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

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

Full Text: HTML

Citation Number: 22

Abstract

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 ...

Related Articles:

A concise route for the preparation of nucleobase-simplified cADPR mimics by click chemistry

[Li, Lingjun; Lin, Baichuan; Yang, Zhenjun; Zhang, Liangren; Zhang, Lihe Tetrahedron Letters, 2008 , vol. 49, # 29-30 p. 4491 - 4493]

Nd-Aldopentofuranosyl-N′-[p-(isoamyloxy) phenyl]-thiourea derivatives: potential anti-TB therapeutic agents

[Liav, Avraham; Angala, Shiva K.; Brennan, Patrick J.; Jackson, Mary Bioorganic and Medicinal Chemistry Letters, 2008 , vol. 18, # 8 p. 2649 - 2651]

Effect of acyl chain length on selective biocatalytic deacylation on O-aryl glycosides and separation of anomers

[Aggarwal, Neha; Arya, Anu; Mathur, Divya; Singh, Sukhdev; Tyagi, Abhilash; Kumar, Rajesh; Rana, Neha; Singh, Rajendra; Prasad, Ashok K. Bioorganic Chemistry, 2014 , vol. 53, p. 83 - 91]

More Articles...