Carbonyl reductase (NADPH)

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Ribbon diagram of human carbonyl reductase 1, in complex with NADPH and a small molecule inhibitor (not shown). From PDB 1WMA.

In enzymology, a carbonyl reductase (NADPH) (EC 1.1.1.184) is an enzyme that catalyzes the chemical reaction

R-CHOH-R' + NADP⁺ $\rightleftharpoons$ R-CO-R' + NADPH + H⁺

Thus, the two substrates of this enzyme are R-CHOH-R' and NADP⁺, whereas its 3 products 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 1.1.1.184
BRENDA references for 1.1.1.184 (Recommended.)
PubMed references for 1.1.1.184
PubMed Central references for 1.1.1.184
Google Scholar references for 1.1.1.184
Ahmed NK, Felsted RL, Bachur NR (1978). "Heterogeneity of anthracycline antibiotic carbonyl reductases in mammalian livers". Biochem. Pharmacol. 27: 2713–9. 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: 1227–34. 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: 1206–13. PMID 7005231.