MichaelisMentenmallin

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, [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 Km value provides insight into the affinity of the enzyme for its substrate. A lower Km indicates a higher affinity. The Michaelis-Menten model is widely used in biochemistry and pharmacology to study enzyme kinetics and drug action. However, it has limitations, such as assuming a single substrate and not accounting for allosteric effects or enzyme inhibition. Despite these limitations, the Michaelis-Menten model remains a fundamental concept in understanding enzyme-catalyzed reactions.