Abstract
Based on our experience in kinetic modeling of coupled multiple metabolic pathways, we propose a generic rate equation for the dynamical modeling of metabolic kinetics. It is symmetric for forward and backward reactions. Its Michaelis-Menten-King-Altman form makes the kinetic parameters (or functions) easy to relate to experimental values in the database and to use in computation. In addition, such a uniform form is ready to arbitrary number of substrates and products with different stiochiometry. We explicitly show how to obtain such rate equations rigorously for three well-known binding mechanisms. Hence, the proposed rate equation is formally exact under the quasi-steady state condition. Various features of this generic rate equation are discussed. In particular, for irreversible reactions, the product inhibition which directly arises from enzymatic reaction is eliminated in a natural way. We also discuss how to include the effects of modifiers and cooperativity.
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