In reactions catalyzed by allosteric enzymes
A) substrate, activators, and inhibitors all compete for the same binding site on the enzyme.
B) there is no distinction between catalytic and regulatory subunits.
C) the presence of an activator makes the plot of reaction rate against substrate concentration less cooperative.
D) the presence of an inhibitor makes the plot of reaction rate against substrate concentration less cooperative.

Question

Quizplus · Accepted Answer

The presence of an activator typically reduces the cooperativity of the enzyme, making the reaction rate plot less sigmoidal and more hyperbolic, indicating a more Michaelis-Menten-like behavior.

In Reactions Catalyzed by Allosteric Enzymes