Abstract
The role of enzyme cooperativity in the mechanism of metabolic oscillations is analyzed in a concerted allosteric model for the phosphofructokinase reaction. This model of a dimer enzyme activated by the reaction product accounts quantitatively for glycolytic periodicities observed in yeast and muscle. The Hill coefficient characteristic of enzyme-substrate interactions is determined in the model, both at the steady state and in the course of sustained oscillations. Positive cooperativity is a prerequisite for periodic behavior. A necessary condition for oscillation in a dimer K system is a Hill coefficient larger than 1.6 at the unstable stationary state. The analysis suggests that positive as well as negative effectors of phosphofructokinase inhibit glycolytic oscillations by inducing a decrease in enzyme cooperativity. The results are discussed with respect to glycolytic and other metabolic periodicities.
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