Cloning, sequencing, crystallization and X-ray structure of glutathione S-transferase-III from Zea mays var. mutin: a leading enzyme in detoxification of maize herbicides.

@article{Neuefeind1997CloningSC,
  title={Cloning, sequencing, crystallization and X-ray structure of glutathione S-transferase-III from Zea mays var. mutin: a leading enzyme in detoxification of maize herbicides.},
  author={Torsten Neuefeind and Robert Huber and Peter Reinemer and J{\"o}rg Kn{\"a}blein and L Prade and Karlheinz Mann and Bastian Bieseler},
  journal={Journal of molecular biology},
  year={1997},
  volume={274 4},
  pages={577-87}
}
Glutathione S-transferases (GSTs) are enzymes that inactivate toxic compounds by conjugation with glutathione and are involved in resistance towards drugs, antibiotics, insecticides and herbicides. Their ability to confer herbicide tolerance in plants provides a tool to control weeds in a wide variety of agronomic crops. GST-III was prepared from Zea mays var. mutin and its amino acid sequence was determined from two sets of peptides obtained by cleavage with endoprotease Asp-N and with trypsin… CONTINUE READING