Michaelis-Menten Kinetics Overview
The Michaelis-Menten model describes the rate of enzyme-catalyzed reactions. The fundamental equation is:
Where:
- is the reaction velocity.
- is the maximum velocity of the reaction when the enzyme is fully saturated with substrate.
- is the substrate concentration.
- is the Michaelis constant, representing the substrate concentration at which the reaction rate is half of .
Mixed-Order Kinetics
In the context of Michaelis-Menten kinetics:
First-Order Kinetics: When the substrate concentration is much less than (i.e., ), the term in the denominator is approximately equal to . Therefore, the Michaelis-Menten equation simplifies to:
This means the reaction rate is directly proportional to the substrate concentration , which is the hallmark of first-order kinetics.
Zero-Order Kinetics: When the substrate concentration is much greater than (i.e., ), the term is approximately equal to . Therefore, the Michaelis-Menten equation simplifies to:
Here, the reaction rate approaches and becomes independent of the substrate concentration. This is characteristic of zero-order kinetics, where the rate is constant and does not depend on the concentration of the reactant.
Summary of Mixed Order
First-Order Kinetics: At low substrate concentrations, the reaction rate is dependent on the substrate concentration, and the kinetics appear first-order.
Zero-Order Kinetics: At high substrate concentrations, the reaction rate approaches a maximum value ( ) and becomes independent of substrate concentration, showing zero-order kinetics.
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