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The substrate specificity of sirtuins.
Annu. Rev. Biochem. 85, 405-429 (2016)
Sirtuins are NAD(+)-dependent enzymes universally present in all organisms, where they play central roles in regulating numerous biological processes. Although early studies showed that sirtuins deacetylated lysines in a reaction that consumes NAD(+), more recent studies have revealed that these enzymes can remove a variety of acyl-lysine modifications. The specificities for varied acyl modifications may thus underlie the distinct roles of the different sirtuins within a given organism. Additional contributions to sirtuin function may also result from structural variations both within and flanking the conserved catalytic domain. This review summarizes the structure, chemistry, and substrate specificity of sirtuins with a focus on how different sirtuins recognize distinct substrates and thus carry out specific functions. Expected final online publication date for the Annual Review of Biochemistry Volume 85 is June 02, 2016. Please see http://www.annualreviews.org/catalog/pubdates.aspx for revised estimates.
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Publication type
Article: Journal article
Document type
Review
Keywords
Adp-ribosylation; Performance Liquid-chromatography; Sir2 Histone/protein Deacetylases; Adp-ribosyltransferase Activity; Pyruvate-dehydrogenase Complex; Dependent Protein Deacetylases; Plasmodium-falciparum Sir2; Acetyl-coa Synthetase; Fatty Acyl Lysine; Structural Basis; Histone Deacetylase
Language
english
Publication Year
2016
HGF-reported in Year
2016
ISSN (print) / ISBN
0066-4154
e-ISSN
1545-4509
Journal
Annual Review of Biochemistry
Quellenangaben
Volume: 85,
Pages: 405-429
Publisher
Annual Reviews
Publishing Place
Palo Alto, Calif.
Reviewing status
Peer reviewed
Institute(s)
Institute of Functional Epigenetics (IFE)
POF-Topic(s)
30203 - Molecular Targets and Therapies
Research field(s)
Helmholtz Diabetes Center
PSP Element(s)
G-502800-001
PubMed ID
27088879
WOS ID
WOS:000379324700017
Scopus ID
84974727339
Erfassungsdatum
2016-04-20