| long-chain-fatty-acyl-CoA reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.1.50 | ||||||||
| CAS no. | 50936-56-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a long-chain-fatty-acyl-CoA reductase (EC 1.2.1.50) is an enzyme that catalyzes the chemical reaction
- a long-chain aldehyde + CoA + NADP a long-chain acyl-CoA + NADPH + H
a long-chain acyl-CoA + NADPH + HThe 3 substrates of this enzyme are long-chain aldehyde, CoA, and NADP, whereas its 3 products are long-chain acyl-CoA, NADPH, and H.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is long-chain-aldehyde:NADP+ oxidoreductase (acyl-CoA-forming). Other names in common use include acyl-CoA reductase, and acyl coenzyme A reductase.
References
- Riendeau D, Rodriguez A, Meighen E (1982). "Resolution of the fatty acid reductase from Photobacterium phosphoreum into acyl protein synthetase and acyl-CoA reductase activities. Evidence for an enzyme complex". J. Biol. Chem. 257 (12): 6908–15. PMID 7085612.
- Wall L; Meighen EA (1986). "Subunit structure of the fatty-acid reductase complex from Photobacterium phosphoreum". Biochemistry. 25 (15): 4315–4321. doi:10.1021/bi00363a021.
| Aldehyde/oxo oxidoreductases (EC 1.2) | |
|---|---|
| 1.2.1: NAD or NADP | |
| 1.2.2: cytochrome | |
| 1.2.3: oxygen | |
| 1.2.4: disulfide | |
| 1.2.7: iron–sulfur protein | |
| Enzymes | |
|---|---|
| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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