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A-Level Biology OCR A

Inhibitor Enzyme Active Site Substrate Non Competetive Rate Shape

Non-competitive inhibitors bind to allosteric sites, changing active site shape and reducing functional enzyme numbers, thus slowing the reaction.

Non-competitive inhibitors bind to allosteric sites, altering the active site's shape and reducing the enzyme's effectiveness; this reduces the number of available active sites.

Front Explain how a non-competetive inhibitor affects the rate of an enzyme-controlled reaction.
Back Effect of non-competetive inhibitors:
  • Inhibitor binds to enzyme at allosteric site
  • Binding of inhibitor causes tertiary structure of enzyme to change, active site changes shape
  • Active site no longer has complementary shape to substrate so substrate is unable to bind to enzyme
  • Enzyme cannot carry out function - inhibited
  • The inhibitor does not compete with the substrate for the active site 
  • Number of available active sites is reduced permanently, less molecules bind to them in given time, rate of reaction reduced

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