Laboratory evolution of toluene dioxygenase to accept 4-picoline as a substrate.

@article{Sakamoto2001LaboratoryEO,
  title={Laboratory evolution of toluene dioxygenase to accept 4-picoline as a substrate.},
  author={Tomoko Sakamoto and John M. Joern and Akira Arisawa and Frances H. Arnold},
  journal={Applied and environmental microbiology},
  year={2001},
  volume={67 9},
  pages={3882-7}
}
We are using directed evolution to extend the range of dioxygenase-catalyzed biotransformations to include substrates that are either poorly accepted or not accepted at all by the naturally occurring enzymes. Here we report on the oxidation of a heterocyclic substrate, 4-picoline, by toluene dioxygenase (TDO) and improvement of the enzyme's activity by laboratory evolution. The biotransformation of 4-picoline proceeds at only approximately 4.5% of the rate of the natural reaction on toluene… CONTINUE READING

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