Kretschmer M, Hofmann E
Biochem Biophys Res Commun. 1984 Nov 14;124(3):793-6. doi: 10.1016/0006-291x(84)91027-1.
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.
大鼠肝脏中的磷酸果糖激酶-2受到磷酸烯醇丙酮酸和ADP的抑制。磷酸烯醇丙酮酸降低了相对于果糖-6-磷酸和ATP的最大活性，但不会导致磷酸果糖激酶-2完全抑制。ADP增加了该酶对ATP的表观米氏常数，而相对于ATP的最大活性保持不变。ADP不影响果糖-6-磷酸的表观米氏常数。
