Final answer:
Competitive inhibition involves an inhibitor competing with the substrate for the enzyme's active site, and the reaction rate is affected by the substrate concentration. High concentrations of substrate can overcome the inhibition, restoring the enzyme's normal activity.
Step-by-step explanation:
Competitive inhibition of enzyme activity is characterized by the rate of the chemical reaction being influenced by the enzyme, which is dependent on the ratio of enzyme to substrate. This means that the rate of chemical reaction can be affected by the concentration of substrate, and with sufficiently high substrate concentrations, the inhibition by the competitive inhibitor can be overcome. A competitive inhibitor binds reversibly at the active site of the enzyme, competing with the substrate. Since the inhibitor does not act as a substrate and no reaction occurs, the enzyme's catalytic activity is temporarily blocked. However, an increase in substrate concentration can outcompete the inhibitor, allowing for normal enzyme activity.