Glutathione S Alkyltransferase, also known as GST, is an enzyme found in the body that plays a crucial role in the detoxification process. Specifically, it is involved in the conjugation of glutathione with various electrophilic compounds, thereby facilitating their removal from the body.
Glutathione, a tripeptide molecule (composed of three amino acids: cysteine, glycine, and glutamic acid), is a major intracellular antioxidant that helps protect cells from oxidative damage. GSTs enhance the activity of glutathione by catalyzing the transfer of the tripeptide to toxic substances that have entered the body through metabolism, environmental exposure, or drug intake.
The primary function of GSTs is to increase the solubility of these harmful compounds, making it easier for the body to eliminate them. By binding to the toxic substances and glutathione, GSTs transform them into more water-soluble molecules that can be excreted via urine or bile. This process is crucial in reducing the potential damage caused by DNA-damaging agents, carcinogens, and other harmful chemicals.
There are several isoforms of GSTs, including Alpha, Mu, Pi, and Theta, each with different tissue distributions and substrate specificities. Therefore, GSTs have diverse roles in detoxifying endogenous and exogenous compounds, including drugs, environmental pollutants, and reactive oxygen species.
Overall, GSTs are essential enzymes in the body's defense against oxidative stress and toxic insults, playing a vital role in maintaining cellular integrity and protecting against various diseases, including cancer, neurological disorders, and liver diseases.
