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Enzyme Inhibition quiz #1

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  • What is the difference between competitive and noncompetitive enzyme inhibitors?
    Competitive inhibitors bind to the enzyme's active site, competing with the substrate and blocking its access, while noncompetitive inhibitors bind to an allosteric site, causing the enzyme to change shape and preventing substrate binding without competing for the active site.
  • How do competitive inhibitors affect enzyme activity?
    Competitive inhibitors decrease enzyme activity by occupying the active site, preventing the substrate from binding and thus slowing down the catalyzed reaction.
  • What is the role of an allosteric site in noncompetitive inhibition?
    In noncompetitive inhibition, the inhibitor binds to the allosteric site, which is a location other than the active site, causing the enzyme to change shape and reducing its ability to bind the substrate.
  • Why is understanding enzyme inhibition important in medicine and research?
    Understanding enzyme inhibition is important because it allows for the regulation of biochemical reactions, which can be applied to control disease processes and develop drugs that target specific enzymes.
  • What is the main difference between competitive and noncompetitive enzyme inhibitors?
    Competitive inhibitors bind to the enzyme's active site and compete with the substrate, while noncompetitive inhibitors bind to an allosteric site, causing the enzyme to change shape and preventing substrate binding.
  • How do competitive inhibitors slow down enzyme-catalyzed reactions?
    They occupy the enzyme's active site, blocking the substrate from binding and thus decreasing the rate of the reaction.
  • Where do noncompetitive inhibitors bind on an enzyme, and what is the result?
    Noncompetitive inhibitors bind to an allosteric site, which is a location other than the active site, causing the enzyme to change shape and reducing its ability to bind the substrate.
  • What happens to the enzyme's active site when a noncompetitive inhibitor binds to the allosteric site?
    The active site changes shape, preventing the substrate from binding and inhibiting catalysis.
  • Why is enzyme inhibition important for cells?
    It allows cells to regulate the speed of biochemical reactions, preventing reactions from proceeding too quickly and maintaining proper cellular function.
  • How is understanding enzyme inhibition useful in medicine and research?
    It helps in developing drugs that target specific enzymes and in controlling disease processes by regulating biochemical reactions.