Which process involves transforming unreactive molecules into an active form that often leads to enzyme inhibition?

The process of transforming unreactive molecules into an active form that often leads to enzyme inhibition is known as mechanism-based inhibition. This type of inhibition occurs when a substrate analog is converted within the active site of the enzyme into a reactive species. This reactive species then covalently modifies the enzyme, effectively inhibiting its activity. The unique aspect of mechanism-based inhibitors is that they often mimic the natural substrate, allowing them to be processed by the enzyme's catalytic mechanism, yet ultimately result in a non-functional enzyme form.

This is distinct from other types of inhibition. Allosteric inhibition involves the binding of an inhibitor to a site other than the active site, leading to a change in enzyme shape and function. Competitive inhibition happens when an inhibitor directly competes with the substrate for the active site, effectively reducing the amount of enzyme available for substrate binding but not altering the enzyme's structure. Non-competitive inhibition occurs when an inhibitor binds to an alternative site on the enzyme, decreasing its activity regardless of substrate concentration, but again not leading to the transformation of a substrate into an active form that modifies the enzyme itself. Hence, the specific mechanism described in the question is best characterized by mechanism-based inhibition.