| EC |
1.3.1.8 |
| Accepted name: |
acyl-CoA dehydrogenase (NADP+) |
| Reaction: |
acyl-CoA + NADP+ = 2,3-dehydroacyl-CoA + NADPH + H+ |
| Other name(s): |
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+) |
| Systematic name: |
acyl-CoA:NADP+ 2-oxidoreductase |
| Comments: |
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)]. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37251-07-3 |
| References: |
| 1. |
Dommes, V., Luster, W., Cvetanovic, M. and Kunau, W.-H. Purification by affinity chromatography of 2,4-dienoyl-CoA reductases from bovine liver and Escherichia coli. Eur. J. Biochem. 125 (1982) 335–341. [DOI] [PMID: 6749495] |
| 2. |
Seubert, W., Lamberts, I., Kramer, R. and Ohly, B. On the mechanism of malonyl-CoA-independent fatty acid synthesis. I. The mechanism of elongation of long-chain fatty acids by acetyl-CoA. Biochim. Biophys. Acta 164 (1968) 498–517. [DOI] [PMID: 4387390] |
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| [EC 1.3.1.8 created 1972, modified 1986] |
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