Michaelis-Menten kinetics models substrate binding to an enzyme, complex dissociation and product formation. Under the relevant quasi-steady-state regime, its initial-rate law is the saturating relation given by the following equation.
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Michaelis–Menten kinetics is a model that describes the rate of enzyme-catalyzed reactions. It provides a mathematical framework to understand how enzymes interact with substrates and how the reaction rate depends on substrate concentration. This model was developed by Canadian biochemist Leonor Michaelis and German chemist Maud Menten in 1913.