GSTA

GSTA commonly refers to the glutathione S-transferase A class, a group of cytosolic enzymes in the glutathione S-transferase (GST) superfamily. The alpha class includes several enzymes that participate in the detoxification of a wide array of electrophilic compounds by catalyzing the conjugation of reduced glutathione to these substrates. This activity helps neutralize drugs, environmental chemicals, and products of oxidative stress, facilitating their elimination from the body. Some members of the GSTA family also contribute to the metabolism of endogenous molecules and, in certain cases, other enzymatic activities.

In humans, the alpha class comprises multiple enzymes, including GSTA1, GSTA2, GSTA3, GSTA4, and GSTA5. They are expressed in various tissues, with notable abundance in the liver. Structurally, GSTA enzymes generally function as homodimers or heterodimers and possess distinct substrate specificities. The active site architecture includes a G-site that binds glutathione and an H-site that accommodates the electrophilic substrate, enabling efficient catalysis of conjugation reactions.

Genetic variation within GSTA genes can influence enzyme expression and activity, affecting an individual’s capacity to detoxify certain chemicals. Polymorphisms and differential regulation of GSTA expression have been investigated in relation to cancer susceptibility, drug response, and susceptibility to organ toxicity. Beyond detoxification, GSTAs are studied for their roles in pharmacology, toxicology, and biomarker research related to environmental exposures. While GSTA is most commonly used to denote the glutathione S-transferase A class, the broader GST superfamily includes additional classes with related but distinct functions.