A thermostable transketolase evolved for aliphatic aldehyde acceptors

Chem Commun (Camb). 2015 Jan 11;51(3):480-3. doi: 10.1039/c4cc08436e. Epub 2014 Nov 21.

Abstract

Directed evolution of the thermostable transketolase from Geobacillus stearothermophilus based on a pH-based colorimetric screening of smart libraries yielded several mutants with up to 16-fold higher activity for aliphatic aldehydes and high enantioselectivity (>95% ee) in the asymmetric carboligation step.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aldehydes / chemistry*
  • Binding Sites
  • Crystallography, X-Ray
  • Enzyme Stability
  • Geobacillus / enzymology
  • Models, Biological
  • Mutation
  • Stereoisomerism
  • Temperature
  • Transketolase / chemistry
  • Transketolase / genetics
  • Transketolase / metabolism*

Substances

  • Aldehydes
  • Transketolase