Journal
IUBMB LIFE
Volume 58, Issue 9, Pages 499-507Publisher
WILEY-BLACKWELL
DOI: 10.1080/15216540600818143
Keywords
aldo-keto reductase; xylose reductase; catalytic mechanism; substrate selectivity; bioreduction; xylose utilization
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Aldo-keto reductases (AKRs) constitute a large protein superfamily of mainly NAD(P)-dependent oxidoreductases involved in carbonyl metabolism. Catalysis is promoted by a conserved tetrad of active site residues (Tyr, Lys, Asp and His). Recent results of structure-function relationship studies for xylose reductase (AKR2B5) require an update of the proposed catalytic mechanism. Electrostatic stabilization by the epsilon-NH(3)(+) group of Lys is a key source of catalytic power of xylose reductase. A molecular-level analysis of the substrate binding pocket of xylose reductase provides a case of how a very broadly specific AKR achieves the requisite selectivity for its physiological substrate and could serve as the basis for the design of novel reductases with improved specificities for biocatalytic applications.
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