Michaelis-Menten kinetics

Michaelis-Menten kinetics is a model of enzyme kinetics. It was named after Leonor Michaelis and Maud Menten. The model takes the form of an equation that describes the rate of enzymatic reactions. This model is used in various scientific fields, including biochemistry, pharmacology, and systems biology.

Overview

The Michaelis-Menten model is used to analyze the rate at which enzymes react with substrates to form products. The model assumes that the enzyme and substrate form a complex in a reversible reaction, and that the complex then irreversibly decomposes to release the product and regenerate the enzyme.

The rate of product formation is given by the Michaelis-Menten equation:

v = (V_max[S]) / (K_m + [S])

where:

• v is the rate of the reaction
• V_max is the maximum rate achieved by the system
• [S] is the concentration of the substrate
• K_m is the Michaelis constant

Michaelis constant

The Michaelis constant (K_m) is a key parameter in the Michaelis-Menten model. It is defined as the substrate concentration at which the reaction rate is half of V_max. The K_m value provides important information about the affinity of the enzyme for its substrate: a lower K_m indicates a higher affinity.

Applications

The Michaelis-Menten model is widely used in various scientific fields. In biochemistry, it is used to study enzyme kinetics and to design drugs that can inhibit enzyme activity. In pharmacology, it is used to understand drug interactions and to predict the effects of drug dosage changes. In systems biology, it is used to model complex biological systems and to analyze the dynamics of metabolic networks.

See also

• Enzyme kinetics
• Enzyme inhibition
• Lineweaver-Burk plot
• Eadie-Hofstee diagram

References

Michaelis-Menten kinetics Resources
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