In vitro evolution of a polyhydroxybutyrate synthase by intragenic suppression-type mutagenesis.

@article{Taguchi2002InVE,
  title={In vitro evolution of a polyhydroxybutyrate synthase by intragenic suppression-type mutagenesis.},
  author={Seiichi Taguchi and Hirofumi Nakamura and Tomohiro Hiraishi and Ichiro Yamato and Yoshiharu Doi},
  journal={Journal of biochemistry},
  year={2002},
  volume={131 6},
  pages={801-6}
}
In vitro evolution was applied to obtain highly active mutants of Ralstonia eutropha polyester synthase (PhbC(Re)), which is a key enzyme catalyzing the formation of polyhydroxybutyrate (PHB) from (R)-3-hydroxybutyryl-CoA (3HB-CoA). To search for beneficial mutations for activity improvement of this enzyme, we have conducted multi-step mutations, including activity loss and intragenic suppression-type activity reversion. Among 259 revertants, triple mutant E11S12 was obtained as the most active… CONTINUE READING

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