Abstract
Summary Phosphofructokinase from an extreme thermophilic bacterium was partially purified and it showed a thermostable allosteric nature. No detectable loss of activity was observed after incubation of the enzyme solution at 80° for 1 hour. The enzyme activity followed a simple Michaelis-Menten kinetics with respect to each substrate, fructose 6-phosphate and ATP. Phosphoenolpyruvate was a strong inhibitor and by its addition a normal saturation kinetic curve for fructose 6-phosphate was turned into a sigmoidal one, independent of ATP concentration. ADP relieved this inhibition.
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