BRAINCAKEReversible and Irreversible Inhibition
An inhibitor is a substance that binds to an enzyme and reduces its activity. Inhibitors can be classed by how strongly and how permanently they bind.
Reversible inhibitors bind to the enzyme by weak bonds, such as hydrogen bonds and ionic bonds. They bind and leave again, so the enzyme is only inactive while the inhibitor is attached. If the inhibitor is removed (for example by dialysis or by being broken down), full enzyme activity returns. Competitive and non-competitive inhibitors can both be reversible. Many drugs and the cell's own control molecules are reversible inhibitors.
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Key terms in this lesson
- competitive inhibitor
- A molecule with a shape similar to the substrate that binds reversibly to an enzyme's active site, reducing the rate of reaction.
- non-competitive inhibitor
- A molecule that binds to a site other than the active site, changing the enzyme's shape so the substrate can no longer bind.
More in Enzymes
- Measuring Rate of Reaction
- Effect of Substrate Concentration
- Effect of Temperature
- Effect of pH
- Effect of Enzyme Concentration
- Competitive Inhibition
- Non-competitive Inhibition
- End-Product Inhibition
All 14 lessons in Enzymes · All Edexcel AS-level Biology topics