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.O. Various adenosine nucleotides were positive effectors...

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Veröffentlicht in:FEBS letters 1986-06, Vol.201 (2), p.262-266
Hauptverfasser: Taylor, Mark, Gutteridge, Winston E.
Format: Artikel
Sprache:eng
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Zusammenfassung: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.O. 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. Phosphofructokinase D-Fructose 2,6-bisphosphate (Trypanosoma cruzi, Parasitic protozoan)
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(86)80620-2