Catalytic mechanism and role of hydroxyl residues in the active site of theta class glutathione S-transferases. Investigation of Ser-9 and Tyr-113 in a glutathione S-transferase from the Australian sheep blowfly, Lucilia cuprina.

@article{Caccuri1997CatalyticMA,
  title={Catalytic mechanism and role of hydroxyl residues in the active site of theta class glutathione S-transferases. Investigation of Ser-9 and Tyr-113 in a glutathione S-transferase from the Australian sheep blowfly, Lucilia cuprina.},
  author={Anna Maria Caccuri and Giovanni Antonini and Matthew Nicotra and Andrea Battistoni and Mario Lo Bello and Philip G Board and Michael W Parker and Giorgio Ricci},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 47},
  pages={29681-6}
}
Spectroscopic and kinetic studies have been performed on the Australian sheep blowfly Lucilia cuprina glutathione S-transferase (Lucilia GST; EC 2.5.1.18) to clarify its catalytic mechanism. Steady state kinetics of Lucilia GST are non-Michaelian, but the quite hyperbolic isothermic binding of GSH suggests that a steady state random sequential Bi Bi mechanism is consistent with the anomalous kinetics observed. The rate-limiting step of the reaction is a viscosity-dependent physical event, and… CONTINUE READING

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