Final answer:
When competitive inhibition occurs, Vmax stays the same, but Km must increase.
Step-by-step explanation:
When competitive inhibition occurs, Vmax stays the same, but Km must increase. Competitive inhibition is when an inhibitor binds reversibly to an enzyme at the active site, competing with the substrate for binding. The inhibitor and substrate are in competition for the same active site, which affects the kinetics of the reaction. As a result, the Vmax remains unchanged, but the Km increases because it requires a higher concentration of substrate to reach half of the maximum rate.