A new role for α‐ketoglutarate dehydrogenase complex: regulating metabolism through post‐translational modification of other enzymes. (4th June 2015)

• Record Type: Journal Article
• Authors: McKenna, Mary C.; Rae, Caroline D.
• Is Part Of: Journal of neurochemistry. Volume 134:Number 1(2015:Jul.)
• Page Start: 3
• Page End: 6
• Publication Date: 2015-06-04
• Subjects: Neurochemistry -- Periodicals; 616.8042
• DOI: 10.1111/jnc.13150
• Languages: English
• ISSNs: 0022-3042

Abstract

<abstract abstract-type="main" id="jnc13150-abs-0001"> <title>Abstract</title> <p> <graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgj10cncm4v" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /> </p> <p>This Editorial highlights a study by Gibson <italic>et al</italic>. <xref ref-type="link" rid="jnc13150-bib-0009">2015</xref> 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.</p> </abstract>