Final answer:
The inhibitor functions by modifying the enzyme's active site to reduce substrate binding, while the presence of ADP as an allosteric activator enhances the enzyme's affinity for its substrate.
Step-by-step explanation:
In the presence of ADP acting as an allosteric activator, the inhibitor's function undergoes modulation. Allosteric regulation involves a change in the enzyme's conformation due to the binding of a regulatory molecule at a site distinct from the active site.
ADP, serving as an allosteric activator, likely induces a conformational change that mitigates the inhibitory effect, allowing the enzyme to function more effectively. This intricate interplay showcases the dynamic nature of enzyme regulation, where the presence of specific molecules can finely tune the enzyme's activity, influencing cellular processes in response to changing metabolic demands.
Your question is incomplete, most probably the complete question is:
How does the inhibitor function in the presence of ADP, which acts as an allosteric activator?