Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.19 With oxidation of a pair of donors resulting in the reduction of O2 to two molecules of water
ID:1.14.19.44
Description:Acyl-CoA (8-3)-desaturase.
Alternative Name: Acyl-CoA 5-desaturase (methylene-interrupted).

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.19.44
BRENDA Enzyme Link: BRENDA 1.14.19.44
KEGG Enzyme Link: KEGG1.14.19.44
BioCyc Enzyme Link: BioCyc 1.14.19.44
ExPASy Enzyme Link: ExPASy1.14.19.44
EC2PDB Enzyme Link: EC2PDB 1.14.19.44
ExplorEnz Enzyme Link: ExplorEnz 1.14.19.44
PRIAM enzyme-specific profiles Link: PRIAM 1.14.19.44
IntEnz Enzyme Link: IntEnz 1.14.19.44
MEDLINE Enzyme Link: MEDLINE 1.14.19.44
MSA:

1.14.19.44;

Phylogenetic Tree:

1.14.19.44;

Uniprot:
M-CSA:
RHEA:46424 (8Z,11Z,14Z)-eicosatrienoyl-CoA + 2 [Fe(II)-cytochrome b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 2 [Fe(III)-cytochrome b5] + 2 H2O
RULE(radius=1) [*:1]-[CH2;+0:2]-[CH2;+0:3]-[*:4].[Fe+2;H0:5].[Fe+2;H0:6].[H+;H0:7].[H+;H0:8].[O;H0;+0:9]=[O;H0;+0:10]>>[*:1]-[CH;+0:2]=[CH;+0:3]-[*:4].[Fe+3;H0:5].[Fe+3;H0:6].[OH2;+0:9].[OH2;+0:10]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
cDNA cloning and characterization of human Delta5-desaturase involved in the biosynthesis of arachidonic acid.Leonard AE, Kelder B, Bobik EG, Chuang LT, Parker-Barnes JM, Thurmond JM, Kroeger PE, Kopchick JJ, Huang YS, Mukerji P2000 May 110769175
Cloning, expression, and fatty acid regulation of the human delta-5 desaturase.Cho HP, Nakamura M, Clarke SD1999 Dec 2410601301
Metabolic engineering of Saccharomyces cerevisiae for production of Eicosapentaenoic Acid, using a novel {Delta}5-Desaturase from Paramecium tetraurelia.Tavares S, Grotkjær T, Obsen T, Haslam RP, Napier JA, Gunnarsson N2011 Mar21193673
Functional characterization of front-end desaturases from trypanosomatids depicts the first polyunsaturated fatty acid biosynthetic pathway from a parasitic protozoan.Tripodi KE, Buttigliero LV, Altabe SG, Uttaro AD2006 Jan16403015

RHEA:46420 (8Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + 2 [Fe(II)-cytochrome b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + 2 [Fe(III)-cytochrome b5] + 2 H2O
RULE(radius=1) [*:1]-[CH2;+0:2]-[CH2;+0:3]-[*:4].[Fe+2;H0:5].[Fe+2;H0:6].[H+;H0:7].[H+;H0:8].[O;H0;+0:9]=[O;H0;+0:10]>>[*:1]-[CH;+0:2]=[CH;+0:3]-[*:4].[Fe+3;H0:5].[Fe+3;H0:6].[OH2;+0:9].[OH2;+0:10]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
cDNA cloning and characterization of human Delta5-desaturase involved in the biosynthesis of arachidonic acid.Leonard AE, Kelder B, Bobik EG, Chuang LT, Parker-Barnes JM, Thurmond JM, Kroeger PE, Kopchick JJ, Huang YS, Mukerji P2000 May 110769175
Cloning, expression, and fatty acid regulation of the human delta-5 desaturase.Cho HP, Nakamura M, Clarke SD1999 Dec 2410601301
Metabolic engineering of Saccharomyces cerevisiae for production of Eicosapentaenoic Acid, using a novel {Delta}5-Desaturase from Paramecium tetraurelia.Tavares S, Grotkjær T, Obsen T, Haslam RP, Napier JA, Gunnarsson N2011 Mar21193673
Functional characterization of front-end desaturases from trypanosomatids depicts the first polyunsaturated fatty acid biosynthetic pathway from a parasitic protozoan.Tripodi KE, Buttigliero LV, Altabe SG, Uttaro AD2006 Jan16403015