Please use this identifier to cite or link to this item: https://hdl.handle.net/10316/106200
Title: A Molecular Perspective on Sirtuin Activity
Authors: Teixeira, Carla S. S.
Cerqueira, Nuno M. F. S. A.
Gomes, Pedro 
Sousa, Sérgio F.
Keywords: posttranslational modifications; protein acylation; lysine deacetylases; sirtuins
Issue Date: 15-Nov-2020
Publisher: MDPI
Project: UIDB/04378/2020 
SFRH/BD/114886/2016 
Serial title, monograph or event: International Journal of Molecular Sciences
Volume: 21
Issue: 22
Abstract: The protein acetylation of either the α-amino groups of amino-terminal residues or of internal lysine or cysteine residues is one of the major posttranslational protein modifications that occur in the cell with repercussions at the protein as well as at the metabolome level. The lysine acetylation status is determined by the opposing activities of lysine acetyltransferases (KATs) and lysine deacetylases (KDACs), which add and remove acetyl groups from proteins, respectively. A special group of KDACs, named sirtuins, that require NAD+ as a substrate have received particular attention in recent years. They play critical roles in metabolism, and their abnormal activity has been implicated in several diseases. Conversely, the modulation of their activity has been associated with protection from age-related cardiovascular and metabolic diseases and with increased longevity. The benefits of either activating or inhibiting these enzymes have turned sirtuins into attractive therapeutic targets, and considerable effort has been directed toward developing specific sirtuin modulators. This review summarizes the protein acylation/deacylation processes with a special focus on the current developments in the sirtuin research field.
URI: https://hdl.handle.net/10316/106200
ISSN: 1422-0067
DOI: 10.3390/ijms21228609
Rights: openAccess
Appears in Collections:I&D ICBR - Artigos em Revistas Internacionais
I&D CIBB - Artigos em Revistas Internacionais

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