Functional complementation of anthocyanin sequestration in the vacuole by widely divergent glutathione S-transferases.

@article{Alfenito1998FunctionalCO,
  title={Functional complementation of anthocyanin sequestration in the vacuole by widely divergent glutathione S-transferases.},
  author={Mark R. Alfenito and Erik Souer and Christopher Dean Goodman and Rivan Buell and JNM. Mol and Ronald Koes and Virginia Walbot},
  journal={The Plant cell},
  year={1998},
  volume={10 7},
  pages={1135-49}
}
Glutathione S-transferases (GSTs) traditionally have been studied in plants and other organisms for their ability to detoxify chemically diverse herbicides and other toxic organic compounds. Anthocyanins are among the few endogenous substrates of plant GSTs that have been identified. The Bronze2 (Bz2) gene encodes a type III GST and performs the last genetically defined step of the maize anthocyanin pigment pathway. This step is the conjugation of glutathione to cyanidin 3-glucoside (C3G… CONTINUE READING
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