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1.4.7 Limiting Factors Affecting Enzymes
infoNote
The rate of enzyme-controlled reactions is influenced by several factors that can limit enzyme activity if not at optimal levels. These limiting factors include temperature, pH, enzyme concentration, substrate concentration, and inhibitors.
Key Limiting Factors:
Temperature:
As temperature increases, the rate of reaction increases up to the enzyme's optimum temperature due to increased kinetic energy and more frequent enzyme-substrate collisions.
Above the optimum temperature, the rate declines as enzymes become denatured, losing their functional shape.
pH:
Each enzyme has an optimum pH. Deviations from this pH can disrupt the bonds in the enzyme's tertiary structure, altering the active site and reducing activity.
Extreme pH levels can lead to denaturation. For instance, pepsin works best in the acidic conditions of the stomach.
Enzyme Concentration:
Increasing enzyme concentration increases the rate of reaction, as more active sites are available for substrates to bind.
Beyond a certain point, the reaction rate plateaus as substrate concentration becomes the limiting factor.
Substrate Concentration:
Increasing substrate concentration increases the rate of reaction as more enzyme-substrate complexes form.
Once all active sites are occupied, increasing substrate concentration further will not increase the rate, as enzyme concentration becomes the limiting factor.
Inhibitors:
Competitive Inhibitors: These inhibitors compete with the substrate for the enzyme's active site. As their concentration increases, the rate of reaction decreases, as active sites are temporarily blocked.
Non-Competitive Inhibitors: These bind to a different site on the enzyme, causing a change in the enzyme's shape and active site. This reduces the reaction rate, as the substrate can no longer bind effectively.
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