Acetoacetyl-CoA reductase
| acetoacetyl-CoA reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Acetoacetyl-CoA reductase tetramer, Cupriavidus necator | |||||||||
| Identifiers | |||||||||
| EC no. | 1.1.1.36 | ||||||||
| CAS no. | 9028-41-5 | ||||||||
| 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, an acetoacetyl-CoA reductase (EC 1.1.1.36) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are the (R) isomer of a 3-hydroxyacyl derivative of coenzyme A and oxidised nicotinamide adenine dinucleotide phosphate (NADP+). Its products are the corresponding 3-oxoacyl derivative of the coenzyme, reduced NADPH, and a proton.[1][2]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-3-hydroxyacyl-CoA:NADP+ oxidoreductase. Other names in common use include acetoacetyl coenzyme A reductase, hydroxyacyl coenzyme-A dehydrogenase, NADP+-linked acetoacetyl CoA reductase, NADPH:acetoacetyl-CoA reductase, D(−)-beta-hydroxybutyryl CoA-NADP+ oxidoreductase, short chain beta-ketoacetyl(acetoacetyl)-CoA reductase, beta-ketoacyl-CoA reductase, D-3-hydroxyacyl-CoA reductase, and (R)-3-hydroxyacyl-CoA dehydrogenase. This enzyme participates in butanoate metabolism.
See also
- 3-hydroxyacyl-CoA dehydrogenase operating on the enantiomer of the substrate
References
- ^ Enzyme 1.1.1.36 at KEGG Pathway Database.
- ^ Wakil S, Bressler R (March 1962). "Studies on the mechanism of fatty acid synthesis. X. Reduced triphosphopyridine nucleotide-acetoacetyl coenzyme A reductase". The Journal of Biological Chemistry. 237 (3): 687–93. doi:10.1016/S0021-9258(18)60356-4. PMID 14004466.