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?

Introduction to General, Organic and Biochemistry
11th Edition
ISBN:9781285869759
Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Chapter23: Enzymes
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Problem 23.15P: 5 At a very low concentration of a certain substrate, we find that when the substrate concentration...
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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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