The Michaelis-Menten constant (KM) has the following characteristics, EXCEPT: The dimension for Km is concentration such as molarity It is the substrate concentration necessary to reach 1/2 Vmax O It is equal to 1/2 Vmax It is similar to the affinity constant between enzyme and substrate. The Michaelis-Menten Constant (KM): Characteristics and Implications

The Michaelis-Menten Constant KM (KM): Features and Implications

The Michaelis-Menten constant is an important parameter in enzyme kinetics. It provides information about the speed of enzyme reactions. KM is a measurement of enzyme efficiency. It indicates how much substrate the enzyme needs to function at a given rate. The enzyme’s affinity for the substrate is measured by KM. This constant is often called the Michaelis constant, after its discovery in 1913 by German biochemists Maud Menten and Leonor Michaelis. KM can be used to measure the effectiveness of enzyme-catalyzed reaction efficiency. It’s a key parameter in enzyme efficiency. It measures the enzyme’s affinity to its substrate. KM values help to identify the kinetic parameters in enzymatic reaction. They include reaction rates, maximum reactions rates and effects of pH, temperature, on enzyme activity. (Kan, 2020). The KM value can be used to determine the specificity of an enzyme for a given substrate and identify its active sites (Kan et al. 2020). Cont…..

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