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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 is the most common agent taken by mouth to whiten the skin. [10] It can be used as a cream. [10] It is an antioxidant normally made by the body. [10] Whether or not it actually works is unclear as of 2019. [11] Due to side effects that may result from intravenous use, the government of the Philippines recommends against such use. [12]
The attack of the glutathione would leave a charged O – and the aldehyde hydrogen bound to C 1. If the carbonyl oxygen of C 2 can secure a hydrogen from an obliging acidic sidechain of the enzyme, forming an alcohol, then the hydrogen of C 1 might simultaneously slide over with its electrons onto C 2 (the hydride transfer).
Glutathione peroxidase 1 is the most abundant and is a very efficient scavenger of hydrogen peroxide, while glutathione peroxidase 4 is most active with lipid hydroperoxides. Surprisingly, glutathione peroxidase 1 is dispensable, as mice lacking this enzyme have normal lifespans, [123] but they are hypersensitive to induced oxidative stress. [124]
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 +.
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]
The antioxidant enzyme glutathione peroxidase 4 (GPX4) belongs to the family of glutathione peroxidases, which consists of 8 known mammalian isoenzymes (GPX1–8).GPX4 catalyzes the reduction of hydrogen peroxide, organic hydroperoxides, and lipid peroxides at the expense of reduced glutathione and functions in the protection of cells against oxidative stress.
Gamma-glutamyltransferase (also γ-glutamyltransferase, GGT, gamma-GT, gamma-glutamyl transpeptidase; [1] EC 2.3.2.2) is a transferase (a type of enzyme) that catalyzes the transfer of gamma-glutamyl functional groups from molecules such as glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate).
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