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.
Research Article|July 01 1987
Kinetic studies on the reaction catalysed by phosphofructokinase from Trypanosoma brucei
C N Cronin;
Biochem J (1987) 245 (1): 13-18.
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C N Cronin, K F Tipton; Kinetic studies on the reaction catalysed by phosphofructokinase from Trypanosoma brucei. Biochem J 1 July 1987; 245 (1): 13–18. doi: https://doi.org/10.1042/bj2450013
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