Interpreting the broad substrate specificities of glutathione S-transferases

Citation
T. Tchaikovskaya et al., Interpreting the broad substrate specificities of glutathione S-transferases, CHEM-BIO IN, 133(1-3), 2001, pp. 170-172
Citations number
9
Categorie Soggetti
Pharmacology & Toxicology
Journal title
CHEMICO-BIOLOGICAL INTERACTIONS
ISSN journal
00092797 → ACNP
Volume
133
Issue
1-3
Year of publication
2001
Pages
170 - 172
Database
ISI
SICI code
0009-2797(20010228)133:1-3<170:ITBSSO>2.0.ZU;2-G
Abstract
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 s. (C) 2001 Elsevier Science Ireland Ltd. All rights reserved.