MichaeliseMenten

Michaelis-Menten kinetics is a mathematical model used to describe the rate of an enzyme-catalyzed reaction. It was developed by Leonor Michaelis and Maud Menten in 1913. The model assumes that the enzyme and substrate form a reversible complex, and the rate of the reaction is proportional to the concentration of this complex.

The Michaelis-Menten equation is given by:

V = (Vmax * [S]) / (Km + [S])

where V is the initial velocity of the reaction, Vmax is the maximum velocity when all enzyme is saturated with substrate, [S] is the substrate concentration, and Km is the Michaelis constant, which is the substrate concentration at which the reaction rate is half of Vmax.

The Michaelis-Menten model has several assumptions, including that the enzyme is homogeneous and that the substrate binds to a single site on the enzyme. It also assumes that the enzyme-substrate complex breaks down to form products and free enzyme.

The model has been widely used in biochemistry and pharmacology to describe enzyme kinetics and drug action. However, it has limitations, such as not accounting for allosteric effects or multiple substrate binding sites. Despite these limitations, the Michaelis-Menten model remains a fundamental concept in understanding enzyme-catalyzed reactions.