Enzymes and Catalysis
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Questions and Answers

What is the primary function of an enzyme?

  • To decrease the rate of a chemical reaction
  • To be consumed by the reactants
  • To alter the reactants in a chemical reaction
  • To increase the rate of a chemical reaction (correct)
  • What is the characteristic of enzyme-substrate binding according to the induced fit model?

  • The enzyme binds to multiple substrates simultaneously
  • The substrate induces a change in the enzyme's conformation (correct)
  • The enzyme-substrate complex is highly unstable
  • The enzyme's shape is complementary to the substrate's shape
  • What is the purpose of the active site in an enzyme-catalyzed reaction?

  • To increase the activation energy
  • To bind to the substrate by noncovalent interactions (correct)
  • To bind to the products
  • To bind to the reactants
  • Why is the lock-and-key model less likely to be an effective catalyst?

    <p>The ES complex may be too stable, reducing the thermodynamic benefit</p> Signup and view all the answers

    What is the term for the energy required to reach the transition state from the ground state of the reactants?

    <p>Activation energy</p> Signup and view all the answers

    What is the characteristic of enzyme-catalyzed reactions?

    <p>They are 103-1020 times faster than uncatalyzed reactions</p> Signup and view all the answers

    What is the primary function of the transition state?

    <p>To represent an unstable arrangement of atoms in which chemical bonds are being formed or broken</p> Signup and view all the answers

    What is the advantage of inducing a fit in the induced fit model?

    <p>It reduces the distance to the transition state</p> Signup and view all the answers

    What is the characteristic of most enzymes?

    <p>They are proteins</p> Signup and view all the answers

    What is the term for the reactant in an enzyme-catalyzed reaction?

    <p>Substrate</p> Signup and view all the answers

    What is the characteristic of competitive inhibition?

    <p>Km increases</p> Signup and view all the answers

    What is the effect of uncompetitive inhibition on Vmax?

    <p>Decreases</p> Signup and view all the answers

    What is the characteristic of non-competitive inhibition?

    <p>Vmax decreases, Km remains the same</p> Signup and view all the answers

    What is the effect of adding more substrate in competitive inhibition?

    <p>Overcomes the inhibition</p> Signup and view all the answers

    What type of inhibition occurs when the inhibitor binds only to the ES complex?

    <p>Uncompetitive</p> Signup and view all the answers

    What is the effect of non-competitive inhibition on Km?

    <p>Remains the same</p> Signup and view all the answers

    What is the characteristic of irreversible inhibition?

    <p>Forms a stable covalent bond with the enzyme</p> Signup and view all the answers

    What is the effect of uncompetitive inhibition on the ES complex?

    <p>Decreases the formation of ES</p> Signup and view all the answers

    What is the result of irreversible inhibition of acetylcholinesterase (AChE)?

    <p>Death by paralysis</p> Signup and view all the answers

    What is the difference between reversible and irreversible inhibition?

    <p>Reversible inhibition can be overcome by adding more substrate, while irreversible inhibition cannot</p> Signup and view all the answers

    What is the primary purpose of studying Enzyme Kinetics?

    <p>To understand various properties of enzymes such as substrate specificity and affinity</p> Signup and view all the answers

    What is the unit of measurement for Turnover Number (Kcat)?

    <p>sec-1</p> Signup and view all the answers

    What does a small KM value indicate?

    <p>The enzyme requires only a small amount of substrate to become saturated</p> Signup and view all the answers

    What is the purpose of Lineweaver-Burk plots?

    <p>To accurately determine Vmax and KM from experimental data</p> Signup and view all the answers

    What is the result of excessive heat on enzyme function?

    <p>Enzyme becomes completely nonfunctional</p> Signup and view all the answers

    What type of inhibitor binds to the active site of E, competing with S?

    <p>Competitive inhibitor</p> Signup and view all the answers

    What is the definition of Vmax?

    <p>The maximum reaction rate reached when the enzyme is completely saturated with substrate</p> Signup and view all the answers

    What is the significance of Km in enzyme kinetics?

    <p>It gives us information on enzyme affinity for the substrate</p> Signup and view all the answers

    What is the definition of catalytic efficiency?

    <p>The ratio of Kcat to Km</p> Signup and view all the answers

    What is the effect of pH on enzyme function?

    <p>Enzymes work best within a particular range of pH</p> Signup and view all the answers

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