Catalysis by protein acetyltransferase Gcn5
Document Type
Article
Publication Date
2021
Department/School
Chemistry
Publication Title
Biochimica et Biophysica Acta - Gene Regulatory Mechanisms
Abstract
Gcn5 serves as the defining member of the Gcn5-related N-acetyltransferase (GNAT) superfamily of proteins that display a common structural fold and catalytic mechanism involving the transfer of the acyl-group, primarily acetyl-, from CoA to an acceptor nucleophile. In the case of Gcn5, the target is the ε-amino group of lysine primarily on histones. Over the years, studies on Gcn5 structure-function have often formed the basis by which we understand the complex activities and regulation of the entire protein acetyltransferase family. It is now appreciated that protein acetylation occurs on thousands of proteins and can reversibly regulate the function of many cellular processes. In this review, we provide an overview of our fundamental understanding of catalysis, regulation of activity and substrate selection, and inhibitor development for this archetypal acetyltransferase.
Link to Published Version
Recommended Citation
Albaugh, B. N., & Denu, J. M. (2021). Catalysis by protein acetyltransferase Gcn5. Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, 1864(2), 194627. https://doi.org/10.1016/j.bbagrm.2020.194627