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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.
[A] can provide intuitive insight about the order of each of the reagents. If plots of v / [A] vs. [B] overlay for multiple experiments with different-excess, the data are consistent with a first-order dependence on [A]. The same could be said for a plot of v / [B] vs. [A]; overlay is consistent with a first-order dependence on [B].
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 involving the transformation of one substrate into one product.
The rate is first-order in one reactant (ethyl acetate), and also first-order in imidazole, which as a catalyst does not appear in the overall chemical equation. Another well-known class of second-order reactions are the S N 2 (bimolecular nucleophilic substitution) reactions, such as the reaction of n-butyl bromide with sodium iodide in acetone:
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.
The graph for the non-linear relationship between the various factors is represented by a curve; the relationships between the factors can then be found by calculating the dimensions of different areas under the curve. The models used in non-linear pharmacokinetics are largely based on Michaelis–Menten kinetics. A reaction's factors of non ...
In enzyme kinetics, a secondary plot uses the intercept or slope from several Lineweaver–Burk plots to find additional kinetic constants. [1] [2]For example, when a set of v by [S] curves from an enzyme with a ping–pong mechanism (varying substrate A, fixed substrate B) are plotted in a Lineweaver–Burk plot, a set of parallel lines will be produced.
Although the net formula for decomposition or isomerization appears to be unimolecular and suggests first-order kinetics in the reactant, the Lindemann mechanism shows that the unimolecular reaction step is preceded by a bimolecular activation step so that the kinetics may actually be second-order in certain cases. [7]