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Home » Biology Homework Help » Biotechnology » Enzyme Kinetics
Enzyme Kinetics
The rate of reaction catalyzed by an enzyme increases linearly with the substrate concentration upto a point, but it soon reaches the maximum value called Vmax beyond which there is no further increase in reaction rate; this is called saturation. In contrast, the rate of a nonenzymatically catalyzed reaction increases linearly over the entire range of attainable substrate concentrations. The phenomenon of substrate saturation is described by the Michaelis-Menten equation given below:



where, Vmax is the maximum rate of reaction, which occurs when the enzyme is saturated with substrate, v is the rate of reaction, [S] is the substrate concentration and Km is Michaelis constant. This equation can be used to predict the rate of reaction catalyzed by an enzyme at any substrate concentration provided the values of Vmax and Km are known. Km is the substrate concentration needed to obtain a reaction rate equal to ½ Vmax. The substrate concentrations and reaction rates considered in the above equation are always the initial values, i.e. the values at the start of the reaction.

Although few enzymes follow the Michaelis-Menten equation over a wide range of experimental conditions, it is still the most generally applicable equation for describing enzyme catalyzed reactions. The value of Km is characteristic for each enzyme substrate combination, but is independent of the enzyme and/or substrate concentrations. However, Km may be influenced by pH, temperature, ionic strength and other factors.

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