Final answer:
The Michaelis-Menten equation describes how the initial velocity of an enzyme-catalyzed reaction depends on substrate concentration, reaching a maximum rate (Vmax) when the enzyme is saturated. The equation is v = (Vmax[S])/(Km + [S]), where Km is the substrate concentration at which the reaction rate is half the Vmax, indicating the enzyme's affinity for its substrate.
Step-by-step explanation:
The Michaelis-Menten equation is a mathematical representation of the relationship between the initial velocity (v0) of an enzymatic reaction and the substrate concentration ([S]). According to this equation, the reaction velocity increases with substrate concentration but approaches a maximum value, known as Vmax, as the enzyme becomes saturated with substrate. At this point, all active sites of the enzyme are occupied, and the rate of the reaction is limited by the rate at which the enzyme can convert substrate to product.
The Michaelis-Menten equation can be expressed as:
v = \( \frac{V_{max}[S]}{K_m + [S]} \)
Where Vmax represents the maximum rate of the reaction, and Km, the Michaelis constant, is the substrate concentration at which the reaction velocity is half the maximum velocity. An enzyme with a lower Km value has a higher affinity for its substrate, as it reaches half of Vmax at a lower substrate concentration.
The Michaelis-Menten plot graphs reaction velocity as a function of substrate concentration, typically resulting in a hyperbolic curve. This graphical representation helps researchers determine the key kinetic parameters Vmax and Km for a given enzymatic reaction.