The Michaelis–Menten mechanism is the simplest mechanism that will explain
Michaelis–Menten kinetics According to the mechanism, a substrate A first combines with a molecule of enzyme
E, and this process is followed by a step in which the enzyme-substrate complex EA
breaks down (sometimes with the participation of the solvent) into enzyme and reaction
products:
If, as is usual, the substrate A is present in great excess of the enzyme it can be
shown that steady-state conditions apply, and that the rate equation is:
where
is the total concentration of enzyme. This equation is of the form of the Michaelis–Menten
equation. Other, more complicated, mechanisms lead to the Michaelis–Menten equation,
adherence to which therefore does not require that the Michaelis– Menten mechanism
applies.
Source:
PAC, 1996, 68, 149
(A glossary of terms used in chemical kinetics, including reaction dynamics (IUPAC
Recommendations 1996))
on page 172
Cite as:
IUPAC. Compendium of Chemical Terminology, 2nd ed. (the "Gold Book"). Compiled by
A. D. McNaught and A. Wilkinson. Blackwell Scientific Publications, Oxford (1997).
XML on-line corrected version: http://goldbook.iupac.org (2006-) created by M. Nic,
J. Jirat, B. Kosata; updates compiled by A. Jenkins. ISBN 0-9678550-9-8.
https://doi.org/10.1351/goldbook.