Change in α-ketoglutarate dehydrogenase cooperative properties due to dihydrolipoate and NADH

• Published in: FEBS letters Vol. 269; no. 1; pp. 252 - 254
• Main Authors: Bunik, V.I., Buneeva, O.A., Gomazkova, V.S.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 20.08.1990; Elsevier
• Subjects: Allosteric Regulation; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; CoA, coenzyme A; Columbidae; Cooperativity; DEP, diethyl pyrocarbonate; Diethyl Pyrocarbonate - pharmacology; Dihydrolipoate; DTNB, 5,5'-dithio-bis-(2-nitrobenzoic) acid; DTT, dithiothreitol; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Ketoglutarate Dehydrogenase Complex - metabolism; Ketone Oxidoreductases - metabolism; KG, α-ketoglutarate; KGD, α-ketoglutarate dehydrogenase; Macromolecular Substances; Muscles - enzymology; NAD - metabolism; NADH; Oxidation-Reduction; Oxidoreductases; Protein Conformation; Sulfhydryl Compounds; Thioctic Acid - analogs & derivatives; Thioctic Acid - metabolism; TPP, thiamine pyrophosphate; α-Ketoglutarate dehydrogenase; NADH; KG, α-ketoglutarate; KGD, α-ketoglutarate dehydrogenase; Dihydrolipoate; α-Ketoglutarate dehydrogenase; Cooperativity; DTNB, 5,5'-dithio-bis-(2-nitrobenzoic) acid; CoA, coenzyme A; DEP, diethyl pyrocarbonate; DTT, dithiothreitol; TPP, thiamine pyrophosphate; Ligand binding; Lipoic acid; Vertebrata; Regulation(control); Enzymatic activity; Muscle; Oxoglutarate dehydrogenase; Aves; Derived product
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(90)81166-L

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.