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Glutathione reductase from human erythrocytes is a homodimer consisting of 52Kd monomers, each containing 3 domains. GR exhibits single sheet, double layered topology where an anti-parallel beta-sheet is largely exposed to the solvent on one face while being covered by random coils on the other face. [10]
The reactive oxygen species then donates one electron to a glutathione molecule, completing the oxidation-reduction reaction and rendering it unable to perform oxidative damage to the cell. [5] After completion of this reaction, glutathione reductase recycles oxidized glutathione back to the reduced form so that it again can be picked up by GSTs.
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 .
The first SG − anion is released and then receives one proton from adjacent SH group and from the first glutathione monomer. Next the adjacent S − group attack disulphide bond in cysteine-SG complex and release the second SG − anion. It receives one proton in solution and forms the second glutathione monomer. [1]: 137–9
The glutathione binding site, or "G-site", is located in the thioredoxin-like domain of both cytosolic and mitochondrial GSTs. The region containing the greatest amount of variability between the assorted classes is that of helix α2 , where one of three different amino acid residues interacts with the glycine residue of glutathione.
In enzymology, a CoA-glutathione reductase (EC 1.8.1.10) is an enzyme that catalyzes the chemical reaction. CoA + glutathione + NADP + CoA-glutathione + NADPH + H +. The 3 substrates of this enzyme are CoA, glutathione, and NADP +, whereas its 3 products are CoA-glutathione, NADPH, and H +.
The glutathione system includes glutathione, glutathione reductase, glutathione peroxidases, and glutathione S-transferases. [76] This system is found in animals, plants and microorganisms. [ 76 ] [ 121 ] Glutathione peroxidase is an enzyme containing four selenium - cofactors that catalyzes the breakdown of hydrogen peroxide and organic ...
In contrast to thioredoxins, which are reduced by thioredoxin reductase, no oxidoreductase exists that specifically reduces glutaredoxins. Instead, glutaredoxins are reduced by the oxidation of glutathione. Reduced glutathione is then regenerated by glutathione reductase. Together these components compose the glutathione system. [6]
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