Inhibition of rat liver phosphofructokinase-2 by phosphoenolpyruvate and ADP.
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.
D000244:Adenosine Diphosphate / Q000494:pharmacology*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D005636:Fructosephosphates / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008433:Mathematics; D010728:Phosphoenolpyruvate / Q000494:pharmacology*; D010732:Phosphofructokinase-1 / Q000037:antagonists & inhibitors*; D051381:Rats
D005636:Fructosephosphates; D000244:Adenosine Diphosphate; C027618:fructose-6-phosphate; D010728:Phosphoenolpyruvate; D000255:Adenosine Triphosphate; D010732:Phosphofructokinase-1