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Research article summary (published 30 Dec 2005):

The biochemistry of sirtuins.

Full Abstract

Sirtuins are a family of NAD+-dependent protein deacetylases widely distributed in all phyla of life. Accumulating evidence indicates that sirtuins are important regulators of organism life span. In yeast, these unique enzymes regulate gene silencing by histone deacetylation and via formation of the novel compound 2'-O-acetyl-ADP-ribose. In multicellular organisms, sirtuins deacetylate histones and transcription factors that regulate stress, metabolism, and survival pathways. The chemical mechanism of sirtuins provides novel opportunities for signaling and metabolic regulation of protein deacetylation. The biological, chemical, and structural characteristics of these unusual enzymes are discussed in this review.

 

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Author information

Author/s: Sauve, Anthony A (AA); Wolberger, Cynthia (C); Schramm, Vern L (VL); Boeke, Jef D (JD);

Affiliation: Department of Pharmacology, Weill Medical College of Cornell University, New York, New York 10021, USA. aas2004(-atsign-)med.cornell.edu

Journal and publication information

Publication Type: Journal Article; Research Support, N.I.H., Extramural; Review

Journal: Annual review of biochemistry (Annu Rev Biochem), published in United States. (Language: eng)

Reference: 2006-; vol 75 (issue ) : pp 435-65

Dates: Created 2006/06/07; Completed 2007/02/05;

PMID: 16756498, status: MEDLINE (last retrieval date: 12/26/2008)

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Associated Chemicals: O-Acetyl-ADP-Ribose (0) ; Protein Isoforms (0) ; NAD (53-84-9) ; ADP Ribose Transferases (EC 2.4.2.-) ; Sirtuins (EC 3.5.1.-)

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