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Glutathione ( GSH, / ˌɡluːtəˈθaɪoʊn /) is an organic compound with the chemical formula HOCOCH (NH2)CH2CH2CONHCH (CH2SH)CONHCH2COOH. It is an antioxidant in plants, animals, fungi, and some bacteria and archaea.
Glutathione S-transferase A1 is an enzyme that in humans is encoded by the GSTA1 gene. Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families.
Glutamate–cysteine ligase (GCL) EC 6.3.2.2), previously known as γ-glutamylcysteine synthetase (GCS), is the first enzyme of the cellular glutathione (GSH) biosynthetic pathway that catalyzes the chemical reaction:
Glutathione reductase (EC 1.8.1.7) catalyzes the reduction of glutathione disulfide ( GSSG) to the sulfhydryl form glutathione ( GSH ), which is a critical molecule in resisting oxidative stress and maintaining the reducing environment of the cell.
Glutathione synthetase (GSS) (EC 6.3.2.3) is the second enzyme in the glutathione (GSH) biosynthesis pathway. It catalyses the condensation of gamma-glutamylcysteine and glycine, to form glutathione.[2] Glutathione synthetase is also a potent antioxidant. It is found in many species including bacteria, yeast, mammals, and plants.[3] In humans ...
Glutathione S-transferases ( GSTs ), previously known as ligandins, are a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification. The GST family consists of three superfamilies ...
Glutathione disulfide (GSSG) is a disulfide derived from two glutathione molecules. In living cells, glutathione disulfide is reduced into two molecules of glutathione with reducing equivalents from the coenzyme NADPH. This reaction is catalyzed by the enzyme .
