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Glutathione (GSH, / ˌ ɡ l uː t ə ˈ θ aɪ oʊ n /) is an organic compound with the chemical formula HOCOCH(NH 2)CH 2 CH 2 CONHCH(CH 2 SH)CONHCH 2 COOH. It is an antioxidant in plants , animals , fungi , and some bacteria and archaea .
Other names in common use include glutathione synthetase, and GSH synthetase. This enzyme participates in glutamate metabolism and glutathione metabolism . At least one compound, Phosphinate is known to inhibit this enzyme .
Glutathione reductase (GR) also known as glutathione-disulfide reductase (GSR) is an enzyme that in humans is encoded by the GSR gene.Glutathione reductase (EC 1.8.1.7) catalyzes the reduction of glutathione disulfide to the sulfhydryl form glutathione (), which is a critical molecule in resisting oxidative stress and maintaining the reducing environment of the cell.
Glutathione disulfide (GSSG) is a disulfide derived from two glutathione molecules. [1]In living cells, glutathione disulfide is reduced into two molecules of glutathione with reducing equivalents from the coenzyme NADPH.
A second GSH molecule reduces the GS-SeR intermediate back to the selenol, releasing GS-SG as the by-product. A simplified representation is shown below: [5] RSeH + H 2 O 2 → RSeOH + H 2 O RSeOH + GSH → GS-SeR + H 2 O GS-SeR + GSH → GS-SG + RSeH. Glutathione reductase then reduces the oxidized glutathione to complete the cycle:
Buthionine sulfoximine (BSO) is a sulfoximine derivative which reduces levels of glutathione and is being investigated as an adjunct with chemotherapy in the treatment of cancer. [1]
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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.