Structure of porcine aldehyde reductase holoenzyme

Aldehyde reductase, a member of the aldo-keto reductase superfamily, catalyzes the NADPH-dependent reduction of a variety of aldehydes to their corresponding alcohols. The structure of porcine aldehyde reductase-NADPH binary complex has been determined by X-ray diffraction methods and refined to a crystallographic R-factor of 0.20 at 2.4 Å resolution. The tertiary structure of aldehyde reductase is similar to that of aldose reductase and consists of an a b-barrel with the active site located at the carboxy terminus of the strands of the barrel. Unlike aldose reductase, the Ne2 of the imidazole ring of His 113 in aldehyde reductase interacts, through a hydrogen bond, with the amide group of the nicotinamide ring of NADPH.