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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-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
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What is glutathione gamma-glutamylcysteinyltransferase?
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What is glutathione S-transferase P?
In enzymology, a glutathione gamma-glutamylcysteinyltransferase ( EC 2.3.2.15) is an enzyme that catalyzes the chemical reaction. glutathione + [Glu (-Cys)]n-Gly. Gly + [Glu (-Cys)]n + 1-Gly. Thus, the two substrates of this enzyme are glutathione and [Glu (-Cys)]n-Gly, whereas its two products are Gly and [Glu (-Cys)]n+1-Gly.
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. Glutathione synthetase is also a potent antioxidant. It is
The glutathione S-transferase pi gene (GSTP1) is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are thought to function in xenobiotic metabolism and play a role in susceptibility to cancer, and other diseases.
Glutathione hydrolase (EC 3.4.19.13, glutathionase, GGT, gamma-glutamyltranspeptidase) is an enzyme. This enzyme catalyses the following chemical reaction glutathione + H 2 O L-cysteinylglycine + L-glutamate This protein also acts as enzyme EC 2.3.2.2
Bacterial glutathione transferases (GSTs; EC 2.5.1.18) are part of a superfamily of enzymes that play a crucial role in cellular detoxification. [2] . The primary role of GSTs is to catalyze the conjugation of glutathione (GSH) with the electrophilic centers of a wide variety of molecules.
