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The Michaelis constant, denoted as (K_M), is a key concept in Michaelis-Menten kinetics, which describes the rate of enzyme-catalyzed reactions. It represents the substrate concentration at which an enzyme-catalyzed reaction proceeds at half of its maximum velocity ((V_M)).123

Essentially, the Michaelis constant provides a measure of the affinity between an enzyme and its substrate. A lower (K_M) value indicates a higher affinity, meaning the enzyme can reach half its maximum rate with a lower concentration of substrate. Conversely, a higher (K_M) suggests a lower affinity. This concept is fundamental to understanding how enzymes function and how their activity is regulated in biological systems.231

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