Lesson 2.3.3

2.3.3 Enzyme mechanism, specificity and activation energy Quiz: Pearson Edexcel Biology, Unit 2

20 questions

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Lesson 2.3.3, Enzyme mechanism, specificity and activation energy: 20 multiple choice questions for the Pearson Edexcel Biology (9BI0), Unit 2: Genes and Health, written with Revision Ninja.

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The 20 questions

  1. How do enzymes increase the rate of chemical reactions in living organisms?

    • Increasing activation energy
    • Raising body temperature
    • Increasing substrate concentration
    • Lowering activation energy
  2. What is activation energy?

    • Maximum stored energy
    • Minimum reaction energy
    • Energy released overall
    • Total kinetic energy
  3. Which region of an enzyme directly binds to the substrate?

    • Inhibitor site
    • Allosteric site
    • Active site
    • Regulatory domain
  4. Which enzyme model involves the active site changing shape slightly to fit the substrate?

    • Lock and key model
    • Allosteric activation model
    • Induced fit model
    • Competitive inhibition model
  5. What feature of an enzyme's active site determines its substrate specificity?

    • Linear primary structure
    • Identical shape
    • High activation energy
    • Complementary shape
  6. What process occurs when high temperatures disrupt an enzyme's tertiary structure?

    • Hydrolysis
    • Renaturation
    • Phosphorylation
    • Denaturation
  7. Which of the following is an intracellular enzyme?

    • Amylase
    • Pepsin
    • Catalase
    • Trypsin
  8. Which of the following is an extracellular enzyme?

    • Catalase
    • DNA polymerase
    • ATP synthase
    • Amylase
  9. Why is the initial rate measured at the very start of an enzyme reaction?

    • Temperature is highest
    • Product is absent
    • Substrate not limiting
    • Enzyme is denatured
  10. An enzyme catalyses a reaction and produces 20 cm^3 of gas in 40 seconds. What is the average rate of gas production?

    • 0.05 cm^3 per second
    • 800 cm^3 per second
    • 2 cm^3 per second
    • 0.5 cm^3 per second
  11. At low substrate concentrations, how does increasing substrate affect reaction rate?

    • Increases proportionally
    • Stays constant
    • Halves immediately
    • Decreases rapidly
  12. Why does reaction rate plateau at high substrate concentrations?

    • Substrate breaks down
    • Enzyme denatures
    • Activation energy rises
    • Active sites saturated
  13. What happens to reaction rate when enzyme concentration doubles with excess substrate?

    • Rate halves
    • Rate doubles
    • Rate decreases
    • Rate stays constant
  14. Why does increasing temperature up to the optimum increase reaction rate?

    • Lower activation energy
    • Active site expands
    • More enzyme produced
    • More kinetic energy
  15. Why does reaction rate fall rapidly above the optimum temperature?

    • Substrate evaporates
    • Activation energy rises
    • Molecules stop moving
    • Enzyme denatures
  16. How does a change in pH affect an enzyme's active site?

    • Oxidises amino acids
    • Alters R-group charges
    • Increases kinetic energy
    • Breaks peptide bonds
  17. Which variable must be controlled when measuring the effect of enzyme concentration?

    • Enzyme origin
    • Product concentration
    • Test tube volume
    • Temperature and pH
  18. Where does a competitive inhibitor bind to an enzyme?

    • Allosteric site
    • Coenzyme site
    • Substrate site
    • Active site
  19. What shape is characteristic of globular proteins like enzymes?

    • Rigid and linear
    • Long and fibrous
    • Compact and spherical
    • Flat and sheet-like
  20. How do enzymes lower the activation energy of a reaction?

    • Raising collision frequency
    • Orientating substrate molecules
    • Increasing system temperature
    • Altering overall enthalpy

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