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  • Enzyme Inhibition


    The process of slowing down or stopping the activity of an enzyme.

  • What are the two main types of enzyme inhibitors?


    Competitive and noncompetitive inhibitors.

  • Competitive Inhibitors


    Inhibitors that bind to the active site of an enzyme, blocking substrate access.

  • Noncompetitive Inhibitors


    Inhibitors that bind to an allosteric site, altering the enzyme's shape and preventing substrate binding.

  • Active Site


    The region on an enzyme where the substrate binds.

  • Allosteric Site


    An alternative site on an enzyme where noncompetitive inhibitors bind.

  • How do competitive inhibitors affect enzyme activity?


    They compete with the substrate for the active site, preventing substrate binding and slowing down the reaction.

  • How do noncompetitive inhibitors affect enzyme activity?


    They bind to an allosteric site, causing a change in enzyme shape that prevents substrate binding.

  • Catalysis


    The acceleration of a chemical reaction by a catalyst, such as an enzyme.

  • What happens when a competitive inhibitor binds to an enzyme?


    It blocks the substrate from binding to the active site, inhibiting the enzyme's activity.

  • What happens when a noncompetitive inhibitor binds to an enzyme?


    It changes the shape of the enzyme, including the active site, preventing substrate binding.

  • Metabolic Balance


    The equilibrium between different metabolic pathways in a cell.

  • Why is enzyme inhibition important?


    It helps regulate the speed of chemical reactions in cells, maintaining metabolic balance.

  • Drug Design


    The process of designing new medications based on the knowledge of biological targets.

  • How can enzyme inhibitors be used in medicine?


    They can be used to design drugs that regulate enzyme activity in various diseases.

  • Substrate


    The molecule upon which an enzyme acts.

  • What is the role of the active site in enzyme function?


    It is the specific region where the substrate binds and the reaction occurs.

  • What is the effect of a noncompetitive inhibitor on the active site?


    It alters the shape of the active site, preventing substrate binding.

  • Enzyme


    A protein that catalyzes chemical reactions in living organisms.

  • What is the difference between competitive and noncompetitive inhibition?


    Competitive inhibition involves binding to the active site, while noncompetitive inhibition involves binding to an allosteric site.

  • What is the purpose of enzyme inhibition in cells?


    To regulate the speed of chemical reactions and maintain metabolic balance.

  • How do competitive inhibitors and substrates interact?


    They compete for the same binding site on the enzyme.

  • How do noncompetitive inhibitors and substrates interact?


    Noncompetitive inhibitors bind to a different site, not competing directly with the substrate.

  • What is the result of enzyme inhibition on catalysis?


    It slows down or stops the catalysis of the enzyme.

  • What is the significance of the allosteric site in enzyme inhibition?


    It allows noncompetitive inhibitors to bind and alter enzyme activity without competing with the substrate.

  • What is the main function of enzymes in cells?


    To speed up chemical reactions.

  • How does enzyme inhibition relate to drug design?


    Inhibitors can be used to create drugs that target specific enzymes involved in diseases.

  • What is the impact of enzyme inhibition on metabolic pathways?


    It helps control the flow and balance of metabolic reactions.