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Enzyme Inhibitors quiz

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  • What is the main function of enzyme inhibitors?
    Enzyme inhibitors decrease enzymatic activity, slowing down or stopping reactions as needed.
  • What are the two main types of enzyme inhibitors?
    The two main types are reversible inhibitors and irreversible inhibitors.
  • How do irreversible inhibitors interact with enzymes?
    Irreversible inhibitors bind tightly to enzymes through covalent bonds, permanently disabling their function.
  • Give an example of an irreversible enzyme inhibitor.
    Nerve gas is an example of an irreversible enzyme inhibitor.
  • How do reversible inhibitors bind to enzymes?
    Reversible inhibitors bind weakly to enzymes through non-covalent interactions, allowing their effects to be reversed.
  • What are the two types of reversible enzyme inhibitors?
    The two types are competitive inhibitors and non-competitive (allosteric) inhibitors.
  • How do competitive inhibitors affect enzyme activity?
    Competitive inhibitors compete with the substrate for the enzyme's active site, preventing substrate binding.
  • Where do non-competitive inhibitors bind on the enzyme?
    Non-competitive inhibitors bind to a different site on the enzyme, not the active site.
  • What is another name for non-competitive inhibitors?
    Non-competitive inhibitors are also called allosteric inhibitors.
  • How do non-competitive inhibitors prevent substrate interaction?
    They alter the shape of the enzyme's active site, so the substrate can no longer bind effectively.
  • Can the effects of irreversible inhibitors be reversed?
    No, the effects of irreversible inhibitors cannot be reversed because they bind permanently.
  • Why are enzyme inhibitors important for cells?
    They help regulate cellular chemical reactions by controlling when enzymes are active or inactive.
  • What happens to the enzyme after an irreversible inhibitor binds?
    The enzyme is permanently inactivated and cannot catalyze reactions anymore.
  • How can the effects of reversible inhibitors be undone?
    Their effects can be undone because the weak, non-covalent bonds can be broken, releasing the inhibitor.
  • What is the main difference between competitive and non-competitive inhibition?
    Competitive inhibitors block the active site, while non-competitive inhibitors bind elsewhere and change the active site's shape.