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Bheda, P. ; Jing, H.* ; Wolberger, C.* ; Lin, H.*

The substrate specificity of sirtuins.

Annu. Rev. Biochem. 85, 405-429 (2016)
Verlagsversion DOI PMC
Open Access Gold
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Review
Schlagwörter 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
Sprache englisch
Veröffentlichungsjahr 2016
HGF-Berichtsjahr 2016
ISSN (print) / ISBN 0066-4154
e-ISSN 1545-4509
Zeitschrift Annual Review of Biochemistry
Quellenangaben Band: 85, Heft: , Seiten: 405-429 Artikelnummer: , Supplement: ,
Verlag Annual Reviews
Verlagsort Palo Alto, Calif.
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Functional Epigenetics (IFE)
POF Topic(s) 30203 - Molecular Targets and Therapies
Forschungsfeld(er) Helmholtz Diabetes Center
PSP-Element(e) G-502800-001
PubMed ID 27088879
DOI 10.1146/annurev-biochem-060815-014537
WOS ID WOS:000379324700017
Scopus ID 84974727339
Erfassungsdatum 2016-04-20
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