1 Which levels of protein structure can determine the specificity of an enzyme?

1 primary
2 secondary

3 tertiary
4 quaternary

A 1, 2, 3 and 4
B 1, 2 and 3 only

C 1, 2 and 4 only
D 3 and 4 only
2 The breakdown of hydrogen peroxide to water and oxygen is catalysed by the enzyme catalase.

In an investigation into the effect of pH on the rate of reaction of catalase, potato cubes were
added to hydrogen peroxide.

Which dependent variable should be recorded?

A the change in mass of the potato after a given time

B the pH of the solution at regular time intervals
C the number of potato cubes added at the start
D the volume of oxygen given off at regular time intervals
3 Some inhibitors of enzyme reactions bind to the enzyme / substrate complex.

Which statements about this type of inhibition are correct?

1 The active site changes shape.

2 The inhibitor is non-competitive.
3 The initial rate of reaction is reduced.

4 The maximum rate of reaction (Vmax) is increased.

A 1 and 2 only B 1 and 3 only C 2 and 3 only D 2, 3 and 4 only

4 The graph shows the activation energy of an enzyme-catalysed reaction and the same reaction
without a catalyst.

energy Y
reactants

Z
products

reaction

Which of the following shows the activation energy of the uncatalysed reaction?

A X+Y–Z B X+Z–Y C X+Y D Y+Z

5 Which of the following statements are true of all enzymes?

1 soluble in water
2 catalyse the breakdown of large molecules into smaller molecules
3 only have one active site
4 have a quaternary structure

A 1, 2 and 3 only
B 2, 3 and 4 only
C 1 only
D 4 only
6 The graphs show the effects of temperature and pH on enzyme activity.

Q
R

P
rate of rate of
reaction reaction

temperature pH

Which statement explains the enzyme activity at the point shown?

A At P, hydrogen bonds are formed between enzyme and substrate.

B At Q, the kinetic energy of enzyme and substrate is highest.
C At R, peptide bonds in the enzyme begin to break.
D At S, the enzyme is completely denatured.
7 Which statements about the effect of all enzyme inhibitors are correct?

1 alter the shape of the active site

2 denature the enzyme
3 reduce the rate of the enzyme catalysed reaction

A 1, 2 and 3 B 1 and 2 only C 1 and 3 only D 3 only

8 In an enzyme-catalysed reaction, which combination of inhibitor and substrate would result in the
highest rate of reaction?

inhibitor substrate concentration

A competitive high
B competitive low
C non-competitive high
D non-competitive low
 4 For
Examiner’s
Use
2 (a) Describe how enzymes take part in chemical reactions.

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Starch phosphorylase is an enzyme found in plant cells. In potato tuber cells, the enzyme
takes part in the breakdown of starch when the tuber begins to grow.

starch phosphorylase
starch + phosphate ions glucose 1-phosphate

A student investigated the effect of pH on this reaction using two buffer solutions.

The student prepared four test-tubes, A to D, as shown in Table 2.1 and described
below.

The student made an extract of potato tissue that contained the enzyme. Some of this
extract was boiled.

A solution of potassium dihydrogen phosphate was added to some tubes as a source of

phosphate ions.

The test-tubes were left for ten minutes in a water bath at 30 °C and then samples were
tested with iodine solution.

© UCLES 2007 9700/02/M/J/07

 5 For
Examiner’s
Use
Table 2.1

test- contents
tube
volume volume of volume of pH of buffer enzyme results with
of starch glucose potassium solution extract iodine solution
solution / 1-phosphate dihydrogen after ten
cm3 solution / cm3 phosphate minutes
solution / cm3
A 2 0.5 6.5 unboiled negative

B 2 0.5 2.0 unboiled positive

C 2 0.5 6.5 boiled positive

D 2 6.5 boiled negative

(b) (i) State what the student would conclude from a positive result with iodine solution.

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(ii) Explain why the student boiled some of the extract in this investigation.

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(c) Explain the results shown in Table 2.1.

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[Total: 11]

© UCLES 2007 9700/02/M/J/07 [Turn over

 6

3 Trypsin is a protease enzyme, which hydrolyses protein molecules, such as albumen, to For
amino acids. Examiner’s
Use

A student investigated the effect of substrate concentration on the activity of trypsin. Six
different concentrations of albumen were prepared and trypsin was added to each in turn.
The student measured the time for albumen to break down and then calculated the rate of
reaction. The investigation was carried out at 35 °C.

The student’s results are shown in Fig. 3.1.

18

16

14

12

rate of
10
reaction /
arbitrary
units 8

0
0 5 10 15 20 25 30 35
substrate concentration / g dm–3

Fig. 3.1

(a) Explain the results shown in Fig. 3.1.

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(b) The student repeated the investigation at 25 °C.

Draw on Fig. 3.1 a curve to show the results that you would expect. [2]

© UCLES 2008 9700/02/O/N/08

 7

During infections of the lungs, phagocytes move from the blood to the lining of the alveoli. For
Examiner’s
Phagocytes release the enzyme elastase (a protease) in order to digest a pathway through Use

the alveolar wall. Most people produce a glycoprotein, alpha 1-antitrypsin (AAT), in the lung
which inhibits elastase and so prevents widespread breakdown of alveoli. The inhibitory
action of AAT was investigated using the enzyme trypsin.

(c) Describe one way in which AAT may act to inhibit the enzyme elastase.

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(d) Explain how you would adapt the student’s investigation with trypsin to find out how AAT
acts as an inhibitor.

You may use the space below to sketch the graph of the results that you might expect.

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rate of reaction

substrate concentration
[4]
© UCLES 2008 9700/02/O/N/08 [Turn over