A Novel Mechanism for SIRT1 Activators That Does Not Rely on the Chemical Moiety Immediately C-Terminal to the Acetyl-Lysine of the Substrate

A Novel Mechanism for SIRT1 Activators That Does Not Rely on the Chemical Moiety Immediately C-Terminal to the Acetyl-Lysine of the Substrate

SIRT1, an NAD<sup>+</sup>-dependent deacetylase, catalyzes the deacetylation of proteins coupled with the breakdown of NAD<sup>+</sup> into nicotinamide and 2′-O-acetyl-ADP-ribose (OAADPr). Selective SIRT1 activators have potential clinical applications in atherosclerosis, ac...

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Bibliographic Details
Main Authors: Nian-Da Yu, Bing Wang, Xin-Zhu Li, Hao-Zhen Han, Dongxiang Liu
Format: Article
Language:English
Published: MDPI AG 2022-04-01
Series:Molecules
Subjects:
SIRT1
activator
covalent bond
2′-O-acetyl-ADP-ribose
deacetylase
Online Access:https://www.mdpi.com/1420-3049/27/9/2714

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