In the presence of a typical noncompetitive inhibitor of the activity of a particular enzyme toward a given substrate
A) the enzyme is irreversibly inactivated.
B) the potential maximum velocity will remain unchanged from that in the absence of the inhibitor.
C) the interaction of the inhibitor with the substrate is a major factor leading to the inhibition observed.
D) sigmoidal kinetics would be expected if there is no change in protein conformation on the binding of either S or I.
E) the apparent Michaelis constant for the substrate will be the same with or without inhibitor present.

Question

Quizplus · Accepted Answer

Noncompetitive inhibitors do not affect the binding of the substrate to the enzyme, so the apparent Michaelis constant (Km) remains unchanged. However, they do reduce the maximum velocity (Vmax) of the reaction.

In the Presence of a Typical Noncompetitive Inhibitor of the Activity