Results 131 to 140 of about 22,770 (160)
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A ‘random steady-state’ model for the pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase enzyme complexes

Physical Biology, 2010
The multienzyme complexes, pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase, involved in the central metabolism of Escherichia coli consist of multiple copies of three different enzymes, E1, E2 and E3, that cooperate to channel substrate intermediates between their active sites.
T S, Najdi   +2 more
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Isolation and properties of α-ketoglutarate dehydrogenase complex from baker's yeast (Saccharomyces cerevisiae)

Biochemical and Biophysical Research Communications, 1971
Abstract The α-ketoglutarate dehydrogenase complex (KGDC) of baker's yeast was isolated and shown to have a sedimentation velocity (S 20, W ) of 20.9 S. The enzyme complex catalyzes the oxidation of 7.7 μmoles of KG per min per mg protein. The activity of the purified KGDC has an absolute dependence on Co A and NAD and a partially dependence on TPP ...
T, Hirabayashi, T, Harada
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[Diaphorase reactions of lipoamide dehydrogenases from the adrenal ketoglutarate dehydrogenase complex].

Biokhimiia (Moscow, Russia), 1985
Lipoamide dehydrogenase, a component of the bovine adrenal ketoglutarate dehydrogenase complex, catalyzes the oxidation of NADH by p-quinones and ferricyanide. The kinetics of oxidation obey the ping-pong mechanism. At pH 7.0, the constants for the active center oxidation by quinones (kox) are equal to 1.1 X 10(4)-5.3 X 10(5) M-1s-1 and increase as the
N K, Chenas, A A, Butkus, Iu Iu, Kulis
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Studies on the apparent instability of bovine kidney α-ketoglutarate dehydrogenase complex

Archives of Biochemistry and Biophysics, 1974
Abstract The α-ketoglutarate dehydrogenase complex in extracts of bovine kidney and liver mitochondria is inactivated rapidly at 25 °C. This inactivation is not accompanied by loss of activity of the three component enzymes of the complex. This inactivation can be prevented by extensive washing of the mitochondria with dilute phosphate buffer prior ...
openaire   +2 more sources

[Regulation of alpha-ketoglutarate dehydrogenase complex from pigeon breast muscle].

Biokhimiia (Moscow, Russia), 1979
The activity of alpha-ketoglutarate dehydrogenase complex from pigeon breast muscle is controlled by ADP and the reaction products, i. e. succinyl-CoA and NADH. ADP activates the alpha-ketoglutarate dehydrogenase component of the complex, whereas NADH inhibits alpha-ketoglutarate dehydrogenase and lipoyl dehydrogenase.
V S, Gomazkova, O E, Krasovskaia
openaire   +1 more source

Integrative oncology: Addressing the global challenges of cancer prevention and treatment

Ca-A Cancer Journal for Clinicians, 2022
Jun J Mao,, Msce   +2 more
exaly  

_-Ketoglutarate Dehydrogenase Complex in Neurodegeneration

2012
Gary Gibson   +3 more
openaire   +1 more source

[Alpha-ketoglutarate dehydrogenase complex].

Nihon rinsho. Japanese journal of clinical medicine, 2002
Ichiro, Yokota, Yasuhiro, Kuroda
openaire   +1 more source

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