Michaellisäykset

Michaellisäykset, also known as Michaelis-Menten kinetics, is a fundamental concept in enzymology that describes the rate of enzymatic reactions. It is named after Leonor Michaelis and Maud Menten, who proposed the model in 1913. The model describes the relationship between the initial velocity of an enzyme-catalyzed reaction and the concentration of the substrate.

The Michaellis-Menten equation is expressed as V = (Vmax * [S]) / (Km + [S]), where V is the initial reaction velocity, Vmax is the maximum reaction velocity, [S] is the substrate concentration, and Km is the Michaelis constant. Km represents the substrate concentration at which the reaction velocity is half of Vmax. It is an important indicator of the enzyme's affinity for its substrate; a lower Km value signifies a higher affinity.

The model assumes several key conditions: the reaction is irreversible, the concentration of the enzyme is much lower than the substrate concentration, and the system is at steady state, meaning the rate of formation of the enzyme-substrate complex equals the rate of its breakdown. While a simplification of real enzymatic processes, Michaellis-Menten kinetics provides a valuable framework for understanding enzyme behavior and is widely used in biochemistry and pharmacology to study enzyme mechanisms and drug interactions.