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Title
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Structure of porcine aldehyde reductase holoenzyme.
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Authors
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O.el-Kabbani,
K.Judge,
S.L.Ginell,
D.A.Myles,
L.J.DeLucas,
T.G.Flynn.
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Ref.
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Nat Struct Biol, 1995,
2,
687-692.
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PubMed id
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Abstract
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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 A resolution. 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 barrel. Unlike aldose reductase, the N epsilon 2 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.
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