Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 A resolution: structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture.

@article{Reinemer1996ThreedimensionalSO,
  title={Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2 A resolution: structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture.},
  author={Peter Reinemer and L Prade and Peter Hof and Torsten Neuefeind and Robert Huber and R Zettl and Klaus Palme and J. L. Schell and Ingo K{\"o}lln and Hans D. Bartunik and Bastian Bieseler},
  journal={Journal of molecular biology},
  year={1996},
  volume={255 2},
  pages={289-309}
}
Glutathione S-transferases (GST) are a family of multifunctional enzymes involved in the metabolization of a broad variety of xenobiotics and reactive endogenous compounds. The interest in plant glutathione S-transferases may be attributed to their agronomic value, since it has been demonstrated that glutathione conjugation for a variety of herbicides is the major resistance and selectivity factor in plants. The three-dimensional structure of glutathione S-transferase from the plant Arabidopsis… CONTINUE READING

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