Substratmenge

Substratmenge refers to the total amount of substrate available to an enzyme for a particular reaction. It is a fundamental concept in enzymology and is directly related to the rate at which an enzyme can catalyze a reaction. When the substrate concentration is low, the reaction rate is directly proportional to the substrate amount; as more substrate is added, the rate increases. However, at a certain point, the enzyme becomes saturated with substrate. This means all active sites of the enzyme molecules are occupied by substrate molecules, and the enzyme is working at its maximum velocity. Adding more substrate beyond this saturation point will not increase the reaction rate. The relationship between substrate concentration and reaction velocity is often described by the Michaelis-Menten kinetics model. The Michaelis constant, Km, is a key parameter in this model and represents the substrate concentration at which the reaction rate is half of the maximum velocity (Vmax). A lower Km indicates a higher affinity of the enzyme for its substrate, meaning it can achieve half-maximal velocity at a lower substrate concentration. Understanding substratmenge is crucial for determining optimal conditions for enzymatic reactions in research, industrial processes, and biological systems.