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.
D000244:Adenosine Diphosphate / Q000494:pharmacology; D000249:Adenosine Monophosphate / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D000242:Cyclic AMP / Q000494:pharmacology; D005635:Fructosediphosphates / Q000494:pharmacology; D005988:Glyceric Acids / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010732:Phosphofructokinase-1 / Q000378:metabolism*; D014349:Trypanosoma cruzi / Q000201:enzymology*
D005635:Fructosediphosphates; D005988:Glyceric Acids; D000249:Adenosine Monophosphate; D000244:Adenosine Diphosphate; C027652:fructose 2,6-diphosphate; C005156:3-phosphoglycerate; D000255:Adenosine Triphosphate; D000242:Cyclic AMP; D010732:Phosphofructokinase-1