KEGG   ENZYME: 1.3.1.8Help
Entry
EC 1.3.1.8                  Enzyme                                 

Name
acyl-CoA dehydrogenase (NADP+);
2-enoyl-CoA reductase;
dehydrogenase, acyl coenzyme A (nicotinamide adenine dinucleotide phosphate);
enoyl coenzyme A reductase;
crotonyl coenzyme A reductase;
crotonyl-CoA reductase;
acyl-CoA dehydrogenase (NADP+)
Class
Oxidoreductases;
Acting on the CH-CH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
acyl-CoA:NADP+ 2-oxidoreductase
Reaction(IUBMB)
acyl-CoA + NADP+ = 2,3-dehydroacyl-CoA + NADPH + H+ [RN:R00385]
Reaction(KEGG)
Substrate
acyl-CoA [CPD:C00040];
NADP+ [CPD:C00006]
Product
2,3-dehydroacyl-CoA [CPD:C00605];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
The liver enzyme acts on enoyl-CoA derivatives of carbon chain length 4 to 16, with optimum activity on 2-hexenoyl-CoA. In Escherichia coli, cis-specific and trans-specific enzymes exist [EC 1.3.1.37 cis-2-enoyl-CoA reductase (NADPH) and EC 1.3.1.38 trans-2-enoyl-CoA reductase (NADPH)].
History
EC 1.3.1.8 created 1972, modified 1986
Pathway
ec00062  Fatty acid elongation
ec01100  Metabolic pathways
Reference
1  [PMID:6749495]
  Authors
Dommes V, Luster W, Cvetanovic M, Kunau WH.
  Title
Purification by affinity chromatography of 2,4-dienoyl-CoA reductases from bovine liver and Escherichia coli.
  Journal
Eur J Biochem 125:335-41 (1982)
DOI:10.1111/j.1432-1033.1982.tb06688.x
Reference
2  [PMID:4387390]
  Authors
Seubert W, Lamberts I, Kramer R, Ohly B.
  Title
On the mechanism of malonyl-CoA-independent fatty acid synthesis. I. The mechanism of elongation of long-chain fatty acids by acetyl-CoA.
  Journal
Biochim Biophys Acta 164:498-517 (1968)
DOI:10.1016/0005-2760(68)90180-X
Other DBs
ExplorEnz - The Enzyme Database: 1.3.1.8
IUBMB Enzyme Nomenclature: 1.3.1.8
ExPASy - ENZYME nomenclature database: 1.3.1.8
BRENDA, the Enzyme Database: 1.3.1.8
CAS: 37251-07-3

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