Change in alpha-ketoglutarate dehydrogenase cooperative properties due to dihydrolipoate and NADH.
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.
Bunik
V I
VI
Department of Biochemistry, Moscow State University, USSR.
Buneeva
O A
OA
Gomazkova
V S
VS
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
D046911:Macromolecular Substances; D013438:Sulfhydryl Compounds; D009243:NAD; D008063:Thioctic Acid; C015144:dihydrolipoic acid; D007658:Ketone Oxidoreductases; D007655:Ketoglutarate Dehydrogenase Complex; D004047:Diethyl Pyrocarbonate