Скачать или смотреть Michaelis Menten Equation Explained For Beginners

The Michaelis-Menten equation is a mathematical model that describes the rate at which an enzyme catalyzes a chemical reaction. It is based on the idea that enzymes work by binding to their substrate (the chemical that they are acting on) and then converting it into a product. As the amount of substrate decreases with time, the amount of product increases with time.

The equation is written as:

v = Vmax[S]/(Km + [S])

Where:

v is the rate of the reaction (as measured by the formation of product)
Vmax is the maximum velocity of the reaction, which is the rate of the reaction when the enzyme is fully saturated with substrate
[S] is the concentration of substrate
Km is the Michaelis constant, which is a measure of the affinity of the enzyme for the substrate. It is equal to the substrate concentration at which the enzyme is working at half of its maximum velocity.

The equation describes how the rate of the reaction (v) changes as the substrate concentration ([S]) changes. At low substrate concentrations, the rate of the reaction is relatively slow because there are not enough substrate molecules present for the enzyme to work on. As the substrate concentration increases, the rate of the reaction increases until it reaches a maximum (Vmax). Beyond this point, increasing the substrate concentration does not increase the rate of the reaction because the enzyme is already working at its maximum capacity.

The Michaelis constant (Km) represents the substrate concentration at which the enzyme is working at half of its maximum velocity. If Km is large, it means that the enzyme has a low affinity for the substrate and requires a higher substrate concentration to reach its maximum velocity. If Km is small, it means that the enzyme has a high affinity for the substrate and can reach its maximum velocity at a lower substrate concentration.

The Michaelis-Menten equation is useful for understanding how enzymes work and how they can be affected by changes in substrate concentration and other factors. It is often used in biochemistry and pharmacology to study the kinetics of enzyme-catalyzed reactions.