title: A new role for α-ketoglutarate dehydrogenase complex: regulating metabolism through post-translational modification of other enzymes.
abstract: This Editorial highlights a study by Gibson et al. published in this issue of JNeurochem, in which the authors reveal a novel role for the α-ketoglutarate dehydrogenase complex (KGDHC) in post-translational modification of proteins. KGDHC may catalyze post-translational modification of itself as well as several other proteins by succinylation of lysine residues. The authors' report of an enzyme responsible for succinylation of key mitochondrial enzymes represents a major step toward our understanding of the complex functional metabolome. TCA, tricarboxylic acid; KG, α-ketoglutarate; KGDHC, α-ketoglutarate dehydrogenase complex; FUM, fumarase; MDH, malate dehydrogenase; ME, malic enzyme; GDH, glutamate dehydrogenase; AAT, aspartate aminotransferase; GS, glutamine synthetase; PAG, phosphate-activated glutaminase; SIRT3, silent information regulator 3; SIRT5, silent information regulator 5.
authors.affiliation: Department of Pediatrics and Program in Neuroscience, University of Maryland School of Medicine, Baltimore, Maryland, USA.
authors.forename: Mary C
authors.initials: MC
authors.lastname: McKenna
authors.affiliation: Neuroscience Research Australia and School of Medical Sciences UNSW, Randwick, NSW, Australia.
authors.forename: Caroline D
authors.initials: CD
authors.lastname: Rae
mesh_terms: D000214:Acyl Coenzyme A / Q000378:metabolism*; D000818:Animals; D005260:Female; D007655:Ketoglutarate Dehydrogenase Complex / Q000378:metabolism*; D008297:Male; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D009474:Neurons / Q000378:metabolism*
chemical_list: D000214:Acyl Coenzyme A; D009419:Nerve Tissue Proteins; D007655:Ketoglutarate Dehydrogenase Complex