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11-Feb-2016 02:49

Glutathione reduces disulfide bonds formed within cytoplasmic proteins to cysteines by serving as an electron donor.In the process, glutathione is converted to its oxidized form, glutathione disulfide (GSSG), also called The biosynthesis pathway for glutathione is found in some bacteria, such as cyanobacteria and proteobacteria, but is missing in many other bacteria.

Next, Cys63 nucleophilically attacks the sulfide of Cys58, releasing a GS-anion, which, in turn, picks up a solvent proton and is released from the enzyme, thereby creating the second GSH.

The midpoint potential of the critical cysteine pair is -318 m V.

In addition to the redox-dependent control, the plant GCL enzyme is feedback inhibited by glutathione.) to other molecules, such as reactive oxygen species to neutralize them, or to protein cysteines to maintain their reduced forms.

Most eukaryotes, including humans, synthesize glutathione, but some do not, such as Leguminosae, Entamoeba, and Giardia.

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The only archaea that make glutathione are halobacteria.-glutamic acid, and glycine; it does not have to be present as a supplement in the diet.

Glutathione (GSH) is an important antioxidant in plants, animals, fungi, and some bacteria and archaea.



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