Final answer:
KM and Vmax are key kinetic factors in enzyme-catalyzed reactions. KM is the substrate concentration at which the velocity of the reaction is half of the maximum velocity. Vmax represents the maximum initial rate of the reaction when all enzyme active sites are saturated.
Step-by-step explanation:
The values of KM and Vmax are important factors in enzyme-catalyzed reactions. KM, or the Michaelis constant, is the substrate concentration at which the velocity of the reaction is half of the maximum velocity (Vmax). A high KM value indicates weak binding between the enzyme and the substrate, while a low KM indicates strong binding. Vmax represents the maximum initial rate of the reaction when all enzyme active sites are saturated. It is important to note that the Michaelis-Menten equation provides an approximate value of Vmax, not the exact value.