Carbonyl reductase (NADPH)

In enzymology, a carbonyl reductase (NADPH) () 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 , , , and .

References