Sandbox Reserved 771: Difference between revisions
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'''Glutathione synthetase''' (GSS) is an homo-dimeric, ATP-depending <scene name='56/564047/Biological_assembly/2'>ligase</scene> responsible for the condensation of γ-Glutamylcysteine and glycine to form Glutathione during the second step of the glutathione biosynthesis pathway. Glutathione considered to be one of the most abundant and important antioxidants present in mammalian cells. In addition to protecting cells from the oxidative damage caused by free radicals, it is believed to be involved in the detoxification of xenobiotics, as well as membrane transport | '''Glutathione synthetase''' (GSS) is an homo-dimeric, ATP-depending <scene name='56/564047/Biological_assembly/2'>ligase</scene> responsible for the condensation of γ-Glutamylcysteine and glycine to form Glutathione (GSH) during the second step of the glutathione biosynthesis pathway. Glutathione considered to be one of the most abundant and important antioxidants present in a wide range of cells - including bacterial, plant, and mammalian cells. In addition to protecting cells from the oxidative damage caused by free radicals, it is believed to be involved in the detoxification of xenobiotics, as well as membrane transport. | ||
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Glutathione Synthetase is the key enzyme involved in the ATP-dependent condensation of γ-Glutamylcysteine and glycine to form Glutathione during the second step of the glutathione biosynthesis pathway. The ATP-dependence of the catalysis qualifies GSS for inclusion into the ligase enzyme | Glutathione Synthetase is the key enzyme involved in the ATP-dependent condensation of γ-Glutamylcysteine and glycine to form Glutathione during the second step of the glutathione biosynthesis pathway. The condensation begins by binding of ATP to GSS in the presence of γ-Glutamylcysteine, to form an enzyme-bound acyl-phosphate that binds glycine and generates the enzyme-product complex. Dissociation of GSS from the E::P complex results in release of GSH, ADP, and inorganic phosphate (Pi). The ATP-dependence of the catalysis qualifies GSS for inclusion into the ligase enzyme superfamily. Further, a Hill constant of ~0.67 indicates that GSS exhibits negative cooperativity towards the substrate γ-Glutamylcysteine. | ||