Directed evolution of transketolase activity on non-phosphorylated substrates.

@article{Hibbert2007DirectedEO,
  title={Directed evolution of transketolase activity on non-phosphorylated substrates.},
  author={Edward G. Hibbert and Tarik Senussi and Se{\'a}n J. Costelloe and Wenling Lei and Mark Edward Brennan Smith and John M Ward and Helen C Hailes and Paul A Dalby},
  journal={Journal of biotechnology},
  year={2007},
  volume={131 4},
  pages={
          425-32
        }
}
We have used active-site targeted directed evolution by saturation mutagenesis to improve the activity of E. coli transketolase towards non-phosphorylated substrates. Residues were selected for each set based on either structural proximity to substrate, or on phylogenetic variation. Each library was screened towards the reaction between hydroxypyruvate (HPA) and glycolaldehyde (GA) to form L-erythrulose, and the location of improved mutants related to the natural sequence entropy at each… CONTINUE READING
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