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Research Report SRR95-001
Cofactor Modifications To Michaelis Menten Kinetics
Henry C. Tuckwell
Abstract:
In order to construct mathematical models for the dynamical operation of central
nervous system synapses, accurate chemical kinetic theory is required for
enzymatic
reactions. The Michaelis-Menton formula for the rate of an enzymatic reaction
is modified when there are cofactors involved. We distinguish the cases of
essential and non-essential cofactors. In the case of an essential cofactor,
the formula for the reaction rate is found to depend on the relative magnitudes
of the concentrations of the primary enzyme and the cofactor, extending a result
previously employed by various authors. The case of a non-essential cofactor
is more complex and leads to reaction rate formulas which depend explicitly
on the concentration of both the primary enzyme and the cofactor. The relative
magnitudes of the concentrations of the latter two substances again determines
the functional dependence of the reaction rate on these quantities. Simplified
expressions are obtained under certain assumptions on a parameter describing
the relative efficacies of the enzyme alone and the enzyme with cofactor.
An example is given which arises from a mathematical model of a dopaminergic
synapse, namely the conversion of tyrosine to DOPA via tyrosine hydroxylase and
its biopterin cofactor.
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