Evolution of differential substrate specificities in Mu class glutathione transferases probed by DNA shuffling.

@article{Hansson1999EvolutionOD,
  title={Evolution of differential substrate specificities in Mu class glutathione transferases probed by DNA shuffling.},
  author={L O Hansson and Robyn Bolton-Grob and Taieb Massoud and Bengt Mannervik},
  journal={Journal of molecular biology},
  year={1999},
  volume={287 2},
  pages={265-76}
}
A library of variant enzymes was created by combined shuffling of the DNA encoding the human Mu class glutathione transferases GST M1-1 and GST M2-2. The parental GSTs are 84 % sequence identical at the protein level, but their specific activities with the substrates aminochrome and 2-cyano-1,3-dimethyl-1-nitrosoguanidine (cyanoDMNG) differ by more than 100-fold. Aminochrome is of particular interest as an oxidation product of dopamine and of possible significance in the etiology of Parkinson's… CONTINUE READING

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