[Characteristics of kinetics of the enzymatic oxoglutarate dehydrogenase reaction in a system with 2,6-dichlorophenolindophenol].
The 2-oxoglutarate: 2,6-dichlorophenolindophenol (DCPIP)--oxidoreductase reaction catalyzed by the oxoglutarate dehydrogenase complex from bovine adrenal glands corresponds to the kinetic mechanism of a "ping-pong" type. There are signs of positive cooperativity of the oxoglutarate dehydrogenase interaction with the substrate and negative cooperativity of that with the electron acceptor. The half-maximal rate of the model reaction is provided by 0.01 mM concentrations of 2-oxoglutarate and DCPIP. The exceeding of the DCPIP optimum concentration (0.1 mM) results in the enzyme inhibition.
Taranda
N I
NI
Strumilo
S A
SA
Vinogradov
V V
VV
D015086:2,6-Dichloroindophenol / Q000378:metabolism*; D000302:Adrenal Cortex / Q000201:enzymology; D000818:Animals; D002417:Cattle; D007215:Indophenol / Q000031:analogs & derivatives*; D007655:Ketoglutarate Dehydrogenase Complex / Q000378:metabolism*; D007658:Ketone Oxidoreductases / Q000378:metabolism*; D007700:Kinetics; D008928:Mitochondria / Q000201:enzymology; D013379:Substrate Specificity
D007215:Indophenol; D015086:2,6-Dichloroindophenol; D007658:Ketone Oxidoreductases; D007655:Ketoglutarate Dehydrogenase Complex
Osobennosti kinetiki fermentativnoĭ oksoglutaratdegidrogenaznoĭ reaktsii v sisteme s 2,6-dikhlorfenolindofenolom.