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  2. Allosteric modulator - Wikipedia

    en.wikipedia.org/wiki/Allosteric_modulator

    The site that an allosteric modulator binds to (i.e., an allosteric site) is not the same one to which an endogenous agonist of the receptor would bind (i.e., an orthosteric site). Modulators and agonists can both be called receptor ligands. [2] Allosteric modulators can be 1 of 3 types either: positive, negative or neutral.

  3. Enzyme inhibitor - Wikipedia

    en.wikipedia.org/wiki/Enzyme_inhibitor

    Inhibition of this enzyme causes an uncontrolled increase in the acetylcholine neurotransmitter, muscular paralysis and then death. Neurotoxicity can also result from the inhibition of receptors; for example, atropine from deadly nightshade (Atropa belladonna) that functions as a competitive antagonist of the muscarinic acetylcholine receptors ...

  4. Mixed inhibition - Wikipedia

    en.wikipedia.org/wiki/Mixed_inhibition

    [1] [2] Non-competitive inhibition is sometimes thought of as a special case of mixed inhibition. In mixed inhibition, the inhibitor binds to an allosteric site, i.e. a site different from the active site where the substrate binds. However, not all inhibitors that bind at allosteric sites are mixed inhibitors. [1] Mixed inhibition may result in ...

  5. Allosteric regulation - Wikipedia

    en.wikipedia.org/wiki/Allosteric_regulation

    Allosteric regulation of an enzyme. In the fields of biochemistry and pharmacology an allosteric regulator (or allosteric modulator) is a substance that binds to a site on an enzyme or receptor distinct from the active site, resulting in a conformational change that alters the protein's activity, either enhancing or inhibiting its function.

  6. Allosteric enzyme - Wikipedia

    en.wikipedia.org/wiki/Allosteric_enzyme

    Allosteric enzymes are enzymes that change their conformational ensemble upon binding of an effector (allosteric modulator) which results in an apparent change in binding affinity at a different ligand binding site. This "action at a distance" through binding of one ligand affecting the binding of another at a distinctly different site, is the ...

  7. Suicide inhibition - Wikipedia

    en.wikipedia.org/wiki/Suicide_inhibition

    Stereoisomers of Soman, a G-series nerve agent and suicide inhibitor of acetylcholinesterase.Note the non-carbon chiral center.. In biochemistry, suicide inhibition, also known as suicide inactivation or mechanism-based inhibition, is an irreversible form of enzyme inhibition that occurs when an enzyme binds a substrate analog and forms an irreversible complex with it through a covalent bond ...

  8. Competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Competitive_inhibition

    A competitive inhibitor could bind to an allosteric site of the free enzyme and prevent substrate binding, as long as it does not bind to the allosteric site when the substrate is bound. For example, strychnine acts as an allosteric inhibitor of the glycine receptor in the mammalian spinal cord and brain stem. Glycine is a major post-synaptic ...

  9. Reuptake inhibitor - Wikipedia

    en.wikipedia.org/wiki/Reuptake_inhibitor

    Escitalopram, a selective serotonin reuptake inhibitor (SSRI) used as an antidepressant.. Reuptake inhibitors (RIs) are a type of reuptake modulators.It is a drug that inhibits the plasmalemmal transporter-mediated reuptake of a neurotransmitter from the synapse into the pre-synaptic neuron.