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 language||English (US)|
|Number of pages||3|
|State||Published - Feb 28 2001|
- Glutathione transferase
- Substrate reorientation
- Thiolate anion
ASJC Scopus subject areas