Michaelis–Menten Kinetics
Here, the rate of reaction becomes dependent on the ES complex and the reaction becomes a unimolecular reaction with an order of zero. Though the
enzymatic mechanism for the unimolecular reaction
can be quite complex, there is typically one rate-determining enzymatic step that
allows this reaction to be modelled as a single catalytic step with an apparent unimolecular rate constant Kcat.
If the reaction path proceeds over one or several intermediates, Kcat will be a function of several elementary rate constants, whereas in the simplest case
of a single elementary reaction (e.g. no intermediates) it will be identical to the elementary unimolecular rate constant K2.
The apparent unimolecular rate constant Kcat is also
called turnover number and denotes the maximum
number of enzymatic reactions catalysed per second.
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