For an enzyme-catalyzed reaction, the presence of 10 nM of a reversible inhibitor yields a Vmax value that is 80% of the value in the absence of the inhibitor. The KM is unchanged by the inhibitor. (a) What type of inhibition is taking place? (b) Calculate the dissociation constant for the inhibitor (Ki). (c) What percentage of the enzyme molecules have bound inhibitor?

Chemistry for Today: General, Organic, and Biochemistry
9th Edition
ISBN:9781305960060
Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen
Publisher:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen
Chapter20: Enzymes
Section: Chapter Questions
Problem 20.75E: In the multienzyme sequence shown below, molecules of D are able to fit to the enzyme E1 and prevent...
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For an enzyme-catalyzed reaction, the presence of 10 nM of a reversible inhibitor yields a Vmax value that is 80% of the value in the absence of the inhibitor. The KM is unchanged by the inhibitor.

(a) What type of inhibition is taking place?

(b) Calculate the dissociation constant for the inhibitor (Ki).

(c) What percentage of the enzyme molecules have bound inhibitor?

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