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Non-Competitive Inhibitors

Non-competitive inhibitors bind to a site which is not the active site.This binding to the allosteric site changes the tertiary structure(shape) of the enzyme's active site and the substrate is no longer complementary to the shape of the active site.Increasing the substrate concentration on the inhibited enzymes has no effect on the rate of reaction. The rate of reaction does not reach its maximum Vmax.

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Specification: AQA Biology (7401), AS-level, 3.1.4.2 Many proteins are enzymes. Topic: Enzymes.

Key terms in this lesson

tertiary structure
The further coiling and folding of a polypeptide into a specific three-dimensional shape, held by ionic bonds, hydrogen bonds and disulfide bridges between R-groups.
active site
The region of an enzyme, formed by the tertiary structure, with a shape complementary to its substrate, where the substrate binds.
competitive inhibitor
A molecule with a shape similar to the substrate that binds to the active site, reducing the number of enzyme-substrate complexes formed.

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