Michaelis–Menten kinetics

In biochemistry, Michaelis–Menten kinetics, named after Leonor Michaelis and Maud Menten, is the simplest case of enzyme kinetics, applied to enzyme-catalysed reactions involving the transformation of one substrate into one product. It takes the form of a differential equation describing the reaction rate ${\displaystyle v}$ (rate of formation of product P, with concentration ${\displaystyle p}$) as a function of ${\displaystyle a}$, the concentration of the substrate  A (using the symbols recommended by the IUBMB). Its formula is given by the Michaelis–Menten equation:

${\displaystyle v={\frac {\mathrm {d} p}{\mathrm {d} t}}={\frac {Va}{K_{\mathrm {m} }+a}}}$

${\displaystyle V}$, which is often written as ${\displaystyle V_{\max }}$, represents the limiting rate approached by the system at saturating substrate concentration for a given enzyme concentration. The Michaelis constant ${\displaystyle K_{\mathrm {m} }}$ has units of concentration, and for a given reaction is equal to the concentration of substrate at which the reaction rate is half of ${\displaystyle V}$. Biochemical reactions involving a single substrate are often assumed to follow Michaelis–Menten kinetics, without regard to the model's underlying assumptions. Only a small proportion of enzyme-catalysed reactions have just one substrate, but the equation still often applies if only one substrate concentration is varied.