Km and Vmax: What’s the Difference?

Km and Vmax are two important parameters used in enzyme kinetics to describe the behavior of an enzyme-catalyzed reaction.

Km (Michaelis constant) is a measure of how well an enzyme binds to its substrate. It represents the substrate concentration at which the reaction rate is half of its maximum value. In other words, it is the concentration of substrate at which the enzyme is working at half of its maximum velocity. The Km value is dependent on both the enzyme and the substrate being used in the reaction. The lower the Km value, the higher the affinity of the enzyme for the substrate.

On the other hand, Vmax (maximum velocity) is a measure of the maximum rate of reaction that can be achieved under saturating substrate concentrations. It represents the maximum number of substrate molecules that an enzyme can convert into product per unit of time, when all enzyme active sites are fully occupied by substrate. The Vmax value is dependent on the enzyme concentration and the reaction conditions.

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