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Inhibition of rat liver phosphofructokinase-2 by phosphoenolpyruvate and ADP
Biochemical and Biophysical Research Communications
|November 14, 1984
Abstract:
Phosphofructokinase-2 from rat liver is inhibited by phosphoenolpyruvate and ADP. Phosphoenolpyruvate reduces the maximum activity in respect to fructose-6-phosphate and ATP but does not give rise to complete inhibition of phosphofructokinase-2. ADP increases the apparent Michaelis constant of the enzyme for ATP and leaves the maximum activity in respect to ATP unchanged. The apparent Michaelis constant for fructose-6-phosphate is not influenced by ADP.