| carbonyl reductase (NADPH) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 carbonyl reductase tetramer, Mouse | |||||||||
| Identifiers | |||||||||
| EC no. | 1.1.1.184 | ||||||||
| CAS no. | 89700-36-7 | ||||||||
| 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 carbonyl reductase (NADPH) (EC 1.1.1.184) is an enzyme that catalyzes the chemical reaction
R-CO-R' + NADPH + H+ :R-CHOH-R' + NADP+
Thus, the two products of this enzyme are R-CHOH-R' and NADP+, whereas its 3 substrates are R-CO-R', NADPH, and H+.
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 secondary-alcohol:NADP+ oxidoreductase. Other names in common use include aldehyde reductase 1, prostaglandin 9-ketoreductase, xenobiotic ketone reductase, NADPH-dependent carbonyl reductase, ALR3, carbonyl reductase, nonspecific NADPH-dependent carbonyl reductase, aldehyde reductase 1, and carbonyl reductase (NADPH). This enzyme participates in arachidonic acid metabolism, and has recently been shown to catabolize S-Nitrosoglutathione, as a means to degrade NO in an NADPH-dependent manner.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1CYD, 1WMA, 2HRB, and 2PFG.
References
- Ahmed NK, Felsted RL, Bachur NR (1978). "Heterogeneity of anthracycline antibiotic carbonyl reductases in mammalian livers". Biochem. Pharmacol. 27 (23): 2713–9. doi:10.1016/0006-2952(78)90047-3. PMID 31888.
- Lin YM, Jarabak J (1978). "Isolation of two proteins with 9-ketoprostaglandin reductase and NADP-linked 15-hydroxyprostaglandin dehydrogenase activities and studies on their inhibition". Biochem. Biophys. Res. Commun. 81 (4): 1227–34. doi:10.1016/0006-291X(78)91267-6. PMID 666816.
- Wermuth B (1981). "Purification and properties of an NADPH-dependent carbonyl reductase from human brain. Relationship to prostaglandin 9-ketoreductase and xenobiotic ketone reductase". J. Biol. Chem. 256 (3): 1206–13. PMID 7005231.