Year: 2016
Type: review
Abstract: 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.
Source: Annual Review of Biochemistry
Language: English
Subfield: Geriatrics and Gerontology
Field: Medicine
Domain: Health Sciences
Open Access status: bronze
Awards: The Chemistry of Gene Silencing, Chemical/biochemical tools for studying novel protein acyl lysine modifications, BioCARS: A Synchroton Structural Biology Resource, Networks, Pathways and Dynamics of Lysine Modification, Macromolecular Crystallography at the National Synchrotron Light Source, Chemical Approaches for Studying the Biology of NAD-consuming Enzymes
OpenAlex ID: W2181797758