Which of the following statements about inhibitors of enzyme-catalyzed reactions is TRUE?

Question

Quizplus · Accepted Answer

Competitive inhibitors compete with the substrate for binding at the active site of the enzyme, but they do not affect the maximum rate (Vmax) of the reaction because if enough substrate is present, it can outcompete the inhibitor and reach the maximum rate of reaction. The presence of a competitive inhibitor increases the apparent KM (the Michaelis constant, which is the substrate concentration at which the reaction rate is half of Vmax), as it requires a higher substrate concentration to reach half of Vmax in the presence of the inhibitor.

Which of the Following Statements About Inhibitors of Enzyme-Catalyzed Reactions