EC |
1.13.11.31 |
Accepted name: |
arachidonate 12-lipoxygenase |
Reaction: |
arachidonate + O2 = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate |
Other name(s): |
Δ12-lipoxygenase; 12-lipoxygenase; 12Δ-lipoxygenase; C-12 lipoxygenase; 12S-lipoxygenase; leukotriene A4 synthase; LTA4 synthase |
Systematic name: |
arachidonate:oxygen 12-oxidoreductase |
Comments: |
The product is rapidly reduced to the corresponding 12S-hydroxy compound. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 82391-43-3 |
References: |
1. |
Hamberg, M. and Samuelsson, B. Prostaglandin endoperoxides. Novel transformations of arachidonic acid in human platelets. Proc. Natl. Acad. Sci. USA 71 (1974) 3400–3404. [DOI] [PMID: 4215079] |
2. |
Nugteren, D.H. Arachidonate lipoxygenase in blood platelets. Biochim. Biophys. Acta 380 (1975) 299–307. [DOI] [PMID: 804329] |
3. |
Wallach, D.P. and 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 663 (1981) 361–372. [DOI] [PMID: 6783111] |
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[EC 1.13.11.31 created 1983] |
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EC |
1.13.11.33 |
Accepted name: |
arachidonate 15-lipoxygenase |
Reaction: |
arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate |
Other name(s): |
15-lipoxygenase; linoleic acid ω6-lipoxygenase; ω6 lipoxygenase |
Systematic name: |
arachidonate:oxygen 15-oxidoreductase |
Comments: |
The product is rapidly reduced to the corresponding 15S-hydroxy compound. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 82249-77-2 |
References: |
1. |
Bryant, R.W., Bailey, J.M., Schewqe, T. and Rapoport, S.M. Positional specificity of a reticulocyte lipoxygenase. Conversion of arachidonic acid to 15-S-hydroperoxy-eicosatetraenoic acid. J. Biol. Chem. 257 (1982) 6050–6055. [PMID: 6804460] |
2. |
Narumiya, S. and Salmon, J.A. Arachidonic acid-15-lipoxygenase from rabbit peritoneal polymorphonuclear leukocytes. Methods Enzymol. 86 (1982) 45–48. [PMID: 6813644] |
3. |
Oliw, E.H. and Sprecher, H. Metabolism of polyunsaturated fatty acids by an (n-6)-lipoxygenase associated with human ejaculates. Biochim. Biophys. Acta 1002 (1989) 283–291. [DOI] [PMID: 2496760] |
4. |
Shibata, D., Steczko, J., Dixon, F.E., Hermodson, M., Yasdanparast, R. and Axelrod, B. Primary structure of soybean lipoxygenase-1. J. Biol. Chem. 262 (1987) 10080–10085. [PMID: 3112136] |
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[EC 1.13.11.33 created 1984] |
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EC |
1.13.11.34 |
Accepted name: |
arachidonate 5-lipoxygenase |
Reaction: |
arachidonate + O2 = leukotriene A4 + H2O (overall reaction) (1a) arachidonate + O2 = (6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyicosa-6,8,11,14-tetraenoate (1b) (6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyicosa-6,8,11,14-tetraenoate = leukotriene A4 + H2O |
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For diagram of leukotriene biosynthesis, click here |
Glossary: |
leukotriene A4 = (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate |
Other name(s): |
leukotriene-A4 synthase; Δ5-lipoxygenase; 5Δ-lipoxygenase; arachidonic 5-lipoxygenase; arachidonic acid 5-lipoxygenase; C-5-lipoxygenase; LTA synthase; leukotriene A4 synthase |
Systematic name: |
arachidonate:oxygen 5-oxidoreductase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 80619-02-9 |
References: |
1. |
Matsumoto, T., Funk, C.D., Radmark, O., Hoog, J.-O., Jornvall, H. and Samuelsson, B. Molecular cloning and amino acid sequence of human 5-lipoxygenase. Proc. Natl. Acad. Sci. USA 85 (1988) 26–30. [DOI] [PMID: 2829172] |
2. |
Ohishi, N., Izumi, T., Minami, M., Kitamura, S., Seyama, Y., Ohkawa, S., Terao, S., Yotsumoto, H., Takaku, F. and Shimizu, T. Leukotriene A4 hydrolase in the human lung. Inactivation of the enzyme with leukotriene A4 isomers. J. Biol. Chem. 262 (1987) 10200–10205. [PMID: 3038871] |
3. |
Shimizu, T., Izumi, T., Seyama, Y., Tadokoro, K., Rädmark, O. and Samuelsson, B. Characterization of leukotriene A4 synthase from murine mast cells: evidence for its identity to arachidonate 5-lipoxygenase. Proc. Natl. Acad. Sci. USA 83 (1986) 4175–4179. [DOI] [PMID: 3012557] |
4. |
Shimizu, T., Rädmark, O. and Samuelssohn, B. Enzyme with dual lipoxygenase activities catalyzes leukotriene A4 synthesis from arachidonic acid. Proc. Natl. Acad. Sci. USA 81 (1984) 689–693. [DOI] [PMID: 6322165] |
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[EC 1.13.11.34 created 1984, modified 1990] |
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EC |
1.13.11.40 |
Accepted name: |
arachidonate 8-lipoxygenase |
Reaction: |
arachidonate + O2 = (5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14-tetraenoate |
Other name(s): |
8-lipoxygenase; 8(R)-lipoxygenase |
Systematic name: |
arachidonate:oxygen 8-oxidoreductase |
Comments: |
From the coral Pseudoplexaura porosa. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 100900-72-9 |
References: |
1. |
Bundy, G.L., Nidy, E.G., Epps, D.E., Mizsak, S.A. and Wnuk, R.J. Discovery of an arachidonic acid C-8 lipoxygenase in the gorgonian coral Pseudoplexaura porosa. J. Biol. Chem. 261 (1986) 747–751. [PMID: 2867091] |
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[EC 1.13.11.40 created 1989] |
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EC
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1.13.11.44
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Deleted entry: | linoleate diol synthase. Activity is covered by EC 1.13.11.60, linoleate 8R-lipoxygenase and EC 5.4.4.6, 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase. |
[EC 1.13.11.44 created 2000, deleted 2011] |
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EC |
1.13.11.45 |
Accepted name: |
linoleate 11-lipoxygenase |
Reaction: |
linoleate + O2 = (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate |
Glossary: |
arachidonate = (all-Z)-icosa-5,8,11,14-tetraenoate
linoleate = (9Z,12Z)-octadeca-9,12-dienoate
α-linolenate = (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
γ-linolenate = (6Z,9Z,12Z)-octadeca-6,9,12-trienoate
oleate = (Z)-octadec-9-enoate |
Other name(s): |
linoleate dioxygenase; manganese lipoxygenase |
Systematic name: |
linoleate:oxygen 11S-oxidoreductase |
Comments: |
The product (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate, is converted, more slowly, into (9Z,11E)-(13R)-13-hydroperoxyoctadeca-9,11-dienoate. The enzyme from the fungus Gaeumannomyces graminis requires Mn2+. It also acts on α-linolenate, whereas γ-linolenate is a poor substrate. Oleate and arachidonate are not substrates. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Hamberg, M., Su, C. and Oliw, E.H. Manganese lipoxygenase: Discovery of bis-allylic hydroperoxide as product and intermediate in a lipoxygenase reaction. J. Biol. Chem. 273 (1998) 13080–13088. [DOI] [PMID: 9582346] |
2. |
Oliw, E.H., Su, C., Skogstrom, T. and Benthin, G. Analysis of novel hydroperoxides and other metabolites of oleic, linoleic and linolenic acids by liquid chromatography-mass spectrometry with ion trap MSn. Lipids 33 (1998) 843–852. [DOI] [PMID: 9778131] |
3. |
Su, C. and Oliw, E.H. Manganese lipoxygenase: Purification and characterization. J. Biol. Chem. 273 (1998) 13072–13079. [DOI] [PMID: 9582345] |
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[EC 1.13.11.45 created 2000] |
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EC
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1.14.13.205
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Transferred entry: | long-chain fatty acid ω-monooxygenase. Now EC 1.14.14.80, long-chain fatty acid ω-monooxygenase
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[EC 1.14.13.205 created 2015, deleted 2018] |
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EC |
1.14.14.80 |
Accepted name: |
long-chain fatty acid ω-monooxygenase |
Reaction: |
a long-chain fatty acid + [reduced NADPH—hemoprotein reductase] + O2 = an ω-hydroxy-long-chain fatty acid + [oxidized NADPH—hemoprotein reductase] + H2O |
Other name(s): |
CYP704B1 (gene name); CYP52M1 (gene name); CYP4A (gene name); CYP86A (gene name) |
Systematic name: |
long-chain fatty acid,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (ω-hydroxylating) |
Comments: |
A cytochrome P-450 (heme thiolate) enzyme. The plant enzyme CYP704B1, which is involved in the synthesis of sporopollenin, a complex polymer found at the outer layer of spores and pollen, acts on palmitate (18:0), stearate (18:0) and oleate (18:1). The plant enzyme CYP86A1 also acts on laurate (12:0). The enzyme from the yeast Starmerella bombicola (CYP52M1) acts on C16 to C20 saturated and unsaturated fatty acids and can also hydroxylate the (ω-1) position. The mammalian enzyme CYP4A acts on laurate (12:0), myristate (14:0), palmitate (16:0), oleate (18:1), and arachidonate (20:4). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Benveniste, I., Tijet, N., Adas, F., Philipps, G., Salaun, J.P. and Durst, F. CYP86A1 from Arabidopsis thaliana encodes a cytochrome P450-dependent fatty acid ω-hydroxylase. Biochem. Biophys. Res. Commun. 243 (1998) 688–693. [DOI] [PMID: 9500987] |
2. |
Hoch, U., Zhang, Z., Kroetz, D.L. and Ortiz de Montellano, P.R. Structural determination of the substrate specificities and regioselectivities of the rat and human fatty acid ω-hydroxylases. Arch. Biochem. Biophys. 373 (2000) 63–71. [DOI] [PMID: 10620324] |
3. |
Dobritsa, A.A., Shrestha, J., Morant, M., Pinot, F., Matsuno, M., Swanson, R., Møller, B.L. and Preuss, D. CYP704B1 is a long-chain fatty acid ω-hydroxylase essential for sporopollenin synthesis in pollen of Arabidopsis. Plant Physiol. 151 (2009) 574–589. [DOI] [PMID: 19700560] |
4. |
Huang, F.C., Peter, A. and Schwab, W. Expression and characterization of CYP52 genes involved in the biosynthesis of sophorolipid and alkane metabolism from Starmerella bombicola. Appl. Environ. Microbiol. 80 (2014) 766–776. [DOI] [PMID: 24242247] |
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[EC 1.14.14.80 created 2015 as EC 1.14.13.205, transferred 2018 to EC 1.14.14.80] |
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EC |
1.14.19.4 |
Accepted name: |
acyl-lipid (11-3)-desaturase |
Reaction: |
(1) an (11Z,14Z)-icosa-11,14-dienoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an (8Z,11Z,14Z)-icosa-8,11,14-trienoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O (2) an (11Z,14Z,17Z)-icosa-11,14,17-trienoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = an (8Z,11Z,14Z,17Z)-icosa-8,11,14,17-tetraenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O |
Glossary: |
di-homo-γ-linolenate = (8Z,11Z,14Z)-icosa-8,11,14-trienoate |
Other name(s): |
acyl-lipid 8-desaturase; Δ8 fatty acid desaturase; Δ8-desaturase; Δ8-fatty-acid desaturase; efd1 (gene name); D8Des (gene name); phytosphinganine,hydrogen donor:oxygen Δ8-oxidoreductase (incorrect); SLD |
Systematic name: |
acyl-lipid,ferrocytochrome b5:oxygen oxidoreductase [(11-3),(11-2)-cis-dehydrogenating] |
Comments: |
The enzyme, characterized from the protist Euglena gracilis [1] and the microalga Rebecca salina [2], introduces a cis double bond at the 8-position in 20-carbon fatty acids that are incorporated into a glycerolipid and have an existing Δ11 desaturation. The enzyme is a front-end desaturase, introducing the new double bond between the pre-existing double bond and the carboxyl-end of the fatty acid. It contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome. Involved in alternative pathways for the biosynthesis of the polyunsaturated fatty acids arachidonate and icosapentaenoate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Wallis, J.G. and Browse, J. The Δ8-desaturase of Euglena gracilis: an alternate pathway for synthesis of 20-carbon polyunsaturated fatty acids. Arch. Biochem. Biophys. 365 (1999) 307–316. [DOI] [PMID: 10328826] |
2. |
Zhou, X.R., Robert, S.S., Petrie, J.R., Frampton, D.M., Mansour, M.P., Blackburn, S.I., Nichols, P.D., Green, A.G. and Singh, S.P. Isolation and characterization of genes from the marine microalga Pavlova salina encoding three front-end desaturases involved in docosahexaenoic acid biosynthesis. Phytochemistry 68 (2007) 785–796. [DOI] [PMID: 17291553] |
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[EC 1.14.19.4 created 2008, modified 2015] |
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EC |
1.14.19.30 |
Accepted name: |
acyl-lipid (8-3)-desaturase |
Reaction: |
(1) an (8Z,11Z,14Z)-icosa-8,11,14-trienoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (5Z,8Z,11Z,14Z)-icosatetra-5,8,11,14-tetraenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O (2) an (8Z,11Z,14Z,17Z)-icosa-8,11,14,17-tetraenoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = a (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O |
Glossary: |
(8Z,11Z,14Z)-icosa-8,11,14-trienoate = di-homo-γ-linolenate
(5Z,8Z,11Z,14Z)-icosa-8,11,14-trienoate = arachidonate |
Other name(s): |
acyl-lipid 5-desaturase; Δ5-fatty-acid desaturase; DES5 (gene name); D5des (gene name); FADS1 |
Systematic name: |
Δ8 acyl-lipid,ferrocytochrome b5:oxygen oxidoreductase (5,6 cis-dehydrogenating) |
Comments: |
The enzyme, which has been characterized from multiple organisms including the moss Physcomitrella patens, the marine microalga Rebecca salina, and the filamentous fungus Mortierella alpina, introduces a cis double bond at the 5-position in 20-carbon polyunsaturated fatty acids incorporated in a glycerolipid that contain a Δ8 double bond. The enzyme contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase, and does not require an external cytochrome. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Michaelson, L.V., Lazarus, C.M., Griffiths, G., Napier, J.A. and Stobart, A.K. Isolation of a Δ5-fatty acid desaturase gene from Mortierella alpina. J. Biol. Chem. 273 (1998) 19055–19059. [DOI] [PMID: 9668087] |
2. |
Kaewsuwan, S., Cahoon, E.B., Perroud, P.F., Wiwat, C., Panvisavas, N., Quatrano, R.S., Cove, D.J. and Bunyapraphatsara, N. Identification and functional characterization of the moss Physcomitrella patens Δ5-desaturase gene involved in arachidonic and eicosapentaenoic acid biosynthesis. J. Biol. Chem. 281 (2006) 21988–21997. [DOI] [PMID: 16728405] |
3. |
Zhou, X.R., Robert, S.S., Petrie, J.R., Frampton, D.M., Mansour, M.P., Blackburn, S.I., Nichols, P.D., Green, A.G. and Singh, S.P. Isolation and characterization of genes from the marine microalga Pavlova salina encoding three front-end desaturases involved in docosahexaenoic acid biosynthesis. Phytochemistry 68 (2007) 785–796. [DOI] [PMID: 17291553] |
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[EC 1.14.19.30 created 2015] |
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EC |
1.14.19.44 |
Accepted name: |
acyl-CoA (8-3)-desaturase |
Reaction: |
(1) (8Z,11Z,14Z)-icosa-8,11,14-trienoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = arachidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O (2) (8Z,11Z,14Z,17Z)-icosa-8,11,14,17-tetraenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoyl-CoA + 2 ferricytochrome b5 + 2 H2O |
Other name(s): |
FADS1 (gene name); acyl-CoA 5-desaturase (methylene-interrupted) |
Systematic name: |
Δ8-acyl-CoA,ferrocytochrome b5:oxygen oxidoreductase (5,6-cis-dehydrogenating) |
Comments: |
The enzyme introduces a cis double bond at carbon 5 of acyl-CoAs that contain a double bond at position 8. The enzymes from algae, mosses, mammals and the protozoan Leishmania major catalyse the desaturation of dihomo-γ-linoleate [(8Z,11Z,14Z)-icosa-8,11,14-trienoate] and (8Z,11Z,14Z,17Z)-icosa-8,11,14,17-tetraenoate to generate arachidonate and (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoate, respectively. The enzyme contains a cytochrome b5 domain that acts as the direct electron donor to the desaturase active site and does not require an external cytochrome. cf. EC 1.14.19.37, acyl-CoA 5-desaturase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Cho, H.P., Nakamura, M. and Clarke, S.D. Cloning, expression, and fatty acid regulation of the human Δ5 desaturase. J. Biol. Chem. 274 (1999) 37335–37339. [DOI] [PMID: 10601301] |
2. |
Leonard, A.E., Kelder, B., Bobik, E.G., Chuang, L.T., Parker-Barnes, J.M., Thurmond, J.M., Kroeger, P.E., Kopchick, J.J., Huang, Y.S. and Mukerji, P. cDNA cloning and characterization of human Δ5-desaturase involved in the biosynthesis of arachidonic acid. Biochem. J. 347 Pt 3 (2000) 719–724. [PMID: 10769175] |
3. |
Tripodi, K.E., Buttigliero, L.V., Altabe, S.G. and Uttaro, A.D. Functional characterization of front-end desaturases from trypanosomatids depicts the first polyunsaturated fatty acid biosynthetic pathway from a parasitic protozoan. FEBS J. 273 (2006) 271–280. [DOI] [PMID: 16403015] |
4. |
Tavares, S., Grotkjær, T., Obsen, T., Haslam, R.P., Napier, J.A. and Gunnarsson, N. Metabolic engineering of Saccharomyces cerevisiae for production of eicosapentaenoic acid, using a novel Δ5-desaturase from Paramecium tetraurelia. Appl. Environ. Microbiol. 77 (2011) 1854–1861. [DOI] [PMID: 21193673] |
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[EC 1.14.19.44 created 2015] |
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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 |
2.3.1.147 |
Accepted name: |
glycerophospholipid arachidonoyl-transferase (CoA-independent) |
Reaction: |
1-organyl-2-arachidonoyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine = 1-organyl-2-arachidonoyl-sn-glycero-3-phosphoethanolamine + 1-organyl-2-lyso-sn-glycero-3-phosphocholine |
Systematic name: |
1-organyl-2-arachidonoyl-sn-glycero-3-phosphocholine:1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine arachidonoyltransferase (CoA-independent) |
Comments: |
Catalyses the transfer of arachidonate and other polyenoic fatty acids from intact choline or ethanolamine-containing glycerophospholipids to the sn-2 position of a lyso-glycerophospholipid. The organyl group on sn-1 of the donor or acceptor molecule can be alkyl, acyl or alk-1-enyl. The term 'radyl' has sometimes been used to refer to such substituting groups. Differs from EC 2.3.1.148 glycerophospholipid acyltransferase (CoA-dependent) in not requiring CoA and in its specificity for poly-unsaturated acyl groups. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 102347-79-5 |
References: |
1. |
Robinson, M., Blank, M.L., Snyder, F. Acylation of lysophospholipids by rabbit alveolar macrophages. Specific CoA-dependent and CoA-independent reactions. J. Biol. Chem. 260 (1985) 7889–7895. [PMID: 4008481] |
2. |
Snyder, F., Lee, T.C., Blank, M.L. The role of transacylases in the metabolism of arachidonate and platelet-activating factor. Prog. Lipid Res. 31 (1992) 65–86. [DOI] [PMID: 1641397] |
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[EC 2.3.1.147 created 1999] |
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EC |
2.3.1.148 |
Accepted name: |
glycerophospholipid acyltransferase (CoA-dependent) |
Reaction: |
1-organyl-2-acyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine = 1-organyl-2-acyl-sn-glycero-3-phosphoethanolamine + 1-organyl-2-lyso-sn-glycero-3-phosphocholine |
Systematic name: |
1-organyl-2-acyl-sn-glycero-3-phosphocholine:1-organyl-2-lyso-sn-glycero-3-phosphoethanolamine acyltransferase (CoA-dependent) |
Comments: |
Catalyses the transfer of fatty acids from intact choline- or ethanolamine-containing glycerophospholipids to the sn-2 position of a lyso-glycerophospholipid. The organyl group on sn-1 of the donor or acceptor molecule can be alkyl, acyl or alk-1-enyl. The term 'radyl' has sometimes been used to refer to such substituting groups. Differs from EC 2.3.1.147 glycerophospholipid arachidonoyl-transferase (CoA-independent) in requiring CoA and not favouring the transfer of polyunsaturated acyl groups. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9054-54-0 |
References: |
1. |
Irvine, R.F., Dawson, R.M.C. Transfer of arachidonic acid between phospholipids in rat liver microsomes. Biochem. Biophys. Res. Commun. 91 (1979) 1399–1405. [DOI] [PMID: 526311] |
2. |
Robinson, M., Blank, M.L., Snyder, F. Acylation of lysophospholipids by rabbit alveolar macrophages. Specific CoA-dependent and CoA-independent reactions. J. Biol. Chem. 260 (1985) 7889–7895. [PMID: 4008481] |
3. |
Snyder, F., Lee, T.C., Blank, M.L. The role of transacylases in the metabolism of arachidonate and platelet-activating factor. Prog. Lipid Res. 31 (1992) 65–86. [DOI] [PMID: 1641397] |
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[EC 2.3.1.148 created 1999] |
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EC |
3.1.1.67 |
Accepted name: |
fatty-acyl-ethyl-ester synthase |
Reaction: |
a long-chain-fatty-acyl ethyl ester + H2O = a long-chain-fatty acid + ethanol |
Glossary: |
a long-chain-fatty acid = a fatty acid with an aliphatic chain of 13-22 carbons. |
Other name(s): |
FAEES |
Systematic name: |
long-chain-fatty-acyl-ethyl-ester acylhydrolase |
Comments: |
The reaction, forms ethyl esters from fatty acids and ethanol in the absence of coenzyme A or ATP. Best substrates are unsaturated octadecanoic acids; palmitate, stearate and arachidonate also act, but more slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 90119-16-7 |
References: |
1. |
Mogelson, S. and Lange, L.G. Nonoxidative ethanol metabolism in rabbit myocardium: purification to homogeneity of fatty acyl ethyl ester synthase. Biochemistry 23 (1984) 4075–4081. [PMID: 6487591] |
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[EC 3.1.1.67 created 1989] |
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EC |
3.1.1.116 |
Accepted name: |
sn-1-specific diacylglycerol lipase |
Reaction: |
a 1,2-diacyl-sn-glycerol + H2O = a 2-acylglycerol + a fatty acid |
Other name(s): |
DAGLA (gene name); DAGLB (gene name) |
Systematic name: |
diacylglycerol sn-1-acylhydrolase |
Comments: |
The enzyme, present in animals, is specific for the sn-1 position. When acting on 1-acyl-2-arachidonoyl-sn-glycerol, the enzyme forms 2-arachidonoylglycerol, the most abundant endocannabinoid in the mammalian brain. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Chau, L.Y. and Tau, H.H. Release of arachidonate from diglyceride in human platelets requires the sequential action of a diglyceride lipase and a monoglyceride lipase. Biochem. Biophys. Res. Commun. 100 (1988) 1688–1695. [DOI] [PMID: 7295321] |
2. |
Bisogno, T., Howell, F., Williams, G., Minassi, A., Cascio, M.G., Ligresti, A., Matias, I., Schiano-Moriello, A., Paul, P., Williams, E.J., Gangadharan, U., Hobbs, C., Di Marzo, V. and Doherty, P. Cloning of the first sn1-DAG lipases points to the spatial and temporal regulation of endocannabinoid signaling in the brain. J. Cell Biol. 163 (2003) 463–468. [DOI] [PMID: 14610053] |
3. |
Bisogno, T. Assay of DAGLα/β activity. Methods Mol. Biol. 1412 (2016) 149–156. [DOI] [PMID: 27245901] |
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[EC 3.1.1.116 created 2021] |
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EC |
5.3.3.13 |
Accepted name: |
polyenoic fatty acid isomerase |
Reaction: |
(5Z,8Z,11Z,14Z,17Z)-icosapentaenoate = (5Z,7E,9E,14Z,17Z)-icosapentaenoate |
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For diagram of reaction, click here |
Other name(s): |
PFI; eicosapentaenoate cis-Δ5,8,11,14,17-eicosapentaenoate cis-Δ5-trans-Δ7,9-cis-Δ14,17 isomerase; (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate Δ8,11-Δ7,8-isomerase (incorrect); (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate Δ8,11-Δ7,9-isomerase (trans-double-bond-forming) |
Systematic name: |
(5Z,8Z,11Z,14Z,17Z)-icosapentaenoate Δ8,11-Δ7,9-isomerase (trans-double-bond-forming) |
Comments: |
The enzyme from the red alga Ptilota filicina catalyses the isomerization of skip dienes (methylene-interrupted double bonds) in a broad range of fatty acids and fatty-acid analogues, such as arachidonate and γ-linolenate, to yield a conjugated triene. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 159002-84-3 |
References: |
1. |
Wise, M.L., Hamberg, M. and Gerwick, W.H. Biosynthesis of conjugated fatty acids by a novel isomerase from the red marine alga Ptilota filicina. Biochemistry 33 (1994) 15223–15232. [PMID: 7803384] |
2. |
Wise, M.L., Soderstrom, K., Murray, T.F. and Gerwick, W.H. Synthesis and cannabinoid receptor binding activity of conjugated triene anandamide, a novel eicosanoid. Experientia 52 (1996) 88–92. [PMID: 8575565] |
3. |
Wise, M.L., Rossi, J. and Gerwick, W.H. Binding site characterization of polyenoic fatty-acid isomerase from the marine alga Ptilota filicina. Biochemistry 36 (1997) 2985–2992. [DOI] [PMID: 9062129] |
4. |
Zheng, W., Wise, M.L., Wyrick, A., Metz, J.G., Yuan, L. and Gerwick, W.H. Polyenoic fatty-acid isomerase from the marine red alga Ptilota filicina: protein characterization and functional expression of the cloned cDNA. Arch. Biochem. Biophys. 401 (2002) 11–20. [DOI] [PMID: 12054482] |
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[EC 5.3.3.13 created 2004] |
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EC |
6.2.1.15 |
Accepted name: |
arachidonate—CoA ligase |
Reaction: |
ATP + arachidonate + CoA = AMP + diphosphate + arachidonoyl-CoA |
Glossary: |
arachidonate = (all-Z)-icosa-5,8,11,14-tetraenoate |
Other name(s): |
arachidonoyl-CoA synthetase |
Systematic name: |
arachidonate:CoA ligase (AMP-forming) |
Comments: |
Not identical with EC 6.2.1.3 long-chain-fatty-acid—CoA ligase. Icosa-8,11,14-trienoate, but not the other long-chain fatty acids, can act in place of arachidonate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 82047-87-8 |
References: |
1. |
Wilson, D.B., Prescott, S.M. and Majerus, P.W. Discovery of an arachidonoyl coenzyme A synthetase in human platelets. J. Biol. Chem. 257 (1982) 3510–3515. [PMID: 7061494] |
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[EC 6.2.1.15 created 1984] |
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