How does a noncompetitive inhibitor decrease the rate of an enzyme-catalyzed reaction?
A) by binding to the active site of the enzyme, thus preventing binding of the normal substrate
B) by binding to an allosteric site, thus changing the shape of the active site of the enzyme
C) by decreasing the free-energy change of the reaction catalyzed by the enzyme
D) by binding to the substrate, thus changing its shape so that it no longer binds to the active site of the enzyme

Question

Quizplus · Accepted Answer

A noncompetitive inhibitor binds to an allosteric site on the enzyme and causes a conformational change in the enzyme. This change makes the active site less effective at catalyzing the reaction, ultimately decreasing the rate of the enzyme-catalyzed reaction.

How Does a Noncompetitive Inhibitor Decrease the Rate of an Enzyme-Catalyzed