Regulation of Escherichia coli phosphofructokinase in situ.

@article{Reeves1973RegulationOE,
  title={Regulation of Escherichia coli phosphofructokinase in situ.},
  author={Richard E. Reeves and Alberto Sols},
  journal={Biochemical and biophysical research communications},
  year={1973},
  volume={50 2},
  pages={
          459-66
        }
}
Abstract The activity of E. coli phosphofructokinase in situ has been studied in cells permeabilized to its substrates, products and effectors by a toluene-freezing treatment. The in situ enzyme exhibits moderate cooperativity in respect to F6P (n H up to 2.0), rather low affinity for ATP (with Km up to 1 mM when saturated with F6P), activation by ADP, and inhibition, within the physiological range of concentrations, by high ATP and phosphoenolpyruvate. This behaviour of the enzyme in situ at… CONTINUE READING

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