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- W2047811542 abstract "The role of glutamate dehydrogenase (GDH) in amino acid catabolism of the mantle of Mya arenaria was examined using coupled mitochondria and in vitro enzyme activity measurements. The maximal activities of mitochondrial glutamate-oxaloacetate transaminase (GOT) and glutamate-pyruvate transaminase (GPT) are fourfold and twofold greater, respectively, than GDH (deaminating). Based on pH profiles, the relative activities of these enzymes in vivo may be highly dependent on mitochondrial pH. Addition of ADP resulted in a 15-fold activation of GDH (deaminating) and a shift in the pH optimum from 8.1 to 8.6. The in vitro activity of GDH was sufficient to account for all NADH produced in intact mitochondria oxidizing glutamate. In intact mitochondria at pH 7.4 and 8.2, addition of the aminotransferase inhibitor aminooxyacetic acid (AOA) had no effect on the state 3 rate of glutamate oxidation. However, at pH 6.7 in situ GDH (deaminating) activity was insufficient to maintain the rate of glutamate oxidation in the absence of transaminase activity. Glutamate oxidation between pH 6.4 and 8.0 is limited by the electron transport system. At pH 8.3, transport of glutamate into the mitochondria may be rate limiting. Mitochondria oxidizing glutamate in state 4 in the presence of phosphate or in state 2 in the absence of phosphate demonstrated increased oxygen consumption in response to the uncoupler carbonyl m-chlo-rophenyl-hydrazone (CCCP). These studies suggest that in spite of low activities compared to vertebrates, GDH activities could be physiologically significant in amino acid metabolism of Mya arenaria mantle." @default.
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- W2047811542 title "Glutamate catabolism in mitochondria fromMya arenaria mantle: Effects of pH on the role of glutamate dehydrogenase" @default.
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- W2047811542 doi "https://doi.org/10.1002/jez.1402360306" @default.
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