Protein acetylation effects on enzyme activity and metabolic pathway fluxes

Acetylation of proteins seems a widespread process found in the three domains of life. Several studies have shown that besides histones, acetylation of lysine residues also occurs in non‐nuclear proteins. Hence, it has been suggested that this covalent modification is a mechanism that might regulate...

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Bibliographic Details
Published in:Journal of cellular biochemistry 2022-04, Vol.123 (4), p.701-718
Main Authors: Marín‐Hernández, Álvaro, Rodríguez‐Zavala, José S., Jasso‐Chávez, Ricardo, Saavedra, Emma, Moreno‐Sánchez, Rafael
Format: Article
Language:English
Subjects:
Acetylation
covalent regulation
energy metabolism
Enzymatic activity
Enzyme activity
Enzyme kinetics
Enzymes
Fluxes
glycolysis
Histones
Kinetics
Krebs cycle
Localization
Lysine
Metabolic Networks and Pathways
Metabolic pathways
Metabolism
modeling
Protein Processing, Post-Translational
Proteins
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Summary:Acetylation of proteins seems a widespread process found in the three domains of life. Several studies have shown that besides histones, acetylation of lysine residues also occurs in non‐nuclear proteins. Hence, it has been suggested that this covalent modification is a mechanism that might regulate diverse metabolic pathways by modulating enzyme activity, stability, and/or subcellular localization or interaction with other proteins. However, protein acetylation levels seem to have low correlation with modification of enzyme activity and pathway fluxes. In addition, the results obtained with mutant enzymes that presumably mimic acetylation have frequently been over‐interpreted. Moreover, there is a generalized lack of rigorous enzyme kinetic analysis in parallel to acetylation level determinations. The purpose of this review is to analyze the current findings on the impact of acetylation on metabolic enzymes and its repercussion on metabolic pathways function/regulation.
ISSN:0730-2312
1097-4644
DOI:10.1002/jcb.30197