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- W1488346989 abstract "The rate of conversion of α-ketoglutarate to glutamate by the bovine liver mitochondria glutamate dehydrogenase and glutamate-oxaloacetate transaminase has been studied. In arsenate buffer, initial velocity studies (in the absence of added product) are consistent with the concept that the order of addition of substrate to glutamate dehydrogenase is sequential with DPNH adding first followed by α-ketoglutarate and then ammonium ions. The order of addition with respect to ammonium ions and α-ketoglutarate is opposite to that found in Tris-acetate buffer and could be the result of the higher Michaelis constant of ammonium ions in arsenate buffer. The value of this constant was found to be high, compared to physiological levels under all of the experimental conditions employed. Neither of the products of this reaction (DPN and glutamate) were significant inhibitors. Therefore these results suggest that ammonium ions are important regulators of this reaction. The glutamate-oxaloacetate transaminase reaction (when assayed in a coupled assay with malate dehydrogenase and DPNH) seems to react in a typical transaminase or ping-pong manner. α-Ketoglutarate has a much lower Michaelis constant for glutamate dehydrogenase than glutamate-oxaloacetate transaminase and is a substrate inhibitor of glutamate dehydrogenase. Consequently, the ratio of activity of glutamate dehydrogenase to glutamate-oxaloacetate transaminase would be higher at low (0.4 mm) than at high (4 mm) concentrations of α-ketoglutarate. One of the main regulators of the glutamate-oxaloacetate transaminase reaction would be the level of oxaloacetate since this compound is a very potent inhibitor of this reaction." @default.
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- W1488346989 date "1969-01-01" @default.
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- W1488346989 title "Studies of gluconeogenic mitochondrial enzymes" @default.
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- W1488346989 doi "https://doi.org/10.1016/0003-9861(69)90059-9" @default.
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