Journal
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 85
Volume 85, Issue -, Pages 405-429Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-biochem-060815-014537
Keywords
deacylation; succinylation; myristoylation; palmitoylation; ADP-ribosylation
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Funding
- NIGMS NIH HHS [U54 GM103520, R01 GM098596, R01 GM086703] Funding Source: Medline
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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. 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.
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