title: Change in alpha-ketoglutarate dehydrogenase cooperative properties due to dihydrolipoate and NADH.
abstract: Reducing 2 SH-groups of KGD by dihydrolipoate leads to cooperativity in substrate binding. Cooperative properties of KGD in the KGD complex are modulated by NADH. Physiological significance of these observations is discussed.
authors.affiliation: Department of Biochemistry, Moscow State University, USSR.
authors.forename: V I
authors.initials: VI
authors.lastname: Bunik
authors.forename: O A
authors.initials: OA
authors.lastname: Buneeva
authors.forename: V S
authors.initials: VS
authors.lastname: Gomazkova
mesh_terms: D000494:Allosteric Regulation; D000818:Animals; D010856:Columbidae; D004047:Diethyl Pyrocarbonate / Q000494:pharmacology; D007655:Ketoglutarate Dehydrogenase Complex / Q000378:metabolism*; D007658:Ketone Oxidoreductases / Q000378:metabolism*; D046911:Macromolecular Substances; D009132:Muscles / Q000201:enzymology; D009243:NAD / Q000378:metabolism*; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013438:Sulfhydryl Compounds; D008063:Thioctic Acid / Q000031:analogs & derivatives* / Q000378:metabolism
chemical_list: D046911:Macromolecular Substances; D013438:Sulfhydryl Compounds; D009243:NAD; D008063:Thioctic Acid; C015144:dihydrolipoic acid; D007658:Ketone Oxidoreductases; D007655:Ketoglutarate Dehydrogenase Complex; D004047:Diethyl Pyrocarbonate