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Stimulation of Trypanosoma brucei pyruvate kinase by fructose 2,6‐bisphosphate
Author(s) -
SCHAFTINGEN Emile,
OPPERDOES Fred. R.,
HERS HenriGéry
Publication year - 1985
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1985.tb09316.x
Subject(s) - fructose 2,6 bisphosphate , trypanosoma brucei , pyruvate kinase , fructose , phosphoenolpyruvate carboxykinase , biochemistry , fructolysis , biology , chemistry , glycolysis , enzyme , phosphofructokinase , gene
The activity of pyruvate kinase present in a crude extract of the bloodstream form of Trypanosoma brucei was greatly increased by fructose 2,6‐bisphosphate, which converted the saturation curve for phospho en olpyruvate from a sigmoid into a hyperbola with no change in V . Phosphate and arsenate had an effect opposite to that of fructose 2,6‐bisphosphate and the apparent K a for fructose 2,6‐bisphosphate was shifted from 75 nM to 1.5 μM by the presence of 5 mM phosphate. Fructose 1,6‐bisphosphate had effects similar to those of fructose 2,6‐bisphosphate but at approximately 4000‐fold higher concentrations. Pyruvate kinases of Crithidia luciliae and of Leishmania major , two trypanosomatids which are like T. brucei in containing glycosomes, were also stimulated by fructose 2,6‐bisphosphate and inhibited by phosphate.

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