Aldehyde reductase, a member of the aldo-keto reductase superfamily, c
atalyzes the NADPH-dependent reduction of a variety of aldehydes to th
eir corresponding alcohols. The structure of porcine aldehyde reductas
e-NADPH binary complex has been determined by X-ray diffraction method
s and refined to a crystallographic R-factor of 0.20 at 2.4 Angstrom r
esolution. The tertiary structure of aldehyde reductase is similar to
that of aldose reductase and consists of an alpha/beta-barrel with the
active site located at the carboxy terminus of the strands of the bar
rel, Unlike aldose reductase, the N epsilon 2 of the imidazole ring of
His 113 in aldehyde reductase interacts, through a hydrogen bond, wit
h the amide group of the nicotinamide ring of NADPH.