Catalytic mechanism and substrate selectivity of aldo-keto reductases: Insights from structure-function studies of Candida tenuis xylose reductase

Regina Kratzer, David K. Wilson, Bernd Nidetzky

Research output: Contribution to journalArticle

35 Scopus citations

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 ε-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.

Original languageEnglish (US)
Pages (from-to)499-507
Number of pages9
JournalIUBMB Life
Volume58
Issue number9
DOIs
StatePublished - Sep 1 2006

Keywords

  • Aldo-keto reductase
  • Bioreduction
  • Catalytic mechanism
  • Substrate selectivity
  • Xylose reductase
  • Xylose utilization

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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