The regulation of phosphofructokinase in epimastigote Trypanosoma cruzi

Glycosomal (microbody)-enriched fractions prepared from epimastigote Trypanosoma cruzi were used as a partially purified source of phosphofructokinase. D-Fructose 6-phosphate showed sigmoidal kinetics at pH 7.0, but hyperbolic kinetics at pH 8.0. Various adenosine nucleotides were positive effectors; 5'-AMP was the most powerful. ATP showed hyperbolic kinetics under all conditions tested. Several described inhibitors and activators of mammalian phosphofructokinase were without significant effect on the trypanosomal enzyme; the absence of effect of D-fructose 2,6-bisphosphate is of particular note.