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A researcher synthesizes a new molecule called inhibitor X that inhibits the activity of phosphofructokinase (PFK), the enzyme that phosphorylates fructose 6-phosphate during glycolysis. Inhibitor X competes with ATP for binding to the PFK active site. The researcher determines that the Michaelis-Menten constant (Km) with respect to ATP is 40 µM. When 2 µM inhibitor X is added to the purified PFK reaction, the apparent Km for ATP increases to 48 µM. Calculate the dissociation constant of the PFK-inhibitor complex (K₁). K₁= = µM

A researcher synthesizes a new molecule called inhibitor X that inhibits the activity of phosphofructokinase (PFK), the enzyme that phosphorylates fructose 6-phosphate during glycolysis. Inhibitor X competes with ATP for binding to the PFK active site. The researcher determines that the Michaelis-Menten constant (Km) with respect to ATP is 40 µM. When 2 µM inhibitor X is added to the purified PFK reaction, the apparent Km for ATP increases to 48 µM. Calculate the dissociation constant of the PFK-inhibitor complex (K₁). K₁= = µM

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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5 A researcher synthesizes a new molecule called inhibitor X that inhibits the activity of phosphofructokinase (PFK), the enzyme that phosphorylates fructose 6-phosphate during glycolysis. Inhibitor X competes with ATP for binding to the PFK active site. The researcher determines that the Michaelis-Menten constant (Km) with respect to ATP is 40 µM. When 2 µM inhibitor X is added to the purified PFK reaction, the apparent K for ATP increases to 48 µM. Calculate the dissociation constant of the PFK-inhibitor complex (K₁). K₁ = μM
Transcribed Image Text:5 A researcher synthesizes a new molecule called inhibitor X that inhibits the activity of phosphofructokinase (PFK), the enzyme that phosphorylates fructose 6-phosphate during glycolysis. Inhibitor X competes with ATP for binding to the PFK active site. The researcher determines that the Michaelis-Menten constant (Km) with respect to ATP is 40 µM. When 2 µM inhibitor X is added to the purified PFK reaction, the apparent K for ATP increases to 48 µM. Calculate the dissociation constant of the PFK-inhibitor complex (K₁). K₁ = μM
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