The involvement of Mg2+ ions in the reaction catalysed by phosphofructokinase from Trypanosoma brucei was studied. The true substrate for the enzyme was shown to be the MgATP2-complex, and free Mg2+ ions are also required for enzyme activity. At concentrations of MgATP2- of 2.92 mM and greater, and a fructose 6-phosphate concentration of 1 mM and in the presence of EDTA as a Mg2+ buffer, the Km value for Mg2+ was determined to be 294 +/- 18 microM. Neither MgATP nor free ATP is an inhibitor of the enzyme, although apparent inhibition by the latter can be observed as a consequence of the decrease in free Mg2+ by chelation.
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Research Article| October 01 1987
The roles of magnesium ions in the reaction catalysed by phosphofructokinase from Trypanosoma brucei
C N Cronin ;
Biochem J (1987) 247 (1): 41–46.
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C N Cronin, K F Tipton; The roles of magnesium ions in the reaction catalysed by phosphofructokinase from Trypanosoma brucei. Biochem J 1 October 1987; 247 (1): 41–46. doi: https://doi.org/10.1042/bj2470041
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