What happens when an enzyme is bound by an allosteric activator?
A) The enzyme transitions from an activate state to an inactive state.
B) The enzyme transitions from a low affinity state to a high affinity state.
C) The enzyme transitions from a high affinity state to a low affinity state.
D) The enzyme can now bind to the cofactors necessary for the reaction.
E) The enzyme can no longer bind to inhibitors.

Question

Quizplus · Accepted Answer

Allosteric activators bind to an enzyme at a site other than the active site, inducing a conformational change that increases the enzyme's affinity for its substrate, transitioning it from a low affinity state to a high affinity state.

What Happens When an Enzyme Is Bound by an Allosteric