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Curve of the Michaelis–Menten equation labelled in accordance with IUBMB recommendations. In biochemistry, Michaelis–Menten kinetics, named after Leonor Michaelis and Maud Menten, is the simplest case of enzyme kinetics, applied to enzyme-catalysed reactions of one substrate and one product.
Michaelis–Menten kinetics for enzyme-catalysis: first-order in substrate (second-order overall) at low substrate concentrations, zero order in substrate (first-order overall) at higher substrate concentrations; and; the Lindemann mechanism for unimolecular reactions: second-order at low pressures, first-order at high pressures.
The observed velocities predicted by the Michaelis–Menten equation can be used to directly model the time course disappearance of substrate and the production of product through incorporation of the Michaelis–Menten equation into the equation for first order chemical kinetics.
The best known plots of the Michaelis–Menten equation, including the double-reciprocal plot of / against /, [2] the Hanes plot of / against , [3] and the Eadie–Hofstee plot [4] [5] of against / are all plots in observation space, with each observation represented by a point, and the parameters determined from the slope and intercepts of the lines that result.
While e may be any value (positive, negative, or zero) generally positive or negative values smaller in magnitude than one equivalent of substrate are used in reaction progress kinetic analysis. (One might note that pseudo-zero-order kinetics uses excess values much much greater in magnitude than the one equivalent of substrate).
The Monod equation is a mathematical model for the growth of microorganisms. It is named for Jacques Monod (1910–1976, a French biochemist, Nobel Prize in Physiology or Medicine in 1965), who proposed using an equation of this form to relate microbial growth rates in an aqueous environment to the concentration of a limiting nutrient.
[1] [2] Thus, the rate equation is often shown as having first-order dependence on the substrate and zero-order dependence on the nucleophile. This relationship holds for situations where the amount of nucleophile is much greater than that of the intermediate. Instead, the rate equation may be more accurately described using steady-state kinetics.
For Michaelis–Menten–Monod (MMM) kinetics it is intended the coupling of an enzyme-driven chemical reaction of the Michaelis–Menten type [1] with the Monod growth of an organisms that performs the chemical reaction. [2]