Phosphofructokinase from Plasmodium berghei: a kinetic model of allosteric regulation.

@article{Buckwitz1990PhosphofructokinaseFP,
  title={Phosphofructokinase from Plasmodium berghei: a kinetic model of allosteric regulation.},
  author={D Buckwitz and Gisela Jacobasch and Christa Gerth},
  journal={Molecular and biochemical parasitology},
  year={1990},
  volume={40 2},
  pages={225-32}
}
As in mammalian cells, phosphofructokinase (PFK) is of major regulatory importance in the glucose metabolism of Plasmodium berghei. The malarial enzyme shows allosteric properties similar to PFK from various sources; it is activated by fructose-6-phosphate and inhibited by ATP, but differs with respect to allosteric regulation. Enzyme activity is only marginally increased by AMP, a potent activator of many phosphofructokinases. Phosphoenolpyruvate, which is reported to inhibit PFK activity… CONTINUE READING