How does inhibition of an enzyme-catalyzed reaction by a competitive inhibitor differ from inhibition by a noncompetitive inhibitor?
A) Competitive inhibitors interfere with the enzyme; noncompetitive inhibitors interfere with the reactants.
B) Competitive inhibitors bind to the enzyme reversibly; noncompetitive inhibitors bind to it irreversibly.
C) Competitive inhibitors change the enzyme's tertiary structure; noncompetitive inhibitors cause polypeptide subunits to dissociate.
D) Competitive inhibitors bind to the active site of the enzyme; noncompetitive inhibitors bind to a different site.

Question

Quizplus · Accepted Answer

Inhibition of an enzyme-catalyzed reaction by a competitive inhibitor occurs when the inhibitor molecule binds to the active site of the enzyme, preventing the substrate from binding. Noncompetitive inhibitors, on the other hand, bind to the allosteric site of the enzyme, causing a conformational change in the enzyme that prevents the substrate from binding. So the main difference lies in the binding site of the inhibitors.

How Does Inhibition of an Enzyme-Catalyzed Reaction by a Competitive