| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1178867 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2010 | 13 Pages |
Abstract
Sirtuins are ancient proteins widely distributed in all lifeforms of earth. These proteins are universally able to bind NAD+, and activate it to effect ADP-ribosylation of cellular nucleophiles. The most commonly observed sirtuin reaction is the ADP-ribosylation of acetyllysine, which leads to NAD+-dependent deacetylation. Other types of ADP-ribosylation have also been observed, including protein ADP-ribosylation, NAD+ solvolysis and ADP-ribosyltransfer to 5,6-dimethylbenzimidazole, a reaction involved in eubacterial cobalamin biosynthesis. This review broadly surveys the chemistries and chemical mechanisms of these enzymes.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Anthony A. Sauve,