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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 is capable of preventing damage to important cellular components caused by sources such as reactive oxygen species ...
Glutathione peroxidase 1 (GPx1) is the most abundant version, found in the cytoplasm of nearly all mammalian tissues, whose preferred substrate is hydrogen peroxide. Glutathione peroxidase 4 (GPx4) has a high preference for lipid hydroperoxides; it is expressed in nearly every mammalian cell, though at much lower levels.
Infobox references. 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. This reaction is catalyzed by the enzyme glutathione reductase. [2]
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 oxidase. In enzymology, a glutathione oxidase ( EC 1.8.3.3) is an enzyme that catalyzes the chemical reaction. Thus, the two substrates of this enzyme are glutathione and O 2, whereas its two products are glutathione disulfide and H 2 O 2 . This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur ...
Oxidative folding. Oxidative protein folding is a process that is responsible for the formation of disulfide bonds between cysteine residues in proteins. The driving force behind this process is a redox reaction, in which electrons pass between several proteins and finally to a terminal electron acceptor .
Sulfur assimilation. Sulfate reduction and assimilation in plants (APS, adenosine 5'-phosphosulfate; Fdred, Fdox, reduced and oxidized ferredoxin; RSH, RSSR, reduced and oxidized glutathione; SQDG, sulfoquinovosyl diacylglycerol) Sulfur assimilation is the process by which living organisms incorporate sulfur into their biological molecules. [1]
GSNO, along with glutathione and oxidized glutathione (GSSG), have been found to bind to the glutamate recognition site of the NMDA and AMPA receptors (via their γ-glutamyl moieties), and may be endogenous neuromodulators. [18] [19] At millimolar concentrations, they may also modulate the redox state of the NMDA receptor complex. [19]