Protein acetylation effects on enzyme activity and metabolic pathway fluxes

Abstract

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.

PGAM5 deacetylation mediated by SIRT2 facilitates lipid metabolism and liver cancer proliferation

“…More than 20% of the proteins localized in mitochondria undergo (de)acetylation modification [26] . Protein lysine-acetylation modification plays important biological roles in protein-protein interactions and protease activity, affecting protein subcellular localization and protein stability [ 6 , 27 ]. Aberrant protein lysine acetylation can alter a variety of cellular functions and play important roles under physiological and pathological conditions.…”

The Protein Acetylation after Traumatic Spinal Cord Injury: Mechanisms and Therapeutic Opportunities

“…In this review, acetylation refers only to post-translational Nε-lysine acetylation. It is acetylation that enables proteins to possess abundant activities and functions by modulating protein stability, enzyme activity, subcellular localization, and interactions with other PTMs [23,24]. Because each modified protein is distinct, acetylation can be classified as histone acetylation or non-histone acetylation.…”