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Activation of maize zea mays phosphoenolpyruvate carboxylase by glucose 6 phosphate and glycine effects of ph and magnesium



Activation of maize zea mays phosphoenolpyruvate carboxylase by glucose 6 phosphate and glycine effects of ph and magnesium



Photosynthetica (Prague) 19(2): 177-182



The phosphoenolpyruvate carboxylase (PEPC) I isoenzyme was strongly activated by glucose-6-phosphate and glycine, the activation of PEPC II was much smaller. The activations of PEPC I by glucose-6-phosphate and glycine were pH-dependent and not affected by the concentrations of Mg2+ ions. The most significant activation was observed at pH 7.0. Typical hyperbolas were obtained for glycine activation over the entire pH range tested (7.0-9.0) and for glucose-6-phosphate activation at pH above 8.1. At pH 7.5 or lower the saturation curves for glucose-6-phosphate were sigmoidal. The conformational changes brought about by the glucose-6-phosphate and glycine binding lead to activation.

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Accession: 004663575

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