Final answer:
Adding a competitive inhibitor to an enzymatic reaction does not increase product formation; it reduces the enzyme's catalytic activity by preventing substrate binding. Substrate concentration can be increased to overcome inhibition to an extent, but this has a limit, and the maximal reaction rate remains unaffected by the inhibitor.
Step-by-step explanation:
Adding a competitive inhibitor to an enzymatic reaction will not increase the number of products formed. A competitive inhibitor competes with the substrate for the active site on the enzyme, which means it can prevent the substrate from binding, as illustrated in Figure 16.5.12. While increasing substrate concentration can help to outcompete the inhibitor and restore enzyme activity to a point, as shown in Figure 19.6.1, there is a limit to this effect. Beyond a certain substrate concentration, all enzyme active sites will be occupied, and adding more substrate won't further increase the reaction rate or product formation.
Furthermore, the presence of a competitive inhibitor can affect the initial rate of the reaction but does not change the maximum rate the reaction can reach (as indicated by the green line in Figure 19.6.1). This is in contrast to a noncompetitive inhibitor, which affects the maximum rate of the reaction because it binds to a different site on the enzyme and changes its structure, making the active site less effective (as shown by the blue line in the same figure).
Therefore, in the presence of a competitive inhibitor, the enzyme's catalytic activity is lowered, leading to fewer products being formed unless the concentration of the substrate is significantly increased to offset the presence of the inhibitor.