfonamidophenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 17067801 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Methoxyphenyl)-4-(4-methylsulfonamidophenyl)-2(5H)furanone AAP 2000001254 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 3-(4-Methoxyphenyl)-4-(4-methylsulfonamidophenyl)-2(5H)furanone, Cox Inhibitor 11f; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); nM 3-(4-Methoxyphenyl)-4-(4-methylsulfonamidophenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 17067801 PENTACON PENTACON Notes: Request ChEBI ID: 3-(4-Methoxyphenyl)-4-(4-methylsulfonamidophenyl)-2(5H)furanone AAP 2000001255 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Rofecoxib; IC50: 500 nM; Cyclooxygenase-2 (COX-2); CHEBI:8887 (rofecoxib) 500 nM rofecoxib CHEBI:8887 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16798002 PENTACON Added by PENTACON AAP 2000001256 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Rofecoxib; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); CHEBI:8887 (rofecoxib) nM rofecoxib CHEBI:8887 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16798002 PENTACON Added by PENTACON AAP 2000001257 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Methanesulfonamidophenyl)-3-phenylprop-2-en-1-one, Cox Inhibitor 7a; IC50: 3200 nM; Cyclooxygenase-2 (COX-2); 3200 nM (E)-1-(4-Methanesulfonamidophenyl)-3-phenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16798002 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Methanesulfonamidophenyl)-3-phenylprop-2-en-1-one AAP 2000001258 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Methanesulfonamidophenyl)-3-phenylprop-2-en-1-one, Cox Inhibitor 7a; IC50: 3000 nM; Cyclooxygenase-1 (COX-1); 3000 nM (E)-1-(4-Methanesulfonamidophenyl)-3-phenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16798002 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Methanesulfonamidophenyl)-3-phenylprop-2-en-1-one AAP 2000001259 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Methanesulfonamidophenyl)-3-(4-methylphenyl)prop-2-en-1-one, Cox Inhibitor 7b; IC50: 1000 nM; Cyclooxygenase-2 (COX-2); 1000 nM (E)-1-(4-Methanesulfonamidophenyl)-3-(4-methylphenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16798002 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Methanesulfonamidophenyl)-3-(4-methylphenyl)prop-2-en-1-one AAP 2000001260 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Methanesulfonamidophenyl)-3-(4-methylphenyl)prop-2-en-1-one, Cox Inhibitor 7b; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); nM (E)-1-(4-Methanesulfonamidophenyl)-3-(4-methylphenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16798002 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Methanesulfonamidophenyl)-3-(4-methylphenyl)prop-2-en-1-one AAP 2000001261 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-3-(4-Fluorophenyl)-1-(4-methanesulfonamidophenyl)prop-2-en-1-one, Cox Inhibitor 7c; IC50: >100000 nM; Cyclooxygenase-2 (COX-2); nM (E)-3-(4-Fluorophenyl)-1-(4-methanesulfonamidophenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16798002 PENTACON PENTACON Notes: Request ChEBI ID: (E)-3-(4-Fluorophenyl)-1-(4-methanesulfonamidophenyl)prop-2-en-1-one AAP 2000001262 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-3-(4-Fluorophenyl)-1-(4-methanesulfonamidophenyl)prop-2-en-1-one, Cox Inhibitor 7c; IC50: 3300 nM; Cyclooxygenase-1 (COX-1); 3300 nM (E)-3-(4-Fluorophenyl)-1-(4-methanesulfonamidophenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16798002 PENTACON PENTACON Notes: Request ChEBI ID: (E)-3-(4-Fluorophenyl)-1-(4-methanesulfonamidophenyl)prop-2-en-1-one AAP 2000001263 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Methanesulfonamidophenyl)-3-(4-methoxyphenyl)prop-2-en-1-one, Cox Inhibitor 7d; IC50: 10000 nM; Cyclooxygenase-2 (COX-2); 10000 nM (E)-1-(4-Methanesulfonamidophenyl)-3-(4-methoxyphenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16798002 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Methanesulfonamidophenyl)-3-(4-methoxyphenyl)prop-2-en-1-one AAP 2000001264 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Methanesulfonamidophenyl)-3-(4-methoxyphenyl)prop-2-en-1-one, Cox Inhibitor 7d; IC50: 1000 nM; Cyclooxygenase-1 (COX-1); 1000 nM (E)-1-(4-Methanesulfonamidophenyl)-3-(4-methoxyphenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16798002 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Methanesulfonamidophenyl)-3-(4-methoxyphenyl)prop-2-en-1-one AAP 2000001265 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Azidophenyl)-3-phenylprop-2-en-1-one, Cox Inhibitor 7e; IC50: 3400 nM; Cyclooxygenase-2 (COX-2); 3400 nM (E)-1-(4-Azidophenyl)-3-phenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16798002 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Azidophenyl)-3-phenylprop-2-en-1-one AAP 2000001266 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Azidophenyl)-3-phenylprop-2-en-1-one, Cox Inhibitor 7e; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); nM (E)-1-(4-Azidophenyl)-3-phenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16798002 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Azidophenyl)-3-phenylprop-2-en-1-one AAP 2000001267 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Azidophenyl)-3-(4-methylphenyl)prop-2-en-1-one, Cox Inhibitor 7f; IC50: 300 nM; Cyclooxygenase-2 (COX-2); 300 nM (E)-1-(4-Azidophenyl)-3-(4-methylphenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16798002 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Azidophenyl)-3-(4-methylphenyl)prop-2-en-1-one AAP 2000001268 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Azidophenyl)-3-(4-methylphenyl)prop-2-en-1-one, Cox Inhibitor 7f; IC50: 22200 nM; Cyclooxygenase-1 (COX-1); 22200 nM (E)-1-(4-Azidophenyl)-3-(4-methylphenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16798002 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Azidophenyl)-3-(4-methylphenyl)prop-2-en-1-one AAP 2000001269 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Azidophenyl)-3-(4-fluorophenyl)prop-2-en-1-one, Cox Inhibitor 7g; IC50: 10000 nM; Cyclooxygenase-2 (COX-2); 10000 nM (E)-1-(4-Azidophenyl)-3-(4-fluorophenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16798002 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Azidophenyl)-3-(4-fluorophenyl)prop-2-en-1-one AAP 2000001270 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Azidophenyl)-3-(4-fluorophenyl)prop-2-en-1-one, Cox Inhibitor 7g; IC50: 4200 nM; Cyclooxygenase-1 (COX-1); 4200 nM (E)-1-(4-Azidophenyl)-3-(4-fluorophenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16798002 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Azidophenyl)-3-(4-fluorophenyl)prop-2-en-1-one AAP 2000001271 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Azidophenyl)-3-(4-methoxyphenyl)prop-2-ene-1-one, Cox Inhibitor 7h; IC50: 3600 nM; Cyclooxygenase-2 (COX-2); 3600 nM (E)-1-(4-Azidophenyl)-3-(4-methoxyphenyl)prop-2-ene-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16798002 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Azidophenyl)-3-(4-methoxyphenyl)prop-2-ene-1-one AAP 2000001272 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Azidophenyl)-3-(4-methoxyphenyl)prop-2-ene-1-one, Cox Inhibitor 7h; IC50: 400 nM; Cyclooxygenase-1 (COX-1); 400 nM (E)-1-(4-Azidophenyl)-3-(4-methoxyphenyl)prop-2-ene-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16798002 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Azidophenyl)-3-(4-methoxyphenyl)prop-2-ene-1-one AAP 2000001273 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Rofecoxib; IC50: 500 nM; Cyclooxygenase-2 (COX-2); CHEBI:8887 (rofecoxib) 500 nM rofecoxib CHEBI:8887 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16356730 PENTACON Added by PENTACON AAP 2000001274 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Rofecoxib; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); CHEBI:8887 (rofecoxib) nM rofecoxib CHEBI:8887 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16356730 PENTACON Added by PENTACON AAP 2000001275 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-3-(4-Methanesulfonylphenyl)-1-phenylprop-2-en-1-one, Cox Inhibitor 9a; IC50: 800 nM; Cyclooxygenase-2 (COX-2); 800 nM (E)-3-(4-Methanesulfonylphenyl)-1-phenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16356730 PENTACON PENTACON Notes: Request ChEBI ID: (E)-3-(4-Methanesulfonylphenyl)-1-phenylprop-2-en-1-one AAP 2000001276 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-3-(4-Methanesulfonylphenyl)-1-phenylprop-2-en-1-one, Cox Inhibitor 9a; IC50:1100 nM; Cyclooxygenase-1 (COX-1); 1100 nM (E)-3-(4-Methanesulfonylphenyl)-1-phenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16356730 PENTACON PENTACON Notes: Request ChEBI ID: (E)-3-(4-Methanesulfonylphenyl)-1-phenylprop-2-en-1-one AAP 2000001277 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-3-(4-Methanesulfonylphenyl)-1-(4-methylphenyl)prop-2-en-1-one, Cox Inhibitor 9b; IC50: 300 nM; Cyclooxygenase-2 (COX-2); 300 nM (E)-3-(4-Methanesulfonylphenyl)-1-(4-methylphenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16356730 PENTACON PENTACON Notes: Request ChEBI ID: (E)-3-(4-Methanesulfonylphenyl)-1-(4-methylphenyl)prop-2-en-1-one AAP 2000001278 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-3-(4-Methanesulfonylphenyl)-1-(4-methylphenyl)prop-2-en-1-one, Cox Inhibitor 9b; IC50: 1000 nM; Cyclooxygenase-1 (COX-1); 1000 nM (E)-3-(4-Methanesulfonylphenyl)-1-(4-methylphenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16356730 PENTACON PENTACON Notes: Request ChEBI ID: (E)-3-(4-Methanesulfonylphenyl)-1-(4-methylphenyl)prop-2-en-1-one AAP 2000001279 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Fluorophenyl)-3-(4-methanesulfonylphenyl)prop-2-en-1-one, Cox Inhibitor 9c; IC50: 10000 nM; Cyclooxygenase-2 (COX-2); 10000 nM (E)-1-(4-Fluorophenyl)-3-(4-methanesulfonylphenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16356730 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Fluorophenyl)-3-(4-methanesulfonylphenyl)prop-2-en-1-one AAP 2000001280 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Fluorophenyl)-3-(4-methanesulfonylphenyl)prop-2-en-1-one, Cox Inhibitor 9c; IC50: 4200 nM; Cyclooxygenase-1 (COX-1); 4200 nM (E)-1-(4-Fluorophenyl)-3-(4-methanesulfonylphenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16356730 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Fluorophenyl)-3-(4-methanesulfonylphenyl)prop-2-en-1-one AAP 2000001281 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-3-(4-Methanesulfonylphenyl)-1-(4-methoxyphenyl)prop-2-en-1-one, Cox Inhibitor 9d; IC50: 4900 nM; Cyclooxygenase-2 (COX-2); 4900 nM (E)-3-(4-Methanesulfonylphenyl)-1-(4-methoxyphenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16356730 PENTACON PENTACON Notes: Request ChEBI ID: (E)-3-(4-Methanesulfonylphenyl)-1-(4-methoxyphenyl)prop-2-en-1-one AAP 2000001282 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-3-(4-Methanesulfonylphenyl)-1-(4-methoxyphenyl)prop-2-en-1-one, Cox Inhibitor 9d; IC50: 3200 nM; Cyclooxygenase-1 (COX-1); 3200 nM (E)-3-(4-Methanesulfonylphenyl)-1-(4-methoxyphenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16356730 PENTACON PENTACON Notes: Request ChEBI ID: (E)-3-(4-Methanesulfonylphenyl)-1-(4-methoxyphenyl)prop-2-en-1-one AAP 2000001283 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Methanesulfonylphenyl)-3-phenylprop-2-en-1-one, Cox Inhibitor 9e; IC50: 1000 nM; Cyclooxygenase-2 (COX-2); 1000 nM (E)-1-(4-Methanesulfonylphenyl)-3-phenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16356730 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Methanesulfonylphenyl)-3-phenylprop-2-en-1-one AAP 2000001284 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Methanesulfonylphenyl)-3-phenylprop-2-en-1-one, Cox Inhibitor 9e; IC50: 21500 nM; Cyclooxygenase-1 (COX-1); 21500 nM (E)-1-(4-Methanesulfonylphenyl)-3-phenylprop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16356730 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Methanesulfonylphenyl)-3-phenylprop-2-en-1-one AAP 2000001285 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Methanesulfonylphenyl)-3-(4-methylphenyl)prop-2-en-1-one, Cox Inhibitor 9f; IC50: 300 nM; Cyclooxygenase-2 (COX-2); 300 nM (E)-1-(4-Methanesulfonylphenyl)-3-(4-methylphenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16356730 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Methanesulfonylphenyl)-3-(4-methylphenyl)prop-2-en-1-one AAP 2000001286 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Methanesulfonylphenyl)-3-(4-methylphenyl)prop-2-en-1-one, Cox Inhibitor 9f; IC50: 32000 nM; Cyclooxygenase-1 (COX-1); 32000 nM (E)-1-(4-Methanesulfonylphenyl)-3-(4-methylphenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16356730 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Methanesulfonylphenyl)-3-(4-methylphenyl)prop-2-en-1-one AAP 2000001287 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-3-(4-Fluorophenyl)-1-(4-methanesulfonylphenyl)prop-2-en-1-one, Cox Inhibitor 9g; IC50: 600 nM; Cyclooxygenase-2 (COX-2); 600 nM (E)-3-(4-Fluorophenyl)-1-(4-methanesulfonylphenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16356730 PENTACON PENTACON Notes: Request ChEBI ID: (E)-3-(4-Fluorophenyl)-1-(4-methanesulfonylphenyl)prop-2-en-1-one AAP 2000001288 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-3-(4-Fluorophenyl)-1-(4-methanesulfonylphenyl)prop-2-en-1-one, Cox Inhibitor 9g; IC50: 31600 nM; Cyclooxygenase-1 (COX-1); 31600 nM (E)-3-(4-Fluorophenyl)-1-(4-methanesulfonylphenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16356730 PENTACON PENTACON Notes: Request ChEBI ID: (E)-3-(4-Fluorophenyl)-1-(4-methanesulfonylphenyl)prop-2-en-1-one AAP 2000001289 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Methanesulfonylphenyl)-3-(4-methoxyphenyl)prop-2-en-1-one, Cox Inhibitor 9h; IC50: 3200 nM; Cyclooxygenase-2 (COX-2); 3200 nM (E)-1-(4-Methanesulfonylphenyl)-3-(4-methoxyphenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16356730 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Methanesulfonylphenyl)-3-(4-methoxyphenyl)prop-2-en-1-one AAP 2000001290 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 (E)-1-(4-Methanesulfonylphenyl)-3-(4-methoxyphenyl)prop-2-en-1-one, Cox Inhibitor 9h; IC50: 3300 nM; Cyclooxygenase-1 (COX-1); 3300 nM (E)-1-(4-Methanesulfonylphenyl)-3-(4-methoxyphenyl)prop-2-en-1-one arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 16356730 PENTACON PENTACON Notes: Request ChEBI ID: (E)-1-(4-Methanesulfonylphenyl)-3-(4-methoxyphenyl)prop-2-en-1-one AAP 2000001291 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Rofecoxib; IC50: 430 nM; Cyclooxygenase-2 (COX-2); CHEBI:8887 (rofecoxib) 430 nM rofecoxib CHEBI:8887 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 15050636 PENTACON Added by PENTACON AAP 2000001292 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 Rofecoxib; IC50: >500000 nM; Cyclooxygenase-1 (COX-1); CHEBI:8887 (rofecoxib) nM rofecoxib CHEBI:8887 arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 15050636 PENTACON Added by PENTACON AAP 2000001293 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-sulfonylmethylphenyl]-3-(4-(N-sulfonamido)phenyl)-2(5H)furanone, Cox Inhibitor 8a; IC50: >100000 nM; Cyclooxygenase-2 (COX-2); nM 4-[4-(N-sulfonylmethylphenyl\]-3-(4-(N-sulfonamido)phenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 15050636 PENTACON PENTACON Notes: Request Chebi ID: 4-[4-(N-sulfonylmethylphenyl\]-3-(4-(N-sulfonamido)phenyl)-2(5H)furanone AAP 2000001294 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-sulfonylmethylphenyl]-3-(4-(N-sulfonamido)phenyl)-2(5H)furanoneCox Inhibitor 8a; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); nM 4-[4-(N-sulfonylmethylphenyl\]-3-(4-(N-sulfonamido)phenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 15050636 PENTACON PENTACON Notes: Request Chebi ID: 4-[4-(N-sulfonylmethylphenyl\]-3-(4-(N-sulfonamido)phenyl)-2(5H)furanone AAP 2000001295 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-sulfonamido)phenyl]-3-(4-(N-sulfonylmethylphenyl)-2(5H)furanone, Cox Inhibitor 8b; IC50: >100000 nM; Cyclooxygenase-2 (COX-2); nM 4-[4-(N-sulfonamido)phenyl]-3-(4-(N-sulfonylmethylphenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 15050636 PENTACON PENTACON Notes: Request Chebi ID: 4-[4-(N-sulfonamido)phenyl]-3-(4-(N-sulfonylmethylphenyl)-2(5H)furanone AAP 2000001296 Jenn P23219 5742 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-sulfonamido)phenyl]-3-(4-(N-sulfonylmethylphenyl)-2(5H)furanone, Cox Inhibitor 8b; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); nM 4-[4-(N-sulfonamido)phenyl]-3-(4-(N-sulfonylmethylphenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 15050636 PENTACON PENTACON Notes: Request Chebi ID: 4-[4-(N-sulfonamido)phenyl]-3-(4-(N-sulfonylmethylphenyl)-2(5H)furanone AAP 2000001297 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-methanesulfonylphenyl]-3-(4-(N-acetylsulfonamido)phenyl)-2(5H)furanone, Cox Inhibitor 9a; IC50: 4600 nM; Cyclooxygenase-2 (COX-2); 4600 nM 4-[4-(N-methanesulfonylphenyl]-3-(4-(N-acetylsulfonamido)phenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 15050636 PENTACON PENTACON Notes: Request Chebi ID: 4-[4-(N-methanesulfonylphenyl]-3-(4-(N-acetylsulfonamido)phenyl)-2(5H)furanone AAP 2000001298 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-methanesulfonylphenyl]-3-(4-(N-acetylsulfonamido)phenyl)-2(5H)furanone, Cox Inhibitor 9a; IC50: 3200 nM; Cyclooxygenase-1 (COX-1); 3200 nM 4-[4-(N-methanesulfonylphenyl]-3-(4-(N-acetylsulfonamido)phenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 15050636 PENTACON PENTACON Notes: Request Chebi ID: 4-[4-(N-methanesulfonylphenyl]-3-(4-(N-acetylsulfonamido)phenyl)-2(5H)furanone AAP 2000001299 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-acetylsulfonamido)phenyl]-3-(4-methanesulfonylphenyl)-2(5H)furanone, Cox Inhibitor 9b; IC50: 50 nM; Cyclooxygenase-2 (COX-2); 50 nM 4-[4-(N-acetylsulfonamido)phenyl]-3-(4-methanesulfonylphenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 15050636 PENTACON PENTACON Notes: Request ChEBI ID: 4-[4-(N-acetylsulfonamido)phenyl]-3-(4-methanesulfonylphenyl)-2(5H)furanone AAP 2000001300 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4[4-(N-acetylsulfonamido)phenyl]-3-(4-methanesulfonylphenyl)-2(5H)furanone, Cox Inhibitor 9b; IC50: >100000 nM; Cyclooxygenase-1 (COX-1); nM 4-[4-(N-acetylsulfonamido)phenyl]-3-(4-methanesulfonylphenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 15050636 PENTACON PENTACON Notes: Request ChEBI ID: 4-[4-(N-acetylsulfonamido)phenyl]-3-(4-methanesulfonylphenyl)-2(5H)furanone AAP 2000001301 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-sulfonylmethyl)phenyl]-3-(4-sulfonylazidophenyl)-2(5H)furanone, Cox Inhibitor 10a; IC50: 11000 nM; Cyclooxygenase-2 (COX-2); 11000 nM 4-[4-(N-sulfonylmethyl)phenyl]-3-(4-sulfonylazidophenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 15050636 PENTACON PENTACON Notes: Request Chebi ID: 4-[4-(N-sulfonylmethyl)phenyl]-3-(4-sulfonylazidophenyl)-2(5H)furanone AAP 2000001302 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-sulfonylmethyl)phenyl]-3-(4-sulfonylazidophenyl)-2(5H)furanone, Cox Inhibitor 10a; IC50: 31500 nM; Cyclooxygenase-1 (COX-1); 31500 nM 4-[4-(N-sulfonylmethyl)phenyl]-3-(4-sulfonylazidophenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 15050636 PENTACON PENTACON Notes: Request Chebi ID: 4-[4-(N-sulfonylmethyl)phenyl]-3-(4-sulfonylazidophenyl)-2(5H)furanone AAP 2000001303 Jenn P35354 5743 PTGS2 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 4-[4-(N-sulfonylazido)phenyl]-3-(4-sulfonylmethylphenyl)-2(5H)furanone, Cox Inhibitor 10b; IC50: 3100 nM; Cyclooxygenase-2 (COX-2); 3100 nM 4-[4-(N-sulfonylazido)phenyl]-3-(4-sulfonylmethylphenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 15050636 PENTACON PENTACON Notes: Request Chebi ID: 4-[4-(N-sulfonylazido)phenyl]-3-(4-sulfonylmethylphenyl)-2(5H)furanone AAP 2000001304 Jenn P23219 5742 PTGS1 Homo sapiens 9606 Comment/biophysicochemical properties/IC50 41[4-(N-sulfonylazido)phenyl]-3-(4-sulfonylmethylphenyl)-2(5H)furanone, Cox Inhibitor 10b; IC50: >500000 nM; Cyclooxygenase-1 (COX-1); nM 4-[4-(N-sulfonylazido)phenyl]-3-(4-sulfonylmethylphenyl)-2(5H)furanone arachidonic acid CHEBI:15843 Y Y ECO:0000006 PubMed: 15050636 PENTACON PENTACON Notes: Request Chebi ID: 4-[4-(N-sulfonylazido)phenyl]-3-(4-sulfonylmethylphenyl)-2(5H)furanone AAP 2000001305