EC |
1.1.1.188 |
Accepted name: |
prostaglandin-F synthase |
Reaction: |
(5Z,13E)-(15S)-9α,11α,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-9α,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH + H+ |
Other name(s): |
prostaglandin-D2 11-reductase; reductase, 15-hydroxy-11-oxoprostaglandin; PGD2 11-ketoreductase; PGF2α synthetase; prostaglandin 11-ketoreductase; prostaglandin D2-ketoreductase; prostaglandin F synthase; prostaglandin F synthetase; synthetase, prostaglandin F2α; PGF synthetase; NADPH-dependent prostaglandin D2 11-keto reductase; prostaglandin 11-keto reductase |
Systematic name: |
(5Z,13E)-(15S)-9α,11α,15-trihydroxyprosta-5,13-dienoate:NADP+ 11-oxidoreductase |
Comments: |
Reduces prostaglandin D2 and prostaglandin H2 to prostaglandin F2; prostaglandin D2 is not an intermediate in the reduction of prostaglandin H2. Also catalyses the reduction of a number of carbonyl compounds, such as 9,10-phenanthroquinone and 4-nitroacetophenone. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 55976-95-9 |
References: |
1. |
Reingold, D.F., Kawasaki, A. and Needleman, P. A novel prostaglandin 11-keto reductase found in rabbit liver. Biochim. Biophys. Acta 659 (1981) 179–188. [DOI] [PMID: 7248318] |
2. |
Watanabe, K., Shimizu, T. and Hayaishi, O. Enzymatic conversion of prostaglandin-D2 to prostaglandin-F2α in the rat lung. Biochem. Int. 2 (1981) 603–610. |
3. |
Watanabe, K., Yoshida, R., Shimizu, T. and Hayaishi, O. Enzymatic formation of prostaglandin F2α from prostaglandin H2 and D2. Purification and properties of prostaglandin F synthetase from bovine lung. J. Biol. Chem. 260 (1985) 7035–7041. [PMID: 3858278] |
4. |
Wong, P.Y.-K. Purification and partial characterization of prostaglandin D2 11-keto reductase in rabbit liver. Biochim. Biophys. Acta 659 (1981) 169–178. [DOI] [PMID: 7248317] |
5. |
Wong, P.Y.-K. Purification of PGD2 11-ketoreductase from rabbit liver. Methods Enzymol. 86 (1982) 117–125. [PMID: 7132748] |
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[EC 1.1.1.188 created 1984, modified 1989, modified 1990] |
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EC |
1.11.1.20 |
Accepted name: |
prostamide/prostaglandin F2α synthase |
Reaction: |
thioredoxin + (5Z,9α,11α,13E,15S)-9,11-epidioxy-15-hydroxy-prosta-5,13-dienoate = thioredoxin disulfide + (5Z,9α,11α,13E,15S)-9,11,15-trihydroxyprosta-5,13-dienoate |
Glossary: |
prostamide H2 = (5Z)-N-(2-hydroxyethyl)-7-{(1R,4S,5R,6R)-6-[(1E,3S)-3-hydroxyoct-1-en-1-yl]-2,3-dioxabicyclo[2.2.1]hept-5-yl}hept-5-enamide
prostamide F2α = (5Z,9α,11α,13E,15S)-9,11,15-trihydroxy-N-(2-hydroxyethyl)prosta-5,13-dien-1-amide
prostaglandin H2 = (5Z,9α,11α,13E,15S)-9,11-epidioxy-15-hydroxy-prosta-5,13-dienoate
prostaglandin F2α = (5Z,9α,11α,13E,15S)-9,11,15-trihydroxyprosta-5,13-dienoate |
Other name(s): |
prostamide/PGF synthase; prostamide F synthase; prostamide/prostaglandin F synthase; tPGF synthase |
Systematic name: |
thioredoxin:(5Z,9α,11α,13E,15S)-9,11-epidioxy-15-hydroxy-prosta-5,13-dienoate oxidoreductase |
Comments: |
The enzyme contains a thioredoxin-type disulfide as a catalytic group. Prostamide H2 and prostaglandin H2 are the best substrates; the latter is converted to prostaglandin F2α. The enzyme also reduces tert-butyl hydroperoxide, cumene hydroperoxide and H2O2, but not prostaglandin D2 or prostaglandin E2. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Moriuchi, H., Koda, N., Okuda-Ashitaka, E., Daiyasu, H., Ogasawara, K., Toh, H., Ito, S., Woodward, D.F. and Watanabe, K. Molecular characterization of a novel type of prostamide/prostaglandin F synthase, belonging to the thioredoxin-like superfamily. J. Biol. Chem. 283 (2008) 792–801. [DOI] [PMID: 18006499] |
2. |
Yoshikawa, K., Takei, S., Hasegawa-Ishii, S., Chiba, Y., Furukawa, A., Kawamura, N., Hosokawa, M., Woodward, D.F., Watanabe, K. and Shimada, A. Preferential localization of prostamide/prostaglandin F synthase in myelin sheaths of the central nervous system. Brain Res. 1367 (2011) 22–32. [DOI] [PMID: 20950588] |
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[EC 1.11.1.20 created 2011] |
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EC |
1.14.99.1 |
Accepted name: |
prostaglandin-endoperoxide synthase |
Reaction: |
arachidonate + reduced acceptor + 2 O2 = prostaglandin H2 + acceptor + H2O |
Other name(s): |
prostaglandin synthase; prostaglandin G/H synthase; (PG)H synthase; PG synthetase; prostaglandin synthetase; fatty acid cyclooxygenase; prostaglandin endoperoxide synthetase |
Systematic name: |
(5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate,hydrogen-donor:oxygen oxidoreductase |
Comments: |
This enzyme acts both as a dioxygenase and as a peroxidase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39391-18-9 |
References: |
1. |
DeWitt, D.L. and Smith, W.L. Primary structure of prostaglandin G/H synthase from sheep vesicular gland determined from the complementary DNA sequence. Proc. Natl. Acad. Sci. USA 85 (1988) 1412–1416. [DOI] [PMID: 3125548] |
2. |
Ohki, S., Ogino, N., Yamamoto, S. and Hayaishi, O. Prostaglandin hydroperoxidase, an integral part of prostaglandin endoperoxide synthetase from bovine vesicular gland microsomes. J. Biol. Chem. 254 (1979) 829–836. [PMID: 104998] |
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[EC 1.14.99.1 created 1972, modified 1990] |
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EC |
5.3.99.4 |
Accepted name: |
prostaglandin-I synthase |
Reaction: |
(5Z,13E,15S)-9α,11α-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E,15S)-6,9α-epoxy-11α,15-dihydroxyprosta-5,13-dienoate |
Other name(s): |
prostacyclin synthase; prostacycline synthetase; prostagladin I2 synthetase; PGI2 synthase; PGI2 synthetase; (5Z,13E)-(15S)-9α,11α-epidioxy-15-hydroxyprosta-5,13-dienoate 6-isomerase |
Systematic name: |
(5Z,13E,15S)-9α,11α-epidioxy-15-hydroxyprosta-5,13-dienoate 6-isomerase |
Comments: |
A cytochrome P-450 heme-thiolate enzyme. Converts prostaglandin H2 into prostaglandin I2 (prostacyclin). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 65802-86-0 |
References: |
1. |
DeWitt, D.L. and Smith, W.L. Purification of prostacyclin synthase from bovine aorta by immunoaffinity chromatography. Evidence that the enzyme is a hemoprotein. J. Biol. Chem. 258 (1983) 3285–3293. [PMID: 6338016] |
2. |
Ullrich, V., Castle, L. and Weber, P. Spectral evidence for the cytochrome P450 nature of prostacyclin synthetase. Biochem. Pharmacol. 30 (1981) 2033–2036. [DOI] [PMID: 7023490] |
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[EC 5.3.99.4 created 1984, modified 1990] |
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EC |
5.3.99.5 |
Accepted name: |
thromboxane-A synthase |
Reaction: |
(5Z,13E)-(15S)-9α,11α-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-9α,11α-epoxy-15-hydroxythromboxa-5,13-dienoate |
Other name(s): |
thromboxane synthase; (5Z,13E)-(15S)-9α,11α-epidioxy-15-hydroxyprosta-5,13-dienoate thromboxane-A2-isomerase |
Systematic name: |
(5Z,13E)-(15S)-9α,11α-epidioxy-15-hydroxyprosta-5,13-dienoate isomerase |
Comments: |
A cytochrome P-450 heme-thiolate enzyme. Converts prostaglandin H2 into thromboxane A2. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 61276-89-9 |
References: |
1. |
Shen, R.-F. and Tai, H.-H. Immunoaffinity purification and characterization of thromboxane synthase from porcine lung. J. Biol. Chem. 261 (1986) 11592–11599. [PMID: 3745158] |
2. |
Ullrich, V. and Haurand, M. Thromboxane synthase as a cytochrome P450 enzyme. Adv. Prostaglandin Thromboxane Res. 11 (1983) 105–110. [PMID: 6221511] |
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[EC 5.3.99.5 created 1984, modified 1990] |
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