Affiliation:
1. 1Department of Chemistry and Biochemistry, San Francisco State University, San Francisco, CA, U.S.A.
2. 2School of Sciences, University of Louisiana at Monroe, Monroe, LA, U.S.A.
3. 3Department of Biochemistry, Larner College of Medicine, University of Vermont, Burlington, VT, U.S.A.
Abstract
Abstract
Metabolism within an organism is regulated by various processes, including post-translational modifications (PTMs). These types of chemical modifications alter the molecular, biochemical, and cellular properties of proteins and allow the organism to respond quickly to different environments, energy states, and stresses. Malate dehydrogenase (MDH) is a metabolic enzyme that is conserved in all domains of life and is extensively modified post-translationally. Due to the central role of MDH, its modification can alter metabolic flux, including the Krebs cycle, glycolysis, and lipid and amino acid metabolism. Despite the importance of both MDH and its extensively post-translationally modified landscape, comprehensive characterization of MDH PTMs, and their effects on MDH structure, function, and metabolic flux remains underexplored. Here, we review three types of MDH PTMs – acetylation, ADP-ribosylation, and methylation – and explore what is known in the literature and how these PTMs potentially affect the 3D structure, enzymatic activity, and interactome of MDH. Finally, we briefly discuss the potential involvement of PTMs in the dynamics of metabolons that include MDH.
Funder
National Institute of General Medical Sciences