%0 Book Section %T Energy metabolism | 2-Oxoglutarate Dehydrogenase Complex %+ Department of Chemistry, Lomonosov Moscow State University %+ Sechenov First Moscow State Medical University %+ Max Planck Institute for Marine Microbiology %+ Microbiologie structurale - Structural Microbiology (Microb. Struc. (UMR_3528 / U-Pasteur_5)) %A Bunik, Victoria %A Wagner, Tristan %A Bellinzoni, Marco %@ 978-0-12-822040-5 %B Encyclopedia of Biological Chemistry III, Third edition %E Joseph Jez %I Elsevier %V vol.1 %P 259-271 %8 2021 %D 2021 %R 10.1016/B978-0-12-819460-7.00127-4 %K 2-oxoglutarate dehydrogenase %K Carboligase %K DHTKD1 or E1a %K Dihydrolipoamide dehydrogenase %K Dihydrolipoamide succinyl transferase %K DLDH or DLD or E3 %K DLST or E2o or ODO2 %K Multienzyme complex %K OGDH or E1o or ODO1 or KGD %K OGDHL or E1o %K Side reaction with molecular oxygen %K Thiamine diphosphate %K Vitamin %Z Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM]Book sections %X 2-Oxoglutarate dehydrogenase (ogdh gene) is an ubiquitous enzyme with additional isoenzymes (ogdhl and dhtkd1 genes) characterized in animals. Using thiamine (vitamin B1) diphosphate, the isoenzymes catalyze oxidative decarboxylation of 2-oxoglutarate or 2-oxoadipate. The coupled generation of succinyl- or glutaryl-CoA and NADH requires self-assembled multienzyme complexes. The complex core is formed by dihydrolipoyl succinyltransferase (dlst gene), binding multiple copies of 2-oxoglutarate dehydrogenase and dihydrolipoamide dehydrogenase (dldh gene). The components stoichiometry depends on the complex sources and/or isolation conditions. Components of the 2-oxoglutarate dehydrogenase complex also catalyze carboligase reaction or reaction with molecular oxygen, which are of potential physiological significance. %G English %L pasteur-03259560 %U https://pasteur.hal.science/pasteur-03259560 %~ PASTEUR %~ CNRS %~ UNIV-PARIS %~ UNIVERSITE-PARIS