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Answer :
Final answer:
There are three types of enzyme inhibitors: competitive, noncompetitive, and allosteric inhibitors. Competitive inhibitors bind to the active site, noncompetitive inhibitors bind to an allosteric site, and allosteric inhibitors also bind to an allosteric site.
Explanation:
There are three types of enzyme inhibitors: competitive inhibitors, noncompetitive inhibitors, and allosteric inhibitors. Competitive inhibitors bind to the active site of the enzyme and compete with the substrate for binding. Noncompetitive inhibitors bind to an allosteric site on the enzyme, causing a conformational change that prevents the substrate from binding. Allosteric inhibitors also bind to an allosteric site and induce a conformational change that reduces the enzyme's affinity for the substrate.
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The types of enzyme inhibitors are broken down into three basic categories: non-competitive, competitive, and uncompetitive.
The competitive inhibitor and the substrate share a structure with which they can match, analogous to the idea of a jigsaw puzzle.
The noncompetitive inhibitor binds away from the enzyme's active site. In order to prevent the substrate from entering the active site or inhibit catalytic activity, the irreversible/permanent inhibitor forms a covalent bond with an amino acid side group within the active site. The competitive inhibitor attaches itself to the enzyme at the Active Site. It is true that the shape is distorted when the noncompetitive inhibitor binds to the enzyme. Enzyme inhibitors disrupt an enzyme's interaction with its substrate.
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