Final answer:
Yes, we can compare the effectiveness of an inhibitor by checking how much they change Km and Vmax during a reaction. By increasing Km, an inhibitor reduces enzyme efficiency, while decreasing Vmax indicates a decrease in catalytic activity. Comparing these changes helps evaluate the impact of inhibitors on enzyme effectiveness.
Step-by-step explanation:
Yes, we can compare the effectiveness of an inhibitor by checking how much they change Km and Vmax during a reaction. Km represents the substrate concentration at which the reaction rate has reached half of the maximum rate. So, if an inhibitor increases Km, it means that more substrate is required to reach the half-maximal rate, indicating reduced enzyme efficiency. On the other hand, Vmax represents the maximum initial rate of the reaction. If an inhibitor decreases Vmax, it means that the enzyme's catalytic activity has been decreased. By comparing changes in Km and Vmax, we can assess the impact of different inhibitors on enzyme effectiveness.