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