Sirtuin chemical mechanisms

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• 作者：Anthony A. Sauve
• 关键词：Sirtuin ; AADPR ; Protein deacetylation ; Enzyme mechanism ; NAD
• 刊名：Biochimica et Biophysica Acta - Proteins and Proteomics
• 出版年：2010
• 出版时间：August 2010
• 年：2010
• 卷：1804
• 期：8
• 页码：1591-1603
• 全文大小：1041 K

文摘

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.