The Michaelis-Menten equation is a mathematical equation that describes the relationship between the reaction rate of an enzyme-catalyzed reaction and the concentration of the substrate. It is named after Leonor Michaelis and Maud Menten, who proposed this model in 1913.
The equation is as follows:
v = (Vmax * [S]) / (Km + [S])
Where:
- v is the reaction rate (velocity) of the enzyme-catalyzed reaction.
- Vmax is the maximum reaction rate when the enzyme is fully saturated with substrate.
- [S] is the concentration of the substrate.
- Km is the Michaelis constant, which represents the substrate concentration at which the reaction rate is half of Vmax.
The Michaelis-Menten equation assumes that the enzyme-substrate complex forms reversibly and that the rate-determining step is the breakdown of the enzyme-substrate complex to form the product.
The equation allows us to understand the relationship between substrate concentration and the reaction rate. At low substrate concentrations ([S] << Km), the reaction rate is directly proportional to the substrate concentration, and the enzyme is considered to be operating under "first-order kinetics" with respect to the substrate. As the substrate concentration increases, the reaction rate eventually reaches a maximum value (Vmax) when the enzyme is saturated with substrate.
The Km value is an important parameter that represents the affinity of the enzyme for the substrate. A lower Km indicates a higher affinity, as it reflects a lower substrate concentration required for the enzyme to achieve half of its maximum reaction rate.
The Michaelis-Menten equation is widely used in enzyme kinetics studies to determine enzyme parameters, assess enzyme activity, and understand the behavior of enzyme-catalyzed reactions.
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