Enzymes and metabolism: exam questions

5 questions, 12 marks. Write your answers on paper, then open each mark scheme.

Question 1

Paper 1A style

Which process is an example of catabolism?

  1. Formation of glycogen from glucose in liver cells
  2. Synthesis of a polypeptide at a ribosome
  3. Hydrolysis of starch to maltose in the small intestine
  4. Production of glucose in photosynthesis
[1 mark]
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Answer: C [1]

Question 2

Paper 1A style

Which statement describes induced-fit binding?

  1. The active site is a rigid shape exactly complementary to the substrate before binding.
  2. Both the substrate and the active site change shape when binding occurs.
  3. The substrate changes shape but the enzyme does not.
  4. The enzyme denatures slightly each time a substrate binds.
[1 mark]
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Answer: B [1]

Question 3

Paper 1B style

Students investigated the effect of temperature on the activity of catalase extracted from potato. They measured the volume of oxygen released from hydrogen peroxide in the first 60 seconds. The data are for practice and show the mean of three repeats. (a) Calculate the mean rate of oxygen production at 35 °C, in cm³ s⁻¹. [1] (b) Describe the effect of temperature on the volume of oxygen released. [2] (c) Explain the result at 55 °C. [2]

Volume of oxygen released in 60 s at different temperatures
Temperature / °CMean volume of oxygen in 60 s / cm³
156.0
2511.4
3519.8
4515.6
552.4
[5 marks]
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  • (a) 19.8 ÷ 60 = 0.33 cm³ s⁻¹ [1]
  • (b) volume increases from 15 °C to 35 °C / up to an optimum of about 35 °C [1]
  • (b) volume decreases above 35 °C, falling steeply to 2.4 cm³ at 55 °C [1]
  • (c) (most) catalase molecules are denatured / bonds holding tertiary structure break [1]
  • (c) active site changes shape so hydrogen peroxide cannot bind / fewer enzyme–substrate complexes form [1]
  • (c) accept: some enzyme molecules still active so a little oxygen is produced [1]
  • (c) [max 2]

Question 4

Paper 2A style

Outline how the structure of a globular protein allows it to act as an enzyme.

[2 marks]
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  • active site formed from only a few amino acids / R groups [1]
  • interactions between amino acids elsewhere in the folded (tertiary) structure hold the active site in its shape [1]
  • active site has shape/chemical properties that bind the substrate / allow catalysis OWTTE [1]
  • globular protein is soluble so can move / collide with substrate [1]
  • [max 2]

Question 5

Paper 2A style

Explain how an enzyme increases the rate of a reaction, with reference to activation energy.

[3 marks]
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  • activation energy is energy needed to break bonds in the substrate / to start the reaction [1]
  • binding to active site stresses / weakens bonds in the substrate [1]
  • enzyme lowers the activation energy [1]
  • so more substrate molecules have enough energy to react (at a given temperature) [1]
  • overall energy change of the reaction is not altered [1]
  • [max 3]