What do competitive inhibitors typically compete with?

Competitive inhibitors typically compete with the substrate for binding to the active site of an enzyme. When a competitive inhibitor is present, it mimics the structure of the substrate, allowing it to bind to the active site and thereby blocking the actual substrate from attaching. This competition can be overcome by increasing the concentration of the substrate, which can effectively outcompete the inhibitor and allow the enzyme to function normally. Understanding this mechanism is crucial, as it illustrates how competitive inhibition can regulate enzyme activity and affect metabolic pathways.