Effect of substrate concentration on enzyme action
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Answer:
Enzymes will work best if there is plenty of substrate. As the concentration of the substrate increases, so does the rate of enzyme activity. However, the rate of enzyme activity does not increase forever..
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A simple chemical reaction with a single substrate shows a linear relationship between the rate of formation of product and the concentration of substrate, as shown below:
For an enzyme-catalysed reaction, there is usually a hyperbolic relationship between the rate of reaction and the concentration of substrate, as shown below:
(A) At low concentration of substrate, there is a steep increase in the rate of reaction with increasing substrate concentration. The catalytic site of the enzyme is empty, waiting for substrate to bind, for much of the time, and the rate at which product can be formed is limited by the concentration of substrate which is available.
(B) As the concentration of substrate increases, the enzyme becomes saturated with substrate. As soon as the catalytic site is empty, more substrate is available to bind and undergo reaction. The rate of formation of product now depends on the activity of the enzyme itself, and adding more substrate will not affect the rate of the reaction to any significant effect.
The rate of reaction when the enzyme is saturated with substrate is the maximum rate of reaction, Vmax.
The relationship between rate of reaction and concentration of substrate depends on the affinity of the enzyme for its substrate. This is usually expressed as the Km (Michaelis constant) of the enzyme, an inverse measure of affinity.
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