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. 1987 Oct 1;247(1):41–46. doi: 10.1042/bj2470041

The roles of magnesium ions in the reaction catalysed by phosphofructokinase from Trypanosoma brucei.

C N Cronin 1, K F Tipton 1
PMCID: PMC1148366  PMID: 2961325

Abstract

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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Selected References

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