How do competitive inhibitors interact with enzymes?

Competitive inhibitors interact with enzymes by reversibly binding to the active site. This means that they compete with the substrate for the same binding spot on the enzyme. The presence of a competitive inhibitor can be overcome by increasing the concentration of the substrate, as more substrate molecules can successfully bind to the active site, effectively outcompeting the inhibitor.

This reversible interaction is crucial as it distinguishes competitive inhibitors from irreversible inhibitors, which permanently bind to the active site and inhibit enzyme activity. By selectively blocking the active site temporarily, competitive inhibitors effectively slow down the reaction without permanently altering the enzyme's structure or function. Thus, understanding this reversible competition is central to grasping enzyme kinetics and the dynamics of enzyme regulation.