Escherichia coli phosphoenolpyruvate carboxylase. Studies on the mechanism of synergistic activation by nucleotides.

Abstract

Kinetic studies were done to obtain a quantitative estimation of the synergistic interactions that occur between phosphoenolpyruvate carboxylase (orthophosphate:oxaloacetate carboxylase (phosphorylating) E.C. 4.1.1.31) from Escherichia coli K12 and various combinations of its primary substrate, P-enolpyruvate, and the activators acetylcoenzyme A, CDP, GTP… (More)

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Cite this paper

@article{Smith1980EscherichiaCP, title={Escherichia coli phosphoenolpyruvate carboxylase. Studies on the mechanism of synergistic activation by nucleotides.}, author={Tawnya E Smith and Kunisserry A Balasubramanian and A E Beezley}, journal={The Journal of biological chemistry}, year={1980}, volume={255 4}, pages={1635-42} }