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Microbial aldo-keto reductases.

Elizabeth M Ellis1

  • 1Departments of Bioscience and Pharmaceutical Sciences, University of Strathclyde, 204 George Street, G1 1XW, Glasgow, UK. elizabeth.ellis@strath.ac.uk

FEMS Microbiology Letters
|November 19, 2002
PubMed
Summary
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Aldo-keto reductases (AKR) are enzymes in microbes with diverse functions. Researchers are identifying new AKR enzymes and their roles in metabolism and biotransformation.

Area of Science:

  • Biochemistry
  • Enzymology
  • Microbiology

Background:

  • The aldo-keto reductase (AKR) superfamily comprises enzymes crucial for reducing aldehydes and ketones.
  • Microbial genomes reveal numerous open reading frames encoding putative AKR enzymes, expanding the known diversity.
  • Established microbial AKRs include xylose reductases, 2,5-diketo-D-gluconic acid reductases, and beta-keto ester reductases.

Purpose of the Study:

  • To explore the diverse functions and roles of microbial aldo-keto reductases (AKR).
  • To investigate the potential of novel microbial AKR enzymes in biotransformation processes.

Main Methods:

  • Genome sequencing projects to identify putative AKR enzymes.
  • Gene disruption, heterologous expression systems, and expression profiling to deduce enzyme functions.

Related Experiment Videos

  • Structural and mechanistic analysis of the conserved (alpha/beta)(8) fold and catalytic mechanisms.

    • Main Results:

    • Microbial AKR enzymes share a common (alpha/beta)(8) structure and catalytic mechanism, with variations in substrate-binding pockets.
    • The physiological roles of many microbial AKR enzymes remain largely unknown.
    • Several microbial AKR enzymes are currently utilized in biotransformation reactions.

    Conclusions:

    • Ongoing research using various methods aims to elucidate the metabolic roles of microbial AKR enzymes.
    • Significant potential exists for the discovery, study, and application of novel microbial AKR enzymes in biotechnology.