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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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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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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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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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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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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, 1974Abstract 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 ...
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[Regulation of alpha-ketoglutarate dehydrogenase complex from pigeon breast muscle].
Biokhimiia (Moscow, Russia), 1979The 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
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Integrative oncology: Addressing the global challenges of cancer prevention and treatment
Ca-A Cancer Journal for Clinicians, 2022Jun J Mao,, Msce +2 more
exaly
Interaction of the α-Ketoglutarate Dehydrogenase Complex with Basic Polypeptides*
The Journal of Biochemistry, 1974K, Imai, Y, Tomita
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_-Ketoglutarate Dehydrogenase Complex in Neurodegeneration
2012Gary Gibson +3 more
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[Alpha-ketoglutarate dehydrogenase complex].
Nihon rinsho. Japanese journal of clinical medicine, 2002Ichiro, Yokota, Yasuhiro, Kuroda
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Reversible reduction of thioctamide catalyzed by the α-ketoglutaric dehydrogenase complex
Biochimica et Biophysica Acta, 1957D R, SANADI, R L, SEARLS
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