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Catalytic mechanism and substrate selectivity of aldo-keto reductases: insights from structure-function studies of Candida tenuis xylose reductase.
IUBMB Life. 2006 Sep; 58(9):499-507.IL

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.

Authors+Show Affiliations

Institute of Biotechnology and Biochemical Engineering, and Research Centre Applied Biocatalysis, Graz University of Technology, Graz, Austria.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

17002977

Citation

Kratzer, Regina, et al. "Catalytic Mechanism and Substrate Selectivity of Aldo-keto Reductases: Insights From Structure-function Studies of Candida Tenuis Xylose Reductase." IUBMB Life, vol. 58, no. 9, 2006, pp. 499-507.
Kratzer R, Wilson DK, Nidetzky B. Catalytic mechanism and substrate selectivity of aldo-keto reductases: insights from structure-function studies of Candida tenuis xylose reductase. IUBMB Life. 2006;58(9):499-507.
Kratzer, R., Wilson, D. K., & Nidetzky, B. (2006). Catalytic mechanism and substrate selectivity of aldo-keto reductases: insights from structure-function studies of Candida tenuis xylose reductase. IUBMB Life, 58(9), 499-507.
Kratzer R, Wilson DK, Nidetzky B. Catalytic Mechanism and Substrate Selectivity of Aldo-keto Reductases: Insights From Structure-function Studies of Candida Tenuis Xylose Reductase. IUBMB Life. 2006;58(9):499-507. PubMed PMID: 17002977.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Catalytic mechanism and substrate selectivity of aldo-keto reductases: insights from structure-function studies of Candida tenuis xylose reductase. AU - Kratzer,Regina, AU - Wilson,David K, AU - Nidetzky,Bernd, PY - 2006/9/28/pubmed PY - 2007/1/4/medline PY - 2006/9/28/entrez SP - 499 EP - 507 JF - IUBMB life JO - IUBMB Life VL - 58 IS - 9 N2 - 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. SN - 1521-6543 UR - https://www.unboundmedicine.com/medline/citation/17002977/Catalytic_mechanism_and_substrate_selectivity_of_aldo_keto_reductases:_insights_from_structure_function_studies_of_Candida_tenuis_xylose_reductase_ L2 - https://doi.org/10.1080/15216540600818143 DB - PRIME DP - Unbound Medicine ER -