Interpreting the broad substrate specificities of glutathione S-transferases

Tatyana Tchaikovskaya, Yury V. Patskovsky, Alexander Federov, Steven C. Almo, Mark Girvin, Irving Listowsky

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Abstract

Catalytic mechanisms of glutathione S-transferases (GSTs) were viewed in terms of the independent steps of GSH binding and activation and the productive reorientation of the electrophilic substituent of the second substrate. NMR and isothermal titration microcalorimetric methods were used to study GST-ligand interactions. The family of five human Mu-class GSTs was employed as a paradigm to study structure, catalysis and subunit assembly mechanisms.

Original languageEnglish (US)
Pages (from-to)170-172
Number of pages3
JournalChemico-Biological Interactions
Volume133
Issue number1-3
Publication statusPublished - Feb 28 2001

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Keywords

  • Catalysis
  • Glutathione transferase
  • Substrate reorientation
  • Thiolate anion

ASJC Scopus subject areas

  • Toxicology

Cite this

Tchaikovskaya, T., Patskovsky, Y. V., Federov, A., Almo, S. C., Girvin, M., & Listowsky, I. (2001). Interpreting the broad substrate specificities of glutathione S-transferases. Chemico-Biological Interactions, 133(1-3), 170-172.