Journal of the American Chemical Society

Transition state of ADP-ribosylation of acetyllysine catalyzed by Archaeoglobus fulgidus Sir2 determined by kinetic isotope effects and computational approaches

Y Cen, AA Sauve

文献索引：Cen, Yana; Sauve, Anthony A. Journal of the American Chemical Society, 2010 , vol. 132, # 35 p. 12286 - 12298

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被引用次数: 22

摘要

Sirtuins are protein-modifying enzymes distributed throughout all forms of life. These enzymes bind NAD+, a universal metabolite, and react it with acetyllysine residues to effect deacetylation of protein side chains. This NAD+-dependent deacetylation reaction has been observed for sirtuin enzymes derived from archaeal, eubacterial, yeast, metazoan, and mammalian species, suggesting conserved chemical mechanisms for these enzymes. The ...