How can you overcome the interference of a competitive inhibitor in a reaction?

Increasing the concentration of the correct substrate is an effective way to overcome the interference of a competitive inhibitor because competitive inhibitors bind to the active site of the enzyme, preventing the substrate from accessing it. By raising the concentration of the substrate, the likelihood of substrate molecules binding to the enzyme increases compared to that of the inhibitor. This competitive advantage can effectively outcompete the inhibitor for binding to the enzyme's active site, thereby restoring enzyme activity despite the presence of the inhibitor.

This principle is rooted in enzyme kinetics, specifically the Michaelis-Menten model, which describes how enzymes interact with substrates and inhibitors. In the presence of a competitive inhibitor, the apparent Km (Michaelis constant) of the reaction increases, indicating that a higher substrate concentration is needed to reach half the maximum velocity of the reaction. However, the maximum velocity (Vmax) remains unchanged since it ultimately depends on the amount of enzyme available, not the presence of the inhibitor.

In contrast, decreasing the temperature generally reduces the kinetic energy of molecules, potentially slowing down the reaction overall and not specifically addressing the competitive inhibition. Adding more competitive inhibitors would exacerbate the issue by providing more molecules that compete for the active site, leading to even greater inhibition. Using a different enzyme may not be practical or