The Enzyme Database

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EC 1.14.13.199      
Transferred entry: docosahexaenoic acid ω-hydroxylase. Now EC 1.14.14.79, docosahexaenoic acid ω-hydroxylase
[EC 1.14.13.199 created 2014, deleted 2018]
 
 
EC 1.14.14.79     
Accepted name: docosahexaenoic acid ω-hydroxylase
Reaction: docosahexaenoate + [reduced NADPH—hemoprotein reductase] + O2 = 22-hydroxydocosahexaenoate + [oxidized NADPH—hemoprotein reductase] + H2O
Glossary: docosahexaenoate = (4Z,7Z,10Z,13Z,16Z,19Z)-docosa-4,7,10,13,16,19-hexaenoate
icosapentaenoate = (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoate
Other name(s): CYP4F3B; CYP4V2; docosahexaenoate,NADPH:O2 oxidoreductase (22-hydroxydocosahexaenoate forming)
Systematic name: docosahexaenoate,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (22-hydroxydocosahexaenoate-forming)
Comments: A cytochrome P-450 (heme-thiolate) protein isolated from human eye tissue. Defects in the enzyme are associated with Bietti crystalline corneoretinal dystrophy. The enzyme also produces some 21-hydroxydocosahexaenoate. Acts in a similar way on icosapentaenoic acid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Nakano, M., Kelly, E.J., Wiek, C., Hanenberg, H. and Rettie, A.E. CYP4V2 in Bietti’s crystalline dystrophy: ocular localization, metabolism of ω-3-polyunsaturated fatty acids, and functional deficit of the p.H331P variant. Mol. Pharmacol. 82 (2012) 679–686. [DOI] [PMID: 22772592]
[EC 1.14.14.79 created 2014 as EC 1.14.13.199, transferred 2018 to EC 1.14.14.79]
 
 
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]
[EC 1.14.19.4 created 2008, modified 2015]
 
 
EC 5.3.3.13     
Accepted name: polyenoic fatty acid isomerase
Reaction: (5Z,8Z,11Z,14Z,17Z)-icosapentaenoate = (5Z,7E,9E,14Z,17Z)-icosapentaenoate
For diagram of reaction, click here
Other name(s): PFI; eicosapentaenoate cis5,8,11,14,17-eicosapentaenoate cis5-trans7,9-cis14,17 isomerase; (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate Δ8,117,8-isomerase (incorrect); (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate Δ8,117,9-isomerase (trans-double-bond-forming)
Systematic name: (5Z,8Z,11Z,14Z,17Z)-icosapentaenoate Δ8,117,9-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]
[EC 5.3.3.13 created 2004]
 
 


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