The role of the glycine triad in human glutathione synthetase
► G-loop glycine triad mutations greatly reduce the activity of human glutathione synthetase. ► Mutations to glycine triad residues decrease ligand binding and prevent active site closure. ► G-loop glycines Gly369 and Gly370 have essential roles in hGS, while Gly371 has lesser involvement. Experimen...
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Veröffentlicht in: | Biochemical and biophysical research communications 2010-10, Vol.400 (4), p.511-516 |
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Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | ► G-loop glycine triad mutations greatly reduce the activity of human glutathione synthetase. ► Mutations to glycine triad residues decrease ligand binding and prevent active site closure. ► G-loop glycines Gly369 and Gly370 have essential roles in hGS, while Gly371 has lesser involvement.
Experimental kinetics and computational modeling of human glutathione synthetase (hGS) support the significant role of the G-loop glycine triad (G369, G370, G371) for activity of this ATP-grasp enzyme. Enzyme kinetic experiments indicate that G369V and G370V mutant hGS have little activity ( |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/j.bbrc.2010.08.081 |