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The main action of a competitive inhibitor on an enzyme is that it mimics the substrate and enters the active site. Competitive inhibitors closely resemble the structure of the substrate that the enzyme normally acts upon. When these inhibitors bind to the active site, they prevent the actual substrate from binding. This competition between the inhibitor and the substrate can be reversed by increasing the concentration of the substrate, allowing more substrate molecules to bind to the active site.

This mechanism is crucial in regulatory processes within the cell, as it allows for fine-tuning of metabolic pathways. Competitive inhibition can be used strategically in drug design to inhibit specific enzymes involved in disease processes by blocking the substrate access and thus reducing the enzymatic activity associated with disease progression.

Other options describe different types of enzyme interactions. For instance, binding to a separate site would refer to non-competitive inhibitors, which do not directly compete with the substrate for the active site. Altering the enzyme's shape is characteristic of allosteric inhibition, where a molecule binds to an enzyme at a site distinct from the active site and modifies its functionality. Increasing the enzyme's activity would describe a situation not consistent with inhibition, as competitive inhibition serves to reduce enzymatic activity rather than enhance it.