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. PMID31888.
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. PMID666816.