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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 .
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 synthetase deficiency has an autosomal recessive pattern of inheritance. Mutations in the GSS gene cause glutathione synthetase deficiency. This gene provides instructions for making the enzyme glutathione synthetase. This enzyme is involved in a process called the gamma-glutamyl cycle, which takes place in most of the body's cells ...
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]
100042625 Ensembl ENSG00000084207 n/a UniProt P09211 n/a RefSeq (mRNA) NM_000852 XM_036155425 RefSeq (protein) NP_000843 n/a Location (UCSC) Chr 11: 67.58 – 67.59 Mb n/a PubMed search Wikidata View/Edit Human View/Edit Mouse Glutathione S-transferase P is an enzyme that in humans is encoded by the GSTP1 gene. Function Glutathione S-transferases (GSTs) are a family of enzymes that play an ...
Glutathione peroxidase (GPx) (EC 1.11.1.9) is the general name of an enzyme family with peroxidase activity whose main biological role is to protect the organism from oxidative damage. [2] The biochemical function of glutathione peroxidase is to reduce lipid hydroperoxides to their corresponding alcohols and to reduce free hydrogen peroxide to ...
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