Glutathione Synthetase (GSS) Reagents

Glutathione synthetase

Catalyzes the production of glutathione from gamma-glutamylcysteine and glycine in an ATP-dependent manner. Glutathione (gamma-glutamylcysteinylglycine, GSH) is the most abundant intracellular thiol in living aerobic cells and is required for numerous processes including the protection of cells against oxidative damage, amino acid transport, the detoxification of foreign compounds, the maintenance of protein sulfhydryl groups in a reduced state and acts as a cofactor for a number of enzymes.

Glutathione synthetase deficiency (GSS deficiency); Glutathione synthetase deficiency of erythrocytes (GLUSYNDE)

Eukaryotic GSH synthase family

epididymis secretory sperm binding protein Li 64p; epididymis secretory sperm binding protein Li 88n; Glutathione synthase; Glutathione synthetase; GSH S; GSH synthetase; GSH-S; GSHB_HUMAN; GSHS; GSS; HEL-S-64p; HEL-S-88n; MGC14098; OTTHUMP00000030711

Glutathione is important for a variety of biological functions, including protection of cells from oxidative damage by free radicals, detoxification of xenobiotics, and membrane transport. The protein encoded by this gene functions as a homodimer to catalyze the second step of glutathione biosynthesis, which is the ATP-dependent conversion of gamma-L-glutamyl-L-cysteine to glutathione. Defects in this gene are a cause of glutathione synthetase deficiency.