The Michaelis-Menten Constant KM (KM): Features and Implications
The Michaelis–Menten constant (KM), is an important parameter for enzyme kinetics. This gives insight into the rates of enzyme reactions. KM measures enzyme efficiency by indicating how much substrate is required for enzymes to operate at a specific rate. The enzyme’s affinity for the substrate is measured by KM. Because it was discovered by Leonor Michaelis, a German biochemist and Maud Menten, it is known also as the Michaelis constant. KM can be used to measure the effectiveness of enzyme-catalyzed reaction efficiency. This parameter is a measure of enzyme efficiency. It is directly related to enzyme affinity for substrate. KM values can be used to determine the kinetic parameters for enzymatic reactions such as the reaction rates and maximum rates of reaction, as well the effect of temperature and pH on enzyme activity (Kan et. al. 2020). The KM value can be used to determine the specificity of an enzyme for a given substrate and identify its active sites (Liu, et al. 2016). Cont…..
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