Enzyme inhibition: competitive and non-competitive

Cards (89)

  • What is the role of the active site in competitive inhibition?
    It is blocked by the inhibitor, preventing binding
  • How does inhibition affect the reaction process?
    • Inhibitor binds to enzyme, preventing substrate from binding
    • This blocks the enzyme's catalytic activity, slowing or stopping the reaction
    • Different types of inhibition (competitive, non-competitive, uncompetitive) have varying effects
  • What is the name of the process shown in the image?
    Reaction and inhibition
  • What are the key differences between competitive, non-competitive, and uncompetitive inhibition?
    • Competitive inhibition: Inhibitor binds to active site, preventing substrate binding
    • Non-competitive inhibition: Inhibitor binds elsewhere, changing enzyme's shape and reducing activity
    • Uncompetitive inhibition: Inhibitor binds to enzyme-substrate complex, preventing product release
  • How do the two diagrams illustrate the difference between reaction and inhibition?
    The first diagram shows the normal reaction process, while the second diagram shows how an inhibitor can block the reaction
  • How do the two diagrams illustrate the difference between reaction and inhibition?
    The first diagram shows the normal reaction process, while the second diagram shows how an inhibitor can block the reaction
  • What are the key points of enzyme inhibition?
    • Blocks an enzyme's activity
    • Inhibitors are the blocking substances
    • Can slow or stop reactions
    • Inhibitors bind to disrupt enzyme function
  • What is competitive inhibition?
    Inhibition by a similar-shaped inhibitor
  • How does a competitive inhibitor affect the active site of an enzyme?
    It competes with the substrate for binding
  • What is the result of the conformational change in the enzyme during non-competitive inhibition?
    The substrate can't bind effectively to the active site
  • What are substances that stop enzymes called?
    Inhibitors
  • What are the steps involved in non-competitive inhibition?
    1. Inhibitor binds to allosteric site
    2. Active site shape changes
    3. Substrate can't bind effectively
  • What are the key features of competitive inhibition?
    • Competes with substrate for active site
    • Has a similar shape to the substrate
    • Blocks substrate from binding
    • Reduces enzyme's activity
  • What effect does non-competitive inhibition have on the active site?
    It causes a conformational change in the active site
  • How does a competitive inhibitor affect the enzyme kinetics compared to the normal enzyme?
    It has the same Vmax but a different Km
  • Where does a non-competitive inhibitor bind on the enzyme?
    To the allosteric site of the enzyme
  • What is the name of the process shown in the image?
    Reaction and inhibition
  • How does increasing substrate concentration influence enzyme-substrate and enzyme-inhibitor binding?
    • Increasing substrate favors enzyme-substrate binding
    • Decreases enzyme-inhibitor binding
    • Restores enzyme activity
  • How does a noncompetitive inhibitor affect the enzyme kinetics compared to the normal enzyme?
    It has the same Km but a different Vmax
  • What is the mechanism of competitive inhibition in enzymes?
    • Inhibitor resembles substrate shape
    • Binds to enzyme's active site
    • Forms enzyme-inhibitor complex
    • Binding is typically reversible
    • Higher substrate concentration can displace inhibitor
  • What happens to enzyme activity when substrate concentration is low in competitive inhibition?
    Inhibition increases as substrate competes less
  • What is the effect of competitive inhibition on enzyme activity?
    It reduces the enzyme's activity
  • How does increased substrate concentration affect competitive inhibition?
    It reduces inhibition by competing for active site
  • How does a competitive inhibitor affect the enzyme kinetics compared to the normal enzyme?
    It has the same Vmax but a different Km
  • What are the key differences between competitive and noncompetitive inhibitors based on the enzyme kinetics shown in the image?
    • Competitive inhibitor: Same Vmax, different Km
    • Noncompetitive inhibitor: Same Km, different Vmax
  • What is non-competitive inhibition?
    Inhibition when an inhibitor binds to an allosteric site
  • How does cyanide inhibit enzyme activity?
    It binds to an allosteric site, altering the active site
  • What analogy is used to explain non-competitive inhibition?
    • Changing the lock on a door
    • Keys won't fit because the lock is different
  • What are the key steps in the reaction process shown?
    • Substrate binds to enzyme, forming enzyme-substrate complex
    • Enzyme catalyzes reaction, converting substrate to product
    • Product is released, leaving the enzyme free to catalyze another reaction
  • What color is the substrate in the provided analogy image?
    Yellow
  • How does the presence of an inhibitor affect the binding of the substrate to the enzyme?
    It prevents the substrate from binding to the active site
  • What color is the inhibitor in the provided analogy image?
    Blue
  • How do non-competitive inhibitors affect substrate competition?
    They compete indirectly with the substrate
  • What is the difference between a competitive inhibitor and a noncompetitive inhibitor?
    • Competitive inhibitor: Same Vmax as normal enzyme, different Km
    • Noncompetitive inhibitor: Same Km as normal enzyme, different Vmax
  • What is the effect of competitive inhibitors on enzyme activity?
    It depends on substrate concentration
  • How do inhibitors affect enzyme reactions?
    They can slow down or completely stop reactions.
  • What is the purpose of the process shown in the image?
    To illustrate how a reaction can be inhibited
  • What are the key steps in the reaction process shown?
    • Substrate binds to enzyme, forming enzyme-substrate complex
    • Enzyme catalyzes reaction, converting substrate to product
    • Product is released, leaving the enzyme free to catalyze another reaction
  • How does non-competitive inhibition affect the active site?
    It alters the shape of the active site
  • What is the symbol used to represent the substrate concentration in the image?
    [S]