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Michaelis-Menten and Similar Kinetics

Suppose the reaction S — P occurs using an enzyme as a catalyst. The following reaction mechanism is postulated  [Pg.436]

FIGURE 12.1 Effects of substrate (reactant) concentration on the rate of enzymatic reactions (a) simple Michaelis-Menten kinetics (b) substrate inhibition (c) substrate activation. [Pg.437]

Example 12.1 Suppose an enzymatic reaction has the following mechanism  [Pg.438]

The two equilibrium relations and the rate expression allow the unknown surface concentrations [S E], [SE], and [E] to be eliminated. The result is [Pg.438]

This equation gives (0) = 0, a maximum at =. /Km/K2, and (oo) = 0. The assumed mechanism involves a first-order surface reaction with inhibition of the reaction if a second substrate molecule is adsorbed. A similar functional form for (s) can be obtained by assuming a second-order, dual-site model. As in the case of gas-solid heterogeneous catalysis, it is not possible to verify reaction mechanisms simply by steady-state rate measurements. [Pg.438]


See other pages where Michaelis-Menten and Similar Kinetics is mentioned: [Pg.436]    [Pg.436]    [Pg.436]   


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