What is the equation represented by the Michaelis-Menton equation?

The Michaelis-Menten equation describes the rate of enzymatic reactions by relating the reaction velocity to substrate concentration. The correct formulation is V0 = (Vmax * S) / (Km + [S]), where V0 represents the initial reaction velocity, Vmax is the maximum velocity of the reaction when the enzyme is saturated with substrate, Km is the Michaelis constant, which indicates the substrate concentration at which the reaction velocity is half of Vmax, and [S] is the concentration of the substrate.

In this equation, as the substrate concentration increases, the reaction velocity approaches Vmax asymptotically. This relationship is fundamental to understanding enzyme kinetics because it illustrates how the availability of substrate affects the speed of the reaction. The Michaelis constant (Km) provides insight into the affinity of the enzyme for the substrate: a lower Km indicates a higher affinity.

The other formulations do not correctly represent the relationship modeled by the Michaelis-Menten equation. Some incorrectly manipulate the relationship between enzyme saturation and substrate concentration or misplace the terms in the denominator or numerator, which leads to misconceptions in enzyme kinetics. Understanding this equation helps in various applications, such as drug development and metabolic pathway studies.