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Enzyme Inhibitors definitions

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  • Enzyme Inhibitor
    A molecule that decreases enzymatic activity, crucial for regulating or stopping cellular reactions as needed.
  • Irreversible Inhibitor
    A substance that binds tightly, usually via covalent bonds, permanently disabling enzyme function.
  • Reversible Inhibitor
    A molecule that binds weakly through non-covalent interactions, allowing its inhibitory effect to be undone.
  • Covalent Bond
    A strong chemical linkage responsible for the permanent attachment of certain inhibitors to enzymes.
  • Non-covalent Interaction
    A weak chemical association enabling reversible binding between inhibitors and enzymes.
  • Competitive Inhibitor
    A molecule that competes with the substrate for the enzyme's active site, blocking substrate access.
  • Non-competitive Inhibitor
    A molecule that binds to a site other than the active site, altering enzyme shape and reducing activity.
  • Allosteric Inhibitor
    A substance that attaches to a distinct enzyme region, causing conformational changes that hinder substrate binding.
  • Active Site
    The specific enzyme region where substrates or competitive inhibitors bind to initiate or block reactions.
  • Substrate
    A molecule that interacts with an enzyme's active site to undergo a chemical transformation.
  • Product
    The result of an enzymatic reaction, released after substrate conversion.
  • Regulation
    The cellular process of controlling enzyme activity to maintain appropriate reaction rates.
  • Nerve Gas
    A toxic compound that acts as an irreversible inhibitor, leading to permanent enzyme inactivation.