Escherichia coli Phosphoenolpyruvate Carboxylase

@inproceedings{Thomas2001EscherichiaCP,
  title={Escherichia coli Phosphoenolpyruvate Carboxylase},
  author={K Bryn Thomas and Smith and Kunissery and T Balasubramanian and Ann Beezley},
  year={2001}
}
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 coCi K12 and various combinations of its primary substrate, P-enolpyruvate, and the activators acetylcoenzyme A, CDP, GTP, and fructose 1,6-bisphosphate. The analysis involves the evaluation of apparent K values, Ks for P-enolpyruvate and KA for activators, as a… CONTINUE READING