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Glutathione is capable of preventing damage to important cellular components caused by sources such as reactive oxygen species, free radicals, peroxides, lipid peroxides, and heavy metals. [2] It is a tripeptide with a gamma peptide linkage between the carboxyl group of the glutamate side chain and cysteine.
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Dehydroascorbic acid (DHA) is an oxidized form of ascorbic acid (vitamin C). It is actively imported into the endoplasmic reticulum of cells via glucose transporters. [1] It is trapped therein by reduction back to ascorbic acid by glutathione and other thiols. [2]
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]
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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]