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. 1987 Jul 1;245(1):13–18. doi: 10.1042/bj2450013

Kinetic studies on the reaction catalysed by phosphofructokinase from Trypanosoma brucei.

C N Cronin 1, K F Tipton 1
PMCID: PMC1148076  PMID: 2959272

Abstract

The steady-state kinetics of the reaction catalysed by the bloodstream form of Trypanosoma brucei were studied at pH 6.7. In the presence of 50 mM-potassium phosphate buffer, the apparent co-operativity with respect to fructose 6-phosphate and the non-linear relationship between initial velocity and enzyme concentration, which were found when the enzyme was assayed in 50 mM-imidazole buffer [Cronin & Tipton (1985) Biochem. J. 227, 113-124], are not evident. Studies on the variations of the initial rate with changing concentrations of MgATP and fructose 6-phosphate, the product inhibition by fructose 1,6-bisphosphate and the effects of the alternative substrate ITP were consistent with an ordered reaction pathway, in which MgATP binds to the enzyme before fructose 6-phosphate, and fructose 1,6-bisphosphate is the first product to dissociate from the ternary complex.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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