glutathione

Glutathione A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.

[1. A tripeptide of glycine, l-cysteine, and l-glutamate, with l-glutamate having an isopeptide bond with the amino moiety of l-cysteine. Glutathione has a wide variety of roles in a cell; it is the most prevalent non-protein thiol. Glutathione disulfide (GSSG) consists of two glutathiones linked through a disulfide bridge; the term oxidized glutathione for GSSG should be avoided because it includes the sulfones and sulfoxides. (The term reduced glutathione is not necessary because glutathione is the thiol form.) A deficiency of glutathione can cause hemolysis with oxidative stress. It is also used in the course of intermediary metabolism as a donor of thiol (SH) groups and is essential for detoxification of acetaminophen.