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1.

At the start of glycolysis, glucose is phosphorylated to produce glucose 6-phosphate, which is


converted into fructose 6-phosphate. A second phosphorylation reaction is then carried out, in
which fructose 6-phosphate is converted into fructose 1,6-bisphosphate. This reaction is
catalyzed by the enzyme phosphofructokinase. Biochemists measured the enzyme activity of
phosphofructokinase (the rate at which it catalyzed the reaction) at different concentrations of
fructose 6-phosphate. The enzyme activity was measured with a low concentration of ATP and a
high concentration of ATP in the reaction mixture. The graph below shows the results.

L o w A T P c o n c e n tra tio n

E n z y m e a c tiv ity
H ig h A T P c o n c e n tra tio n

F ru c to s e 6 -p h o s p h a te c o n c e n tra tio n
(a)

(i)

Using only the data in the above graph, outline the effect of increasing fructose 6phosphate concentration on the activity of phosphofructokinase, at a low ATP
concentration.
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(2)

(ii)

Explain how increases in fructose 6-phosphate concentration affect the activity of


the enzyme.
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(2)

(b)

(i)

Outline the effect of increasing the ATP concentration on the activity of


phosphofructokinase.
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(2)

(ii)

Suggest an advantage to living organisms of the effect of ATP on


phosphofructokinase.
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(1)
(Total 7 marks)

2.

(a)

Define the term active site of an enzyme.


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(1)

(b)

Outline how enzymes catalyze biochemical reactions.


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(2)

(c)

Explain the effect of pH on enzyme activity.


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(3)

(d)

State three functions of lipids.


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(2)
(Total 8 marks)

3.

Explain the effects of temperature, pH and substrate concentration on enzyme activity.


(Total 8 marks)

4.

(a)

State one named example of a fibrous protein and one named example of a globular
protein.
Fibrous: ...........................................

Globular: ...........................................
(2)

(b)

Outline the effect of enzymes on the reactions they catalyse.


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(2)

(c)

The rate of cellular respiration is controlled by the allosteric inhibition of


phosphofructokinase by ATP. Phosphofructokinase is the first enzyme in the respiration
pathway. Explain the meaning of allosteric inhibition using this example.
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(4)
4

(Total 8 marks)

5.

Consider the metabolic pathway shown below.


1

If there is end-product inhibition, which product (B to E) would inhibit which enzyme (1 to 4)?
Product

Enzyme

A.

B.

C.

D.

1
(1)

6.

Alcohol dehydrogenase is an enzyme that catalyses the reversible reaction of ethanol and ethanal
according to the equation below.
NAD+CH3CH2OH

CH3CHO+NADH+H+

ethanol

ethanal

The initial rate of reaction can be measured according to the time taken for NADH to be
produced.
In an experiment, the initial rate at different concentrations of ethanol was recorded (no
inhibition). The experiment was then repeated with the addition of
-3
l mmol dm 2,2,2-trifluoroethanol, a competitive inhibitor of the enzyme. A third experiment
-3
using a greater concentration of the same inhibitor (3 mmol dm ) was performed. The results for
each experiment are shown in the graph below.
1 .2
1 .1
1 .0
0 .9
0 .8
0 .7
I n itia l r a te o f r e a c tio n 0 .6
0 .5
/ a rb itra ry u n its
0 .4
0 .3
0 .2
0 .1
0 .0

n o in h ib itio n
1 m m o l d m 3 in h ib ito r
3 m m o l d m 3 in h ib ito r
0

10

20

30

40

50

60

70

E th a n o l c o n c e n tra tio n / m m o l d m

80

90

100

[Source: R Taber, Biochemical Education, (1998) 26, pages 239-242]

(a)

Outline the effect of increasing the substrate concentration on the control reaction (no
inhibition).
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(2)

(b)

(i)

State the initial rate of reaction at an ethanol concentration of 50 mmol dm


in the presence of the inhibitor at the following concentrations.

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...................................................................................................

1 mmol dm :
3 mmol dm :

(1)

(ii)

State the effect of increasing the concentration of inhibitor on the initial rate of
reaction.
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(1)

(c)

Explain how a competitive inhibitor works.


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(3)
(Total 7 marks)

7.

(a)

Explain the significance of secondary structure to the structure of a protein.


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(3)

(b)

State the name of a competitive enzyme inhibitor.


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(1)

(c)

Outline the difference between competitive and non-competitive enzyme inhibitors.


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(2)
(Total 6 marks)

8.

What can reduce the effect of a competitive inhibitor of an enzyme?


A.

Decrease the temperature at which the reaction takes place.

B.

Increase the temperature at which the reaction takes place.

C.

Increase the substrate concentration.

D.

Add a non-competitive inhibitor.


(1)

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(3)

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(b)

State the name of a competitive enzyme inhibitor.


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(1)

(c)

Outline the difference between competitive and non-competitive enzyme inhibitors.


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(2)
(Total 6 marks)

9.

Outline enzyme-substrate specificity.


(Total 5 marks)

(2)
(Total 6 marks)

10.

Explain how allosteric control of metabolic pathways by end-product inhibition includes


negative feedback and non-competitive inhibition.
(Total 8 marks)

11.

Explain the effect of substrate concentration on enzyme activity.


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(Total 3 marks)

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12.

(a)

Outline the induced fit model of enzyme activity.


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(3)

(b)

(i)

State two products of the light-dependent reactions of photosynthesis.


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.....................................................................................................................................
(2)

(ii)

Explain the light-independent reactions in photosynthesis.


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(4)
(Total 9 marks)

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13.

What is the advantage of using pectinase in fruit juice production?


A. The pectin content of the fruit is increased, making the nutritional value of the juice higher.
B. The pectin content of the fruit is reduced, making the energy content of the juice lower.
C. The pectin content of the fruit is reduced, making the juice easier to extract.
D. The pectin content of the fruit is increased, giving the juice a thicker texture.
(1)

14.

What effect do enzymes have on the activation energy of exergonic and endergonic reactions?
Activation
energy of
exergonic
reactions

Activation
energy of
endergoni
c
reactions

A.

increases

increases

B.

decreases

decreases

C.

increases

decreases

D.

decreases

increases
(1)

15.

Outline two examples of the commercial application of enzymes in biotechnology.


(Total 6 marks)

16.

The enzyme aspartate carbomyltransferase (ACTase) is a key regulatory enzyme in nucleotide


metabolism in bacteria. The activity of this enzyme was studied in the bacterium Helicobacter
pylori, an important human pathogen. ACTase activity and the growth of H. pylori were
measured at different concentrations of carbomoyl aspartate (CAA), the end product of the
reaction catalysed by ACTase.

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100

100

75

75

A C T a s e a c tiv ity / 5 0
% o f c o n tro l

50
K ey:
A C T a s e a c tiv ity
H . p y lo r i g ro w th

25
0

10

20

G ro w th /
% o f c o n tro l

25

30

40

50

C o n c e n tra tio n o f c a rb a m o y l a s p a rta te / m m o l d m

60

[Source: Burns, et al., Biological Procedures Online, (1998), www.biologicalprocedures.com]

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(a)

(i)

State the growth of H. pylori at a CAA concentration of 30 mmol dm .


.....................................................................................................................................
(1)

(ii)

Calculate the change in ACTase activity between CAA concentrations of 20 and 40


3
mmol dm .
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(1)

(b)

Compare the effect of increasing CAA concentration on the growth of H. pylori and
ACTase activity.
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(2)

(c)

Explain the effect of CAA on ACTase activity.


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(2)

(d)

Suggest a direct medical application of this information.


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(1)
(Total 7 marks)

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17.

Which of the following could cause denaturation of an enzyme?


A.

Substrate concentration

B.

A competitive inhibitor

C.

High temperature

D.

Low salt concentration


(1)

18.

The graph below shows the effect of changing the substrate concentration on an enzyme
controlled reaction.

4 0 % s u b s tra te
2 0 % s u b s tra te
1 0 % s u b s tra te
A m o u n t o f p ro d u c t fo rm e d
5 %

s u b s tra te

2 .5 % s u b s tra te
0 % s u b s tra te
T im e
What is the correct interpretation of these data?
A.

The rate of reaction increases continuously with increase in substrate concentration.

B.

The rate of reaction decreases continuously with increase in substrate concentration.

C.

The rate of reaction increases up to a point and then remains constant.

D.

The rate of reaction is not affected by any change in the substrate concentration.
(1)

19.

How does the enzyme pectinase help in fruit juice production?


A.

Pectinase increases the amount of protein in the juice extracted.

B.

Pectinase decreases the lipid content of the juice extracted.

C.

Pectinase increases the volume of the juice extracted.

D.

Pectinase eliminates toxins from the juice extracted.

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(1)

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20.

In the enzyme controlled pathway shown below, which compound is most likely to inhibit
enzyme (w)?

Precursor
A.

B.

II

C.

III

D.

IV

enzyme
w

enzyme
x
I

enzyme
y
II

enzyme
z
III

IV

(1)

21.

(a)

Describe the role of skin arterioles in the regulation of body temperature.


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(3)

(b)

Explain how temperature affects the rate of transpiration from a typical mesophytic plant.
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(3)

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(c)

Explain the role of temperature on enzyme activity.


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(3)
(Total 9 marks)

22.

Outline two examples of the commercial application of named enzymes in biotechnology.


(Total 6 marks)

23.

Explain competitive and non-competitive inhibition, including allostery.


(Total 8 marks)

24.

Enzymes are used by living organisms to catalyse reactions. Some of these reactions occur in the
cytoplasm of cells. Other reactions take place outside cells, for example the digestion of foods in
the human gut.
(a)

State the name used by biochemists for the chains and cycles of reactions that occur
inside cells.
...............................................................................................................................................
(1)

20

(b)

Enzymes of digestion in humans are secreted by glands. They have a pH optimum which
allows them to work efficiently in the part of the gut into which they are secreted.
(i)

In the table below, identify the missing enzyme, the two glands, and the pH
optimum
Name of
enzyme

amylase

Gland
secret
ing
the
enzy
me

Substr
a
t
e

Products

starch

maltose

triglyce
ri
d
e
s

fatty acids
and
glyc
erol

pH optimum

(4)

(ii)

Outline the effect of pH values above and below the optimum on enzyme structure.
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(2)

(c)

Enzymes that work inside cells are sometimes affected by non-competitive inhibitors.
Explain how a non-competitive inhibitor affects the activity of an enzyme.
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(3)
(Total 10 marks)

21

25.

(a)

(i)

increasing fructose 6-phosphate concentration (initially) causes an increase


in activity;
activity levels out / remains constant as (substrate) concentration continues
to rise;
2

(ii)

more collisions with active site as concentration rises;


at high substrate levels all active sites are occupied so no further increase
in rate / enzyme working at maximum rate;

22

(b)

(i)

decreases activity;
at all fructose 6-phosphate concentrations;
most effect at intermediate fructose 6-phosphate concentrations / little difference
at high fructose 6-phosphate concentrations;
ATP acts as an inhibitor;
2 max

(ii)

end-product inhibition;
respiration rate decreased if ATP already available;

1 max
[7]

26.

(a)

the site (on the surface of an enzyme) to which substrate(s) bind / the site (on the
enzyme) where it catalyzes a chemical reaction;
1

(b)

bring substrates close together in active site / in correct orientation;


forms enzyme-substrate complex / substrate(s) bind to active site;
lowers the activation energy for the reaction;
weakens bonds in the substrate;

2 max

(c)

enzymes have an optimal pH;


lower activity above and below optimum pH / graph showing this;
too acidic / basic pH can denature enzyme;
change shape of active site / tertiary structure altered;
substrate cannot bind to active site / enzyme-substrate complex cannot form;
hydrogen / ionic bonds in the enzyme / active site are broken / altered;
3 max

(d)

energy storage / source of energy / respiration substrate;


(heat) insulation;
protection (of internal organs);
water proofing / cuticle;
buoyancy;
(structural) component of cell membranes;
electrical insulation by myelin sheath;
(steroid) hormones;
glycolipids acting as receptors;
Three correct [2], one or two correct [1].

2 max

Use one tick to mark the first one or two correct answers. Use a second tick to mark the
third correct answer. Mark the first three answers only.
[8]

23

27.

enzymes have an active site;


that fits the substrate precisely;
changes in the chemical environment of the enzyme can lead to a
shape/conformational change in the protein;
leading to a change in the shape of the active site;
may interfere with the binding of the substrate with the active site;
altering pH can alter intermolecular interactions within the protein;
or within the active site;
enzymes have an optimum pH;
increase in temperature can increase molecular motion leading to
disruption of intermolecular interactions;
increases chance of enzyme substrate collisions so enzyme activity increases;
optimal temperature;
temperature changes / pH changes can denature the protein;
the more substrate, the more product / more enzyme-substrate complex forms;
after a point, all active sites are bound to substrate / all active sites occupied;
additional substrate will not lead to a greater rate of product formation at
this point;
For full marks all three conditions must be included, otherwise award [6 max].
[Plus up to [2] for quality]

8 max
[8]

28.

(a)

(b)

(c)

Any two from the following.


fibrous: e.g. fibrin, collagen (do not accept "tendon");
globular: e.g. hemoglobin, fibrinogen, amylase (do not accept "enzyme");
a new reaction pathway is created;
activation energy is reduced;
the equilibrium for the reaction is achieved more quickly /
the reaction is faster;

2 max

ATP inhibits phosphofructokinase at (allosteric) site away from the active site;
inhibition alters the enzymes conformation / structure;
the active site does not accept the substrate molecule;
when respiration increases ATP levels phosphofructokinase is inhibited;
respiration slows down;
phosphofructokinase is the first enzyme in the respiration pathway so
there is no build up of metabolic intermediates;
as ATP is used up by the cell the inhibition of phosphofructokinase is reduced;
respiration speeds up again;
this is an example of negative feedback;
4 max
[8]

29.

D
[1]

30.

(a)

directly proportional / greater concentration, greater rate of reaction;


at high concentrations the increase is smaller / plateau / levels-off (at
3
approximately 70 mmol dm );

2
24

(b)

(i)

1 mmol dm : 0.70 ( 0.02)


3
3 mmol dm : 0.55 ( 0.02)
3
Both needed for [1]. For 1 mmol dm accept 0.7.

1 max

25

(ii)

(c)

lower reaction rate at inhibitor concentration of 3 mmol dm / the greater the


inhibitor concentration the slower the rate of reaction;
trend / overall shape are the same / increases but then levels-off;
but lower at greater concentration of inhibitor;
1 max

substrate and inhibitor (structurally) similar;


inhibitor binds to active site;
prevents substrate from binding;
activity of enzyme prevented;
named example (e.g. malonate inhibits succinate dehydrogenase as
it is similar to succinate);

3 max
[7]

31.

C
[1]

32.

active site of enzyme binds to specific substrate;


shape of the active site and substrate fit/complement each other;
lock and key model;
chemical properties of substrate and enzyme attract / opposite charges;
enzyme/active site is not rigid and substrate can induce slight changes in shape;
allows substrates of similar structure to bind with same enzyme;
induced fit;
causes weakening of bonds in substrate to lower activation energy;
[5]

33.

allosteric enzyme has binding site(s) away from/other than the active site;
(shape of an) allosteric enzyme alternates between active and inactive (form);
non-competitive inhibitor binds to allosteric site/away from active site;
non-competitive inhibitor changes shape of active site;
non-competitive inhibitors do not compete with substrate for the active site;
end-product can inhibit enzyme needed for early/first step in metabolic pathway;
negative feedback since increased level of product decreases rate of its own production;
metabolic pathway regulated according to the requirement for its end-product;
idea that inhibition is reversible;
Award [1] for named enzyme and [1] for its non-competitive/end-product inhibitor.
[8]

34.

(a)

substrate binds / approaches active site;


shape of active site changes;
bonds in substrate weaken;
activation energy decreases;
explains broad specificity of some enzymes;
e.g. proteases;

3 max

26

(b)

(i)

oxygen;
+
NADPH / NADPH + H / NADPH2;
ATP;

2 max

27

(ii)

occurs in stroma of chloroplast;


ribulose disphosphate / RuBP / 5-C sugar combines with CO2;
catalyzed by rubisco / ribulose biphosphate carboxylase;
splits into two 3-C sugars / glycerate 3-phosphate;
ATP and NADPH supply energy and H;
3-C sugars join to form glucose / 6-C sugar;
RuBP regenerated (with use of ATP);

4 max
[9]

35.

C
[1]

28