Michaelis–Menten Kinetics

A kinetic description for many single‑substrate enzyme‑catalyzed reactions in which the steady‑state assumption for the enzyme–substrate complex yields a hyperbolic relationship between initial reaction velocity v and substrate concentration [S] parameterized by Vmax (maximum rate at enzyme saturation) and Km (the Michaelis constant), with v = (Vmax [S])/(Km + [S]) under the model's assumptions.

A kinetic model that describes the initial rate v of a single‑substrate enzyme‑catalyzed reaction under steady‑state conditions by the equation v = (Vmax [S])/(Km + [S]), where Vmax is the maximal rate, Km is the substrate concentration at half Vmax, and the enzyme–substrate complex is assumed to have approximately constant concentration during measurement.