Glutathione Synthetase belongs to the eukaryotic GSH synthase family. Glutathione Synthetase is the second enzyme in the glutathione biosynthesis pathway. It catalyses the condensation of gamma-glutamylcysteine and glycine to form glutathione. Glutathione play an important role in a variety of biological functions, including detoxification of xenobiotics, protection of cells from oxidative damage by free radicals, and membrane transport. The protein functions as a homodimer to catalyze the second step of glutathione biosynthesis, which is the ATP-dependent conversion of gamma-L-glutamyl-L-cysteine to glutathione. Defects in Glutathione Synthetase can also cause the glutathione synthetase deficiency of erythrocytes, which is a mild form causing hemolytic anemia.
Glutathione S-transferase that catalyzes the nucleophilic attack of the sulfur atom of glutathione on the electrophilic groups of a wide range of exogenous and endogenous compounds (Probable). Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). Tissue specificity expressed in liver.Homodimer or heterodimer of GSTA1 and GSTA2.
GSTA1 (Glutathione S-Transferase Alpha 1) is a Protein Coding gene. This gene encodes a member of a family of enzymes that function to add glutathione to target electrophilic compounds. Glutathione S-transferases (GSTs) are involved in the detoxification of carcinogens and may be linked to carcinogenesis. As a vital component of GSTs, GSTA1 plays an important role in carcinogenesis. GSTA1 expression may be a target molecule in the early diagnosis and treatment of lung cancer. Human colonic adenocarcinoma (Caco-2) cells in culture undergo spontaneous differentiation into mature enterocytes in association with progressive increases in expression of glutathione S-transferase alpha-1 (GSTA1). GSTA1 levels may play a role in modulating enterocyte proliferation but do not influence differentiation or apoptosis. GSTA1 may play a key role during pregnancy.
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