Effect of Competitive Inhibition on K_M Value

Enzymes are crucial biological catalysts that increase the rate of biochemical reactions without being consumed. One important characteristic of enzymes is their specificity towards substrates and their dependence on various factors such as temperature, pH, and the presence of inhibitors. For an enzyme following Michaelis-Menten kinetics, the relationship between substrate concentration and reaction rate can be described by the Michaelis-Menten equation. In examining enzyme kinetics, several terms are significant, including V_max, K_M, and turnover number. Given these concepts, consider the affect of competitive inhibition on enzyme behavior.

If an enzyme has a K_M value of 10 mM in the absence of a competitive inhibitor, what effect will the introduction of a competitive inhibitor with a high affinity for the enzyme’s active site most likely have on the K_M value?