Acetylation, ADP-ribosylation and methylation of malate dehydrogenase.
ADP-ribosylation
Acetylation
Malate Dehydrogenase
Metabolon
Methylation
Post-translational modifications
Journal
Essays in biochemistry
ISSN: 1744-1358
Titre abrégé: Essays Biochem
Pays: England
ID NLM: 0043306
Informations de publication
Date de publication:
12 Jul 2024
12 Jul 2024
Historique:
received:
18
03
2024
revised:
20
06
2024
accepted:
24
06
2024
medline:
12
7
2024
pubmed:
12
7
2024
entrez:
12
7
2024
Statut:
aheadofprint
Résumé
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.
Identifiants
pubmed: 38994669
pii: 234701
doi: 10.1042/EBC20230080
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : National Institute of General Medical Sciences (NIGMS)
ID : R35GM133506
Informations de copyright
© 2024 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.