Enzyme

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EC Tree
     1. Oxidoreductases
        1.3 Acting on the CH-CH group of donors
            1.3.1 With NAD+ or NADP+ as acceptor
ID:1.3.1.8
Description:Acyl-CoA dehydrogenase (NADP(+)).
Alternative Name: Enoyl coenzyme A reductase.
2-enoyl-CoA reductase.
Cath: 3.40.50.720; 3.90.180.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.3.1.8
BRENDA Enzyme Link: BRENDA 1.3.1.8
KEGG Enzyme Link: KEGG1.3.1.8
BioCyc Enzyme Link: BioCyc 1.3.1.8
ExPASy Enzyme Link: ExPASy1.3.1.8
EC2PDB Enzyme Link: EC2PDB 1.3.1.8
ExplorEnz Enzyme Link: ExplorEnz 1.3.1.8
PRIAM enzyme-specific profiles Link: PRIAM 1.3.1.8
IntEnz Enzyme Link: IntEnz 1.3.1.8
MEDLINE Enzyme Link: MEDLINE 1.3.1.8
MSA:

1.3.1.8;

Phylogenetic Tree:

1.3.1.8;

Uniprot:
M-CSA:
RHEA:22460 a 2,3-saturated acyl-CoA + NADP(+) = a 2,3-dehydroacyl-CoA + H(+) + NADPH
RULE(radius=1) [*:1]-[CH2;+0:2]-[CH2;+0:3]-[*:4].[*:5]-[c;H0;+0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[n+;H0:10](-[*:11]):[cH;+0:12]:1>>[*:5]-[C;H0;+0:6]1=[CH;+0:12]-[N;H0;+0:10](-[*:11])-[CH;+0:9]=[CH;+0:8]-[CH2;+0:7]-1.[*:1]-[CH;+0:2]=[CH;+0:3]-[*:4]
Reaction
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References

TitleAuthorsDatePubMed ID
Purification by affinity chromatography of 2,4-dienoyl-CoA reductases from bovine liver and Escherichia coli.Dommes V, Luster W, Cvetanović M, Kunau WH1982 Jul6749495
On the mechanism of malonyl-CoA-independent fatty acid synthesis. I. The mechanism of elongation of long-chain fatty acids by acetyl-CoA.Seubert W, Lamberts I, Kramer R, Ohly B1968 Dec 184387390