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Answer :
Enzyme inhibitors inhibit enzyme catalysis and include;
- Competitive inhibitor,
- Non-competitive inhibitors and
- Uncompetitive inhibitors.
What are enzyme inhibitors?
Enzyme inhibitors are molecules whose presence act to inhibit or reduce the catalytic activity of enzymes
The three types of enzyme inhibitors are:
- Competitive inhibitor
- Non-competitive inhibitors
- Uncompetitive inhibitors
Competitive inhibitors compete with substare for enzyme binding site.
Non-competitive inhibitors binds at a different site than the active site.
Uncompetitive inhibitors binds to enzyme substrate complex.
Therefore, enzyme inhibitors inhibit enzyme catalysis and include, Competitive inhibitor, Non-competitive inhibitors and Uncompetitive inhibitors.
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Rewritten by : Barada
Competitive, allosteric, and noncompetitive inhibition are three types of enzyme inhibitors. Competitive inhibitors bind to the active site to block substrate binding, allosteric inhibitors induce conformational changes that reduce enzyme affinity, and noncompetitive inhibitors bind to allosteric sites and block substrate binding.
Competitive inhibition:
In competitive inhibition, an inhibitor molecule binds to the
active site
of an enzyme and blocks the substrate from binding. This happens when the inhibitor concentration is approximately equal to the substrate concentration. For example, sulfa drugs are competitive inhibitors that bind to the active sites of bacterial enzymes, preventing the synthesis of essential molecules.
- Allosteric inhibition:
Allosteric inhibition occurs when an inhibitor molecule binds to a different site on the enzyme, inducing a conformational change that reduces the enzyme's affinity for its substrate. This type of inhibition affects all active sites on the enzyme and can be seen in multi-subunit enzymes. Allosteric activators, on the other hand, bind to locations away from the active site, increasing the enzyme's affinity for its substrate.
- Noncompetitive inhibition:
Noncompetitive inhibition involves an inhibitor molecule binding to an allosteric site on the enzyme, inhibiting the enzyme's activity by blocking substrate binding. This type of inhibition also induces a conformational change in the enzyme, making the active sites less efficient in binding substrates.
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