PuSH - Publication Server of Helmholtz Zentrum München

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

The substrate specificity of sirtuins.

Annu. Rev. Biochem. 85, 405-429 (2016)
Publ. Version/Full Text DOI
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.
Altmetric
Additional Metrics?
Edit extra informations Login
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
ISSN (print) / ISBN 0066-4154
e-ISSN 1545-4509
Quellenangaben Volume: 85, Issue: , Pages: 405-429 Article Number: , Supplement: ,
Publisher Annual Reviews
Publishing Place Palo Alto, Calif.
Reviewing status Peer reviewed