Examples of allosteric in the following topics:
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- In noncompetitive allosteric inhibition, inhibitor molecules bind to an enzyme at the allosteric site.
- However, allosteric inhibitors are not the only molecules that bind to allosteric sites.
- Allosteric activators can increase reaction rates.
- However, while ATP is an inhibitor, ADP is an allosteric activator.
- Allosteric inhibitors modify the active site of the enzyme so that substrate binding is reduced or prevented.
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- A number of enzymes involved in each of the pathways (in particular, the enzyme catalyzing the first committed reaction of the pathway) are controlled by attachment of a molecule to an allosteric (non-active) site on the protein.
- These regulators, known as allosteric effectors, may increase or decrease enzyme activity, depending on the prevailing conditions, altering the steric structure of the enzyme, usually affecting the configuration of the active site.
- The attachment of a molecule to the allosteric site serves to send a signal to the enzyme, providing feedback.
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- Two cAMP molecules bind dimeric CAP with negative cooperativity and function as allosteric effectors by increasing the protein's affinity for DNA.
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- Pyruvate kinase is also regulated by ATP (a negative allosteric effect).