glutatioonStransferaase

Glutathione S-transferases (GSTs) are a family of enzymes found in virtually all living organisms. They play a crucial role in detoxification and cellular defense mechanisms. GSTs catalyze the conjugation of glutathione, a tripeptide antioxidant, to a wide range of electrophilic substrates. This conjugation, known as glutathione conjugation or S-alkylation, typically renders the substrate more water-soluble and less reactive, facilitating its excretion from the cell and organism.

These enzymes are involved in the metabolism of various endogenous and exogenous compounds, including drugs, pesticides, carcinogens, and reactive oxygen species. By detoxifying harmful substances, GSTs protect cells from oxidative stress and damage. They are also implicated in the regulation of cellular signaling pathways and in mediating resistance to certain chemotherapeutic agents.

GSTs are classified into several classes based on their structural and functional similarities, such as alpha, mu, pi, and sigma classes in mammals. The specific substrate specificity and cellular localization of different GST isoforms contribute to their diverse roles in maintaining cellular homeostasis. Genetic variations within GST genes can influence an individual's susceptibility to certain diseases and their response to environmental toxins and medications. Research into GSTs continues to explore their therapeutic potential and their involvement in various pathological conditions.