Evidence for an essential serine residue in the active site of the Theta class glutathione transferases.

@article{Board1995EvidenceFA,
  title={Evidence for an essential serine residue in the active site of the Theta class glutathione transferases.},
  author={Philip G Board and Marjorie Coggan and Matthew C. J. Wilce and Michael W Parker},
  journal={The Biochemical journal},
  year={1995},
  volume={311 ( Pt 1)},
  pages={247-50}
}
A consistent feature of the Alpha-, Mu- and Pi-class glutathione transferases (GSTs) is the presence near the N-terminus of a tyrosine residue that contributes to the activation of glutathione. While this residue appears to be conserved in many Theta-class GSTs, its absence in some suggested that the Theta-class GSTs may have a significantly different structure or catalytic mechanism. The elucidation of the crystal structure of the Theta-class GST from the Australian sheep blowfly, Lucilia… CONTINUE READING

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