MichaelisMentenkonstant

The Michaelis-Menten constant, often denoted as Km, is a fundamental parameter in enzyme kinetics. It represents the substrate concentration at which an enzyme-catalyzed reaction proceeds at half of its maximum velocity (Vmax). In simpler terms, Km indicates the affinity of an enzyme for its substrate. A low Km value signifies a high affinity, meaning the enzyme can efficiently bind to and process the substrate even at low concentrations. Conversely, a high Km value indicates a low affinity, requiring a higher substrate concentration for the enzyme to reach half of its maximal catalytic rate.

The Michaelis-Menten equation, v = (Vmax * [S]) / (Km + [S]), describes the relationship between reaction velocity (v), maximum velocity (Vmax), substrate concentration ([S]), and the Michaelis-Menten constant (Km). This equation is a cornerstone for understanding how enzymes function and how their activity is influenced by substrate availability. Km is a constant for a specific enzyme and substrate under defined conditions, such as temperature and pH. It is an experimentally determined value and provides valuable insights into the enzyme's catalytic efficiency and its role within metabolic pathways. Variations in Km can also be indicative of enzyme inhibition or changes in enzyme structure.