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Structural basis for sirtuin activity and inhibition.


ABSTRACT: Sir2 proteins, or sirtuins, are a family of enzymes that catalyze NAD(+)-dependent deacetylation reactions and can also process ribosyltransferase, demalonylase, and desuccinylase activities. More than 40 crystal structures of sirtuins have been determined, alone or in various liganded forms. These high-resolution architectural details lay the foundation for understanding the molecular mechanisms of catalysis, regulation, substrate specificity, and inhibition of sirtuins. In this minireview, we summarize these structural features and discuss their implications for understanding sirtuin function.

SUBMITTER: Yuan H 

PROVIDER: S-EPMC3522243 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

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Structural basis for sirtuin activity and inhibition.

Yuan Hua H   Marmorstein Ronen R  

The Journal of biological chemistry 20121018 51


Sir2 proteins, or sirtuins, are a family of enzymes that catalyze NAD(+)-dependent deacetylation reactions and can also process ribosyltransferase, demalonylase, and desuccinylase activities. More than 40 crystal structures of sirtuins have been determined, alone or in various liganded forms. These high-resolution architectural details lay the foundation for understanding the molecular mechanisms of catalysis, regulation, substrate specificity, and inhibition of sirtuins. In this minireview, we  ...[more]

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