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Competitive inhibitors bind to the active site of the enzyme, thereby reducing the reaction velocity.
Competitive inhibitors bind to the active site of the enzyme, thereby reducing the reaction velocity.
True
Non-competitive inhibitors bind to the active site of the enzyme, altering its kinetic properties.
Non-competitive inhibitors bind to the active site of the enzyme, altering its kinetic properties.
False
Allosteric modulation occurs through the binding of molecules to the active site of the enzyme.
Allosteric modulation occurs through the binding of molecules to the active site of the enzyme.
False
Irreversible inhibitors form a stable complex with the enzyme, resulting in complete loss of catalytic activity.
Irreversible inhibitors form a stable complex with the enzyme, resulting in complete loss of catalytic activity.
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The optimum pH for enzymes is always pH 7.
The optimum pH for enzymes is always pH 7.
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Competitive inhibitors can be overcome by increasing the substrate concentration.
Competitive inhibitors can be overcome by increasing the substrate concentration.
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Non-competitive inhibitors are always reversible.
Non-competitive inhibitors are always reversible.
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Irreversible inhibitors are always competitive inhibitors.
Irreversible inhibitors are always competitive inhibitors.
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Allosteric enzymes always have a quaternary structure.
Allosteric enzymes always have a quaternary structure.
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Aspirin is a non-competitive inhibitor of cyclo-oxygenase.
Aspirin is a non-competitive inhibitor of cyclo-oxygenase.
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