| 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 | ||||||||
| |||||||||
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+
The 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.
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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.
This page was last edited on 26 August 2023, at 14:47