Daniel F.A.R. Dourado, Pedro Alexandrino Fernandes and Maria Joao Ramos Pages 325 - 337 ( 13 )
Glutathione Transferases (GSTs) are crucial enzymes in the cell detoxification process catalyzing the nucleophilic attack of glutathione (GSH) on toxic electrophilic substrates and producing a less dangerous compound. GSTs studies are of great importance since they have been implicated in the development of drug resistance in tumoral cells and are related to human diseases such as Parkinsons, Alzheimers, atherosclerois, liver cirrhosis, aging and cataract formation. In this review we start by providing an evolutionary perspective of the mammalian cytosolic GSTs known to date. Later on we focus on the more abundant classes alpha, mu and pi and their structure, catalysis, metabolic associated functions, drug resistance relation and inhibition methods. Finally, we introduce the recent insights on the GST class zeta from a metabolic perspective.
Glutathione S-tranferase (GST), Glutathione (GSH), Glutathione S-transferase (GST) classes alpha, mu, pi and zeta, catalysis, metabolism of endogenous compounds, tumorogenesis, inhibition methods
REQUIMTE/Departamento de Quimica, Faculdade de Ciencias, Universidade do Porto, Rua do Campo Alegre, 687, 4169-007 Porto, Portugal.