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Transketolase enzyme discovery and engineering.

Alessia Tonoli1, Paul Anthony Dalby1, Helen Claire Hailes2

  • 1Department of Biochemical Engineering, University College London, London, United Kingdom.

Methods in Enzymology
|November 7, 2025
PubMed
Summary
This summary is machine-generated.

Transketolases (TKs) are enzymes crucial for C-C bond formation. New TK variants with altered substrate specificities and enhanced stability are being discovered and engineered for biocatalysis.

Keywords:
BioinformaticsEnzyme discoveryEnzyme evolutionMetagenomicsTransketolase

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Area of Science:

  • Biochemistry
  • Enzymology
  • Metabolic Engineering

Background:

  • Transketolases (TKs) are key C-C bond forming enzymes utilizing specific phosphorylated sugars.
  • Biocatalytic applications often employ beta-hydroxypyruvic acid as a donor substrate.
  • There is a growing demand for novel TKs with unique properties and expanded substrate scopes.

Purpose of the Study:

  • To provide an overview of TK substrates.
  • To detail metagenomic strategies for discovering novel TKs, including 'split'-TKs.
  • To describe enzyme evolution methods for engineering TKs with improved stability and substrate acceptance.

Main Methods:

  • Metagenomic screening for novel transketolase discovery.
  • Enzyme mutagenesis and directed evolution techniques.
  • Characterization of substrate acceptance and enzyme stability.

Main Results:

  • Identification of unique transketolases through metagenomic approaches.
  • Engineering of TKs with altered substrate profiles via mutagenesis.
  • Development of TK variants with enhanced stability for biocatalysis.

Conclusions:

  • Metagenomics and enzyme evolution are powerful tools for discovering and engineering transketolases.
  • Engineered TKs offer expanded substrate ranges and improved stability for biocatalytic applications.
  • Further research will continue to expand the utility of TKs in synthetic biology and biotechnology.