The Michaelis-Menten mechanism of enzyme catalysis

Because enzyme-controlled reactions are so Important In biochemistry, we need to build a model of their mechanism. The simplest approach proposed by MIchaells and Menten Is our starting point. 

Experimental studies of enzyme kinetics are typically conducted by monitoring the initial rate of product formation in a solution in which the enzyme is present at very low concentration. Indeed, enzymes are such efficient catalysts that significant accelerations may be observed even when their concentrations are more than three orders of magnitude smaller than those of their substrates. 

The principal features of many enzyme-catalyzed reactions are as follows (Fig. 8.2)  

For a given initial concentration of substrate, [S]o, the initial rate of product formation is proportional to the total concentration of enzyme, [E]q. 

For a given [E]q and high values of [S]o, the rate of product formation becomes independent of [S]o, reaching a maximum value known as the maximum velocity, 

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