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Author(s): Kratzer R; Wilson DK; Nidetzky B
Title: Catalytic mechanism and substrate selectivity of aldo-keto reductases: Insights from structure-function studies of Candida tenuis xylose reductase
Source: IUBMB LIFE 58 (9): 499-507
Date: 2006 SEP
Document Type: Journal : Review
DOI:
Language: English
Comment:
Address: Graz Univ Technol, Inst Biotechnol & Biochem Engn, A-8010 Graz, Austria.
Graz Univ Technol, Res Ctr Appl Biocatalysis, A-8010 Graz, Austria. Univ Calif Davis, Sect Mol & Cellular Biol, Davis, CA 95616 USA. Reprint: Nidetzky, B, Graz Univ Technol, Inst Biotechnol & Biochem Engn,
Petersgasse 12, A-8010 Graz, Austria. E-mail: bernd.nidetzky@tugraz.at
Abstract: 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-NH3+ 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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