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  • Title: Phosphofructokinase from Plasmodium berghei: a kinetic model of allosteric regulation.
    Author: Buckwitz D, Jacobasch G, Gerth C.
    Journal: Mol Biochem Parasitol; 1990 May; 40(2):225-32. PubMed ID: 2141917.
    Abstract:
    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, efficiency activates the malarial enzyme. No activation by ADP was observed. Instead, ADP inhibits the enzyme non-allosterically and competitively to the substrate MgATP. Phosphate stimulates the catalytic activity of malarial PFK independently of the activation by F6P and PEP.
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