Glutathione (GSH) is an antioxidant found in every cell of almost all organisms. GSH is essential for mammalian cell survival, and since it is not taken up, it is important to understand how it is synthesized. Glutathione synthetase (GS) catalyzes the second and final step in the ATP-dependent formation of GSH from ?-glutamylcysteine and glycine. Human GS (hGS) is a homodimer that displays negative cooperativity toward the ?-glutamylcysteine substrate. Learning more about how ?-glutamylcysteine interacts with hGS will provide insight into negative cooperativity, a phenomenon which contributes to metabolic regulation but is not yet fully understood, and will increase our knowledge of GSH biosynthesis. The H-loop of hGS is located near the binding site of ?-glutamylcysteine, and the focus of this research is study its role in negative cooperativity and activity.Supported in part by NIH R15GM086833 (MEA), a REP Grant (TWU, MEA), and a UNT Faculty Research Grant (TRC).

Role of H-loop residues in human glutathione synthetase activity

247th National Meeting (2014)

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