The Classic Case Michaelis-Menten Equation

Even the simplest enzyme reaction consists of at least a binding and a catalytic step. The simplest kinetic representation resulting from a reversible binding step, followed by an irreversible catalytic step, is written in Eq. (5.1). 

The rate law, containing just observables, following from the kinetics in Eq. (5.1) is obtained in the most general way in four steps  

identification of the product formation rate or substrate consumption rate [Eq. (5.2)]  

writing steady-state balances for each species [Eqs. (5.3)]—(5.6)]  

The Michaelis-Menten equation, especially if derived with the steady-state concept as above, is a rigorous rate law which not only fits almost all one-substrate enzyme kinetics, except in the case of inhibition (see Section 5.3), but also allows identification of the kinetic constants with the elementary steps in Eq. (5.1). 

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