In the presence of a competitive inhibitor, the apparent Vmax and KM values will

In the presence of a competitive inhibitor, the apparent Vmax (maximum rate of reaction) will remain the same while the KM (Michaelis-Menten constant) value will increase.

Here's the step-by-step explanation:

1. Competitive inhibitors are molecules that are similar in structure to the substrate and can bind to the active site of the enzyme, preventing the substrate from binding.

2. When a competitive inhibitor is present, it competes with the substrate for the active site on the enzyme. This means that more substrate is needed to achieve the same rate of reaction, which effectively increases the KM value. KM is the substrate concentration at which the reaction rate is half of Vmax. An increase in KM means that a higher substrate concentration is required to reach half of Vmax, indicating a decrease in the enzyme's affinity for the substrate.

3. However, the Vmax remains the same because, given enough substrate, it can outcompete the inhibitor and fully saturate the enzyme, reaching the maximum rate of reaction. The Vmax is the maximum rate of reaction that can be achieved by the enzyme, and it is not affected by competitive inhibitors because these inhibitors do not change the enzyme's ability to catalyze the reaction, they just compete with the substrate for binding to the enzyme.

4. Therefore, in the presence of a competitive inhibitor, the apparent Vmax remains the same, and the KM value increases.