MichaelisMentenkäyrää

Michaelis-Menten kinetics describes the rate of enzyme-catalyzed reactions. It is named after Leonor Michaelis and Maud Menten, who proposed the model in 1913. The model is based on the assumption that the enzyme (E) and substrate (S) combine reversibly to form an enzyme-substrate complex (ES), which then undergoes a slow breakdown to form product (P) and free enzyme. The reaction can be represented as: E + S <=> ES -> E + P.

The Michaelis-Menten equation relates the initial reaction velocity (v) to the initial substrate concentration ([S]). It is given by v = (Vmax * [S]) / (Km + [S]), where Vmax is the maximum reaction velocity achieved when the enzyme is saturated with substrate, and Km is the Michaelis constant. Km represents the substrate concentration at which the reaction velocity is half of Vmax. A lower Km indicates a higher affinity of the enzyme for its substrate.

The Michaelis-Menten equation assumes several conditions: the substrate concentration is much higher than the enzyme concentration, the reaction is carried out at constant temperature and pH, and the reverse reaction is negligible. This model is fundamental to understanding enzyme kinetics and is widely used in biochemistry and pharmacology to characterize enzyme behavior and drug interactions. The graphical representation of this equation, plotting initial velocity against substrate concentration, yields a hyperbolic curve.