The structural roles of a conserved small hydrophobic core in the active site and an ionic bridge in domain I of Delta class glutathione S-transferase.

@article{Vararattanavech2006TheSR,
  title={The structural roles of a conserved small hydrophobic core in the active site and an ionic bridge in domain I of Delta class glutathione S-transferase.},
  author={Ardcharaporn Vararattanavech and Peerada Prommeenate and Albert J Ketterman},
  journal={The Biochemical journal},
  year={2006},
  volume={393 Pt 1},
  pages={89-95}
}
GSTs (glutathione S-transferases; E.C.2.5.1.18) are a supergene family of dimeric multifunctional enzymes that have a major role in detoxification pathways. Using a GST from the mosquito Anopheles dirus (adGSTD4-4), we have characterized the enzymatic and physical properties of Leu-6, Thr-31, Leu-33, Ala-35, Glu-37, Lys-40 and Glu-42. These residues generate two motifs located in the N-terminal domain (domain I) that are functionally conserved across GST classes. The aim of this study was to… CONTINUE READING

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