3 Enzymes Paper 2 - N-MQ

A LEVEL Biology
3. Enzymes
Classified by Adeel Ahmad

Classified Past Papers Biology 9700
3. Enzymes
9700/21/M/J/12
4 Penicillin is an antibiotic that interferes with the synthesis of cell walls in bacteria. Even before
penicillin became widely available in the 1940s, the enzyme penicillinase which breaks down
penicillin had been isolated. This enzyme is now found in many bacteria and gives them
resistance to penicillin.
Fig. 4.1 is a ribbon model of the structure of the enzyme penicillinase. The arrow indicates
the active site of the enzyme.
Fig. 4.1
(a) Explain why the shape of the active site of an enzyme, such as penicillinase, is important.
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Classified by Adeel Ahmad 3. Enzymes

Paper 2 - 1
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(b) With reference to Fig. 4.1, identify the aspects of protein structure that are shown and For
those that are not shown. Examiner’s
Use
aspects of protein structure shown
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aspects of protein structure not shown
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Fig. 4.2 shows the changes in energy during the progress of an uncatalysed reaction.
energy
progress of the reaction
Fig. 4.2
(c) (i) Draw on Fig. 4.2 a curve to show changes in energy during the progress of the
same reaction when catalysed by an enzyme. [2]
(ii) State the term given to the energy level that must be overcome before a reaction
can progress.
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© UCLES 2012 9700/21/M/J/12 Paper 2 - 2
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For
9700/22/M/J/12 Examiner’s
5 (b) NQR is an important respiratory enzyme located in the cell surface membrane of the
bacterium that causes cholera.
A student suggested that an inhibitor of the enzyme NQR could be used as a drug in the
prevention and control of cholera.
Suggest and explain how this inhibitor would function.
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9700/22/O/N/12
(e) DNA polymerase is an enzyme involved in the replication of DNA. For
Examiner’s
One of the substrates required by DNA polymerase is ATP. Use
ara-ATP is a chemical that affects DNA polymerase activity.
In an investigation, the effect of different concentrations of ATP on the rate of DNA

synthesis was determined:
• with no ara-ATP
• with a low concentration of ara-ATP
• with a high concentration of ara-ATP.
The results of the investigation are shown in Fig. 5.1.
6 no-ara ATP
5 5 +M ara ATP
rate of DNA synthesis 4

/ arbitrary units
20 +M ara ATP
3
0
0
10 20 30 40 50 60
ATP concentration / +M
Fig. 5.1
Explain, in terms of the mode of action of enzymes, the results of the investigation
shown in Fig. 5.1.
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© UCLES 2012 9700/22/O/N/12
3. Paper
Enzymes
2-4
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9700/22/M/J/13
In some organisms, trehalose is used as an energy store and gives protection against
the harmful effects of very low temperatures. Trehalose is sometimes referred to as a
cryoprotectant, allowing organisms to survive in freezing conditions.
Freezing temperatures can damage the cell surface membrane and membranes within the
cell.
(d) Freezing temperatures can also completely stop enzyme activity by causing the
molecules to undergo ‘cold denaturation’. Enzyme activity is not recovered when
temperatures are increased to a normal working temperature range.
(i) Explain the mode of action of enzymes.
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(ii) Suggest how the molecular structure of the enzyme changes during ‘cold
denaturation’.
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(e) Cryoprotectants, such as trehalose, are of particular interest in their application to For
preserving cells, tissues or organisms for future use. Examiner’s
Use
An investigation was carried out to find the protective effect given by different
concentrations of two cryoprotectants, trehalose and glycerol, on a respiratory enzyme.
The enzyme was subjected to a freezing temperature and then returned to its optimum
temperature. The activity of the enzyme was measured at its optimum temperature.
Fig. 4.2 is a graph showing the results of the investigation.
100
80
percentage 60
of maximum
activity 40
20
0
0 20 40 60 80 100
cryoprotectant concentration / mmol
trehalose
glycerol
Fig. 4.2
With reference to Fig. 4.2, describe the results of the investigation.
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© UCLES 2013 9700/22/M/J/13
3. Paper
Enzymes
2-6
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9700/23/M/J/13 For
Examiner’s
Use
4 The enzyme, catechol oxidase, causes a brown colour to develop when slices of many fruits,
such as apples, are exposed to air.
The enzyme catalyses the following reaction:
catechol oxidase
catechol + oxygen quinone + water
Quinone is then immediately further oxidized in air to a brown-coloured substance. Catechol

and quinone are colourless.
A student investigated the rate of this reaction under different conditions.
(a) State how the student could follow the progress of this reaction.
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In the first investigation, the student measured the initial rate of the reaction in varying
concentrations of catechol. The results are shown in Fig. 4.1.
80
70
60
initial rate 50
of reaction
/ arbitrary
40
units
30
20
10
0
0 1 2 3 4 5 6 7 8
concentration of catechol / mM
Fig. 4.1

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(b) Explain the results shown in Fig. 4.1. For

Examiner’s
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(c) In a second investigation, the student repeated the experiment, but this time added a
competitive inhibitor, para-hydroxybenzoic acid (PHBA), to each reaction mixture.
(i) Sketch on Fig. 4.1 the results that would be obtained for this second investigation.
[2]
(ii) Explain the effect that PHBA will have on the action of phenoloxidase.
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(d) Lemon juice contains citric acid. Adding even a small amount of diluted lemon juice to
apple slices slows the appearance of the brown colour.
Suggest an explanation for this observation.
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For
Examiner’s
9700/22/O/N/13 Use
(b) Chitin and the products of chitin hydrolysis have many useful medical and environmental
applications. Chitinase enzymes can be used commercially to hydrolyse chitin. Enzyme
stability and activity are important considerations in technological applications of
chitinase.
Fig. 2.2 is a graph showing the effects of temperature on chitinase extracted from a soil
bacterium.
The relative activity of the enzyme was measured at different temperatures, with 100%
representing maximum enzyme activity.
100
80
60
relative
activity / %
40
20
0
0 10 20 30 40 50 60 70
temperature / °C
Fig. 2.2
(i) With reference to Fig. 2.2, state the optimum temperature for the chitinase enzyme.
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Fig. 2.3 is a graph showing how temperature affects the stability of chitinase. The activity For
of the enzyme was measured over a time period of 72 hours at each of five different Examiner’s
temperatures. Use
100
80
28 °C
60 37 °C
relative
activity / %
40 40 °C
20
50 °C
0 60 °C
0 4020 60 80
time / h
Fig. 2.3
(ii) With reference to Fig. 2.2 and Fig. 2.3, describe and discuss the effect of
temperature on chitinase activity and stability.
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5 Animals do not have the ability to produce enzymes to digest cellulose. Most herbivores
have bacteria in their digestive systems that can digest cellulose.
Fig. 5.1 shows the results of a study on 24 different herbivores. The percentage of cell wall
material that was digested by each animal was determined. The time taken for the plant
material to pass through the digestive system, the retention time, was also recorded.
70
65
60
percentage
of cell wall 55
material
digested 50
45
40
35
30
0 10 20 30 40 50 60 70 80 90 100
retention time / h
Fig. 5.1

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(b) (i) With reference to Fig. 5.1, describe the results of this study.
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6 (c) Some enzymes are found in phloem tissue.
Describe how enzymes catalyse reactions.
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(c) Type 2 diabetes (insulin-independent diabetes) is a non-infectious disease.
If not treated, this disease is characterised by large fluctuations in the concentration of

glucose in the blood.
Maltase is an enzyme that completes the digestion of starch in humans. Molecules of maltase
are bound to the microvilli of epithelial cells in the small intestine.
Ascorbase is a drug used in the treatment of type 2 diabetes. Molecules of ascorbase have a
very similar shape to that of the substrate for maltase.
(i) Explain how ascorbase acts to inhibit these membrane-bound enzymes.
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(ii) Suggest why ascorbase can be used to treat people who have type 2 diabetes.
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[Total: 12]

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3 The enzyme glutamyl-tRNA reductase (GluTR) is present in many bacteria to make a product
which is essential to their survival.
GluTR acts on the substrate glutamyl-tRNA, which is composed of the amino acid glutamic acid
attached to a tRNA.
Fig. 3.1 shows the structure of glutamyl-tRNA and another compound called glutamycin.
CH3 CH3
NH2 N
rest of N N N N
tRNA OH
N N tRNA portion N N
CH2 O CH2 O
OH O N OH
O O
H2N H 2N
COOH COOH
glutamyl-tRNA glutamycin
Fig. 3.1
(a) Explain how glutamycin can act as an inhibitor for the enzyme GluTR.
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(e) Before acclimatisation can occur, some people develop a condition known as acute mountain
sickness when they travel to high altitude areas.
Acetazolamide is a non-competitive enzyme inhibitor that is used as a drug to prevent and
treat acute mountain sickness.
Explain the effects of a non-competitive inhibitor on the rate of enzyme activity.
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3.Paper
Enzymes
2 - 16
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4 Fig. 4.1 is a computer-generated image of the enzyme hexokinase binding with its substrate,
glucose. The product of the enzyme-catalysed reaction is glucose-6-phosphate.
hexokinase
glucose
Fig. 4.1
(a) Hexokinase binds with glucose using the induced fit mechanism.
Describe how an enzyme-substrate complex forms by this mechanism.
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(b) Suggest how enzymes which use the induced fit mechanism can be less affected by
competitive inhibitors than those which use the lock and key mechanism.
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(c) When a solution of the enzyme hexokinase is heated to 45 °C for 10 minutes, the quantity of
product formed decreases by 50% compared to a sample kept between 30 °C and 40 °C.
Explain this result.
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9700/21/M/J/15
4 (a) Fig. 4.1 shows two ways in which enzymes interact with their substrates.
substrate
enzyme A
enzyme B
Fig. 4.1
Explain the difference between the two ways in which enzymes interact with their substrates
as shown in Fig. 4.1.
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4 Many microorganisms can digest cellulose by using a group of enzymes collectively known as
cellulases. Cellobiose is the disaccharide produced during cellulose digestion.
The cellulase known as β-glucosidase completes the digestion of cellulose by hydrolysing the
cellobiose molecule to produce two β-glucose molecules.
(b) β-glucosidase was extracted from two different bacteria, Agrobacterium tumefaciens and
Thermotoga maritima.
Fig. 4.1 shows the results of an investigation into the effect of temperature between 0 °C and
100 °C, on the activity of each enzyme.
• L represents the lowest temperature at which activity of each enzyme was detected.
• H represents the highest temperature at which activity of each enzyme was detected.
100
80
relative
activity /
% of
maximum 60 H
activity
40
L
20
L
H
0
0 20 40 60 80 100
temperature / °C
Key
enzyme A (extracted from A. tumefaciens)
enzyme T (extracted from T. maritima)
Fig. 4.1

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(i) With reference to Fig. 4.1, describe the differences in the results for the two enzymes,
A and T.
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(ii) Both enzyme A and enzyme T act on cellobiose. They have a similar, but not identical,
primary structure.
Suggest how similarities and differences in the primary structure of the two enzymes
could help to explain the results obtained in the investigation.
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(d) Angiotensin is a polypeptide produced in the body to raise blood pressure.

Angiotensin converting enzyme (ACE) catalyses the final step in angiotensin production.
Fig. 4.2 shows this step.
10 amino acid polypeptide: Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu
ACE
His-Leu
angiotensin: Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
Fig. 4.2
(c) People with high blood pressure can be treated with a drug which lowers the concentration of
angiotensin in the blood.
This drug is a competitive inhibitor of ACE.
Explain how this drug acts as a competitive inhibitor.
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5 (d) The measles pathogen must carry out RNA replication to make new RNA molecules for the
new pathogens. This happens inside the infected cell.
The pathogen carries its own enzyme for RNA replication, but no other enzymes.
Explain why the measles pathogen cannot use an enzyme from the cell to carry out RNA
replication.
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(c) The synthesis and release of elastase enzymes by macrophages and neutrophils is an
important feature in the development and progression of emphysema. Elastase causes the
breakdown of the protein elastin, the main component of elastic fibres.
(i) Explain what is meant by an enzyme.
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(ii) Elastase has an active site with a specific shape. The mode of action of this enzyme
supports the lock and key hypothesis.
Explain the mode of action of elastase.
You may use the space below to draw a diagram or diagrams to help your answer.
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There are two inhibitors of elastase that are produced in the body, TIMP-1 and A1AT:
• macrophage elastase is inhibited by TIMP-1
• neutrophil elastase is inhibited by A1AT.
The inhibitors can be inactivated by the elastase enzymes:
• macrophage elastase can inactivate A1AT
• neutrophil elastase can inactivate TIMP-1.
In healthy lungs, the activity of elastase enzymes is regulated. Tobacco smoke can disrupt
this regulation.
(i) One effect of tobacco smoke is to cause changes in the structure of A1AT, a competitive
inhibitor.
Suggest how structural changes to A1AT will affect its mode of action.
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3 The enzyme catalase is found in many plant and animal tissues.
The enzyme catalyses the decomposition of hydrogen peroxide, which is a toxic product of
metabolism. The reaction is:
catalase
2H2O2 O2 + 2H2O
A research team investigated the activity of two forms of catalase, P and Q, extracted from
Anopheles gambiae, an important vector of malaria. The team investigated the effect of increasing
concentrations of hydrogen peroxide on the activity of these two forms of catalase.
The results are shown in Fig. 3.1.
140
catalase P
120
100
catalase Q
80
activity of catalase
/ arbitrary units 60
40
20
0
0 50 100 150 200 250 300
concentration of hydrogen peroxide / mM
Fig. 3.1
(a) With reference to Fig. 3.1, describe and explain the effect of increasing the concentration of
hydrogen peroxide on the activity of catalase P.
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(b) Each molecule of catalase consists of four identical polypeptides. The two forms of catalase in
A. gambiae differ by only one amino acid at position 2 in the amino acid sequence. Catalase P
has serine and catalase Q has tryptophan.
Suggest how the difference in one amino acid is responsible for the lower activity of catalase Q
compared with catalase P.
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(c) Female mosquitoes feed on blood in order to produce their eggs. After feeding, the metabolic
rate increases for egg production.
The researchers allowed female mosquitoes to feed on blood. They found that female
mosquitoes with only catalase P produced more eggs than those with only catalase Q.
Suggest why there is a difference in egg production between the two types of A. gambiae.
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(d) Metal ions can act as a non-competitive inhibitor of catalase.
Explain how copper ions can act as a non-competitive inhibitor.
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(b) The activity of a phosphatase enzyme was measured at different values of pH by using nine
different buffer solutions. The temperature was kept constant at 30 °C.
5.0
4.5
4.0
3.5
3.0
phosphatase activity
/ arbitrary units 2.5
2.0
1.5
1.0
0.5
0.0
0 1 2 3 4 5 6 7 8 9 10
pH
Fig. 4.1
(i) With reference to Fig. 4.1, describe the effect of pH on the activity of phosphatase.
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(ii) Explain why the activity of phosphatase at pH 1 is very low.
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(c) DNA can be produced commercially for use in genetic engineering. Sometimes
dephosphorylated DNA is required. This involves removal of the terminal phosphate groups
using immobilised phosphatases.
(i) State one way of immobilising an enzyme.
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(ii) Apart from a cost beneﬁt, suggest one advantage of using immobilised phosphatase to
produce dephosphorylated DNA.
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1 Statements A to E are about the structure and functioning of enzymes.
State the correct term to match each of the statements A to E.
A The energy level, lowered by enzyme action, that needs to be overcome by reactants in order
for products to be formed.
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B The mechanism of enzyme action that relies on the active site being partially flexible and
changing shape in order to bind the substrate.
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C The term to describe a protein, such as an enzyme, with a tertiary or quaternary structure
that results in an approximately spherical shape.
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D The term for enzymes that function outside cells.
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E The concentration of substrate that enables an enzyme to achieve half the maximum rate of
reaction.
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2 Trypsin is a protease enzyme found in the digestive system.
Fig. 2.1 shows how the substrate concentration affects the rate of reaction of trypsin.
3.5
3.0
2.5
rate of 2.0
reaction
/ +M min –1 1.5
1.0
0.5
0
0 0.1 0.2 0.3 0.4 0.5 0.6
substrate concentration / mM
Fig. 2.1
(a) Use Fig. 2.1 to:
(i) determine Vmax for trypsin
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(ii) calculate Km for trypsin.
Show your working.
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(b) Describe and explain the shape of the curve in Fig. 2.1.
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(c) Trypsin is composed of one polypeptide chain of 223 amino acids.
The active site of trypsin contains three amino acids which catalyse a hydrolysis reaction.
These three amino acids occupy the following positions in the primary structure of trypsin:
• histidine, position 57
• aspartate, position 102 Concept of Protein Structure (Topic 2) is required
ADEEL AHMAD
• serine, position 195.
(i) In the functioning enzyme, these three amino acids are close together in the active site.
Explain how the structure of the protein makes this possible.
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(ii) When trypsin acts on a substrate, another substance is required as a reactant.
Name this other substance.
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3 (b) Lysozyme hydrolyses the β-1,4 glycosidic bonds present in compounds found in bacterial cell
walls.
(iii) Lysozyme uses the induced fit mechanism.
Explain the mode of action of an enzyme that uses the induced fit mechanism.
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(c) In human tears and saliva, lysozyme acts as an extracellular enzyme.
State what is meant by the term extracellular.
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© UCLES 2016 9700/21/O/N/16 Paper 2 - 32
7
(d) Fig. 3.2 shows the results of an investigation into the effect of substrate concentration on the
rate of reaction catalysed by lysozyme.
4
rate of
reaction
/ μmol min–1
3
0
0 1 2 3 4 5
substrate concentration / mmol
Fig. 3.2
Use Fig. 3.2 to:
(i) state the lowest substrate concentration to give the maximum rate of reaction, Vmax
.......................................................................................................................................[1]
(ii) determine the Michaelis-Menten constant, Km.
Km = ...........................................................[1]
(e) The investigation was repeated in the presence of a competitive inhibitor of lysozyme.
Draw a curve on Fig. 3.2 to show the expected results. [2]
[Total: 13]

© UCLES 2016 9700/21/O/N/16 Paper 2 - 33
9700/22/O/N/16 8
3 (b) The glucose isomerase used in the production of high fructose corn syrup is extracted from a
strain of a bacterium, Thermus thermophilus, which is found in hot springs. The enzyme has
an optimum temperature of 95 °C.
Suggest and explain the advantages of using glucose isomerase from T. thermophilus to
produce high fructose corn syrup, rather than using glucose isomerase that has an optimum
temperature of 37 °C.
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...............................................................................................................................................[3]

© UCLES 2016 9700/22/O/N/16 Paper 2 - 34
9
(c) The commercial production of high fructose corn syrup uses immobilised glucose isomerase.
Fig. 3.1 shows the effect of pH on the activity of immobilised glucose isomerase compared to
glucose isomerase free in solution.
100
immobilised glucose
isomerase
(immobilised enzyme)
80
percentage
activity
60 glucose isomerase
free in solution
(free enzyme)
40
20
0
6 7 8 9
pH
Fig. 3.1
With reference to Fig. 3.1, describe the differences shown between the immobilised enzyme
and the free enzyme as pH changes.
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...............................................................................................................................................[3]

© UCLES 2016 9700/22/O/N/16 Paper 2 - 35
9700/23/O/N/16 4
2 (a) Explain how enzymes lower the activation energy needed to allow reactions to proceed.
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...............................................................................................................................................[2]
(b) Folic acid is a molecule used by all cells for growth. Bacteria cannot absorb folic acid from
their surroundings. Bacteria use an enzyme to make a molecule called PABA. PABA is used
to make folic acid.
An investigation was carried out to determine the effect on the production of PABA when
the concentration of an enzyme inhibitor is increased. Four different concentrations (1 µM to
30 µM) of the inhibitor were used, together with a control with no inhibitor.
The concentration of PABA produced in each reaction mixture was determined at 10 minute
intervals.
5 concentrations
of inhibitor
no inhibitor
1 μM
4
concentration
of PABA
produced / μM
3 μM
3
10 μM
2
30 μM
1
0
0 10 20 30 40 50 60
time / min
Fig. 2.1

© UCLES 2016 9700/23/O/N/16 Paper 2 - 36
5
(i) Use Fig. 2.1 to describe the results of the investigation.
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
.......................................................................................................................................[4]
(ii) Outline an experiment that could be carried out to determine whether the inhibitor of the
enzyme that catalyses the reaction to produce PABA is competitive or non-competitive.
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
.......................................................................................................................................[3]
(iii) Folic acid from the diet is able to enter human cells, but is not able to cross bacterial cell
walls. Human cells do not have an enzyme to make PABA.
Suggest why the inhibitor of this enzyme could be used as a drug to treat bacterial
infections in humans.
...........................................................................................................................................
...........................................................................................................................................
.......................................................................................................................................[1]

© UCLES 2016 9700/23/O/N/16 Paper 2 - 37
9700/22/F/M/17 6
3 Catalase is an enzyme that catalyses the breakdown of hydrogen peroxide, a toxic waste product
of metabolism.
catalase
2H2O2 2H2O + O2
Fig. 3.1 shows the results of an investigation into the effect of hydrogen peroxide concentration
on the rate of the catalase-controlled reaction, with and without the presence of two different
inhibitors.
10
X
8 Y
6
rate of reaction
/ arbitrary units Z
4
0
0 5 10 15 20 25
hydrogen peroxide concentration / mmol dm–3
Fig. 3.1
(a) The inhibitors used in the investigation have different modes of action.
Identify which of curves X, Y and Z are the results for:
• the reaction with the non-competitive inhibitor

• the reaction with the competitive inhibitor
• the reaction without any inhibitor.
non-competitive inhibitor ......................
competitive inhibitor ......................
without any inhibitor ......................

[1]

© UCLES 2017 9700/22/F/M/17 Paper 2 - 38
7
(b) With reference to Fig. 3.1, compare the maximum rate of reaction, Vmax, and the
Michaelis-Menten constant, Km, for curves X, Y and Z.
Vmax ..........................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
Km .............................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
[4]
Hydrogen peroxide has a harmful effect on cells. One effect is to damage DNA.
(c) Describe the structure of DNA.
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
.............................................................................................................................................. [4]

© UCLES 2017 9700/22/F/M/17 Paper 2 - 39
3
9700/21/M/J/17
2 Phosphatases are enzymes that catalyse the removal of phosphate groups from organic
compounds.
Some students investigated the effect of substrate concentration on the rate of the reaction
catalysed by an acid phosphatase (enzyme A). The results are shown in Fig. 2.1.
16
14
12
10
rate of reaction
/ μmol dm–3 8
min–1
6
0
0.0 0.5 1.0 1.5 2.0 2.5 3.0 3.5
concentration of substrate / mmol dm–3
Fig. 2.1
(a) The students used Fig. 2.1 to derive the Michaelis-Menten constant (Km) for enzyme A as
0.3 mmol dm–3.
Explain how they derived Km.
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...............................................................................................................................................[2]

© UCLES 2017 9700/21/M/J/17 Paper 2 - 40
4
(b) The students investigated a different phosphatase enzyme (enzyme B) and found the value
of Km to be higher than 0.3 mmol dm–3.
Explain the difference between the values of Km for these two phosphatase enzymes.
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...............................................................................................................................................[2]
(c) The students repeated their investigation on enzyme A with a competitive inhibitor.
They used the same concentrations of substrate as before, but added a competitive inhibitor
to each reaction mixture.
They used the same concentration of the inhibitor in each reaction mixture.
The students found that Vmax was the same as before, but Km was higher than
0.3 mmol dm–3.
Explain how the addition of the competitive inhibitor results in the same value for Vmax but a
higher value for Km.
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...............................................................................................................................................[4]
[Total: 8]

© UCLES 2017 9700/21/M/J/17 Paper 2 - 41
9700/22/M/J/17 4
2 Lipase is an enzyme with many commercial uses. Some species of bacteria are of great interest
as they produce large quantities of lipase.
(a) Complete Fig. 2.1 to show the hydrolysis of triglyceride by lipase.
lipase
triglyceride + ........................ .............................................................
Fig. 2.1
[2]
Researchers carried out investigations into lipase extracted from a bacterium found in hot springs.
(b) To measure the activity of the bacterial lipase during their investigations, the researchers
used a method based on the biological test for triglycerides.
Outline a biological test that could be carried out to show the presence of triglyceride in a
liquid mixture and describe the positive result for this test.
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...............................................................................................................................................[3]

© UCLES 2017 9700/22/M/J/17 Paper 2 - 42
5
(c) The researchers investigated the effect of pH values between pH 2.0 and pH 10.5 on the
activity of bacterial lipase in hydrolysing triglyceride at a temperature of 37 °C.
100
90
80
70
60
percentage
activity 50
40
30
20
10
0
1.0 2.0 3.0 4.0 5.0 6.0 7.0 8.0 9.0 10.0 11.0 12.0
pH
Fig. 2.2
With reference to Fig. 2.2, describe the effect of pH on the activity of bacterial lipase.
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...............................................................................................................................................[4]

© UCLES 2017 9700/22/M/J/17 Paper 2 - 43
6
(d) A separate investigation into the effect of pH on the same bacterial lipase compared the
enzyme free in solution with the enzyme immobilised by physical attachment to a stable
polymer.
At a temperature of 37 °C, the optimum pH of the enzyme free in solution was the same as
that shown in Fig. 2.2. The optimum pH of the immobilised enzyme was measured as pH 4.
(i) Suggest one reason to explain why the enzyme free in solution has a different optimum
pH compared to the immobilised enzyme.
...........................................................................................................................................
...........................................................................................................................................
.......................................................................................................................................[1]
(ii) Suggest one advantage of immobilising the extracted lipase for commercial use.
...........................................................................................................................................
...........................................................................................................................................
.......................................................................................................................................[1]
[Total: 11]

© UCLES 2017 9700/22/M/J/17 Paper 2 - 44
9700/23/M/J/17 6
2 (ii) Systemin stimulates plant cells to produce enzyme inhibitors known as serpins.
One of these serpins is a competitive inhibitor of some protease enzymes. It inhibits the
protease enzymes found in herbivores, but does not inhibit the proteases in plants.
Suggest how this serpin inhibits only the protease enzymes in herbivores but not those
in plants.
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
.......................................................................................................................................[3]
(iii) The presence of competitive inhibitors, such as serpins, increases the Michaelis-Menten
constant (Km) for the enzymes they inhibit.
Explain why the Km value increases.
...........................................................................................................................................
.......................................................................................................................................[1]

© UCLES 2017 9700/23/M/J/17 Paper 2 - 45
9700/21/O/N/17 9
4 An investigation was carried out to find out how the activity of starch phosphorylase varied with
temperature, when free in solution and when immobilised in alginate.
9 Key
free enzyme
8 immobilised enzyme
enzyme
5
activity
/ arbitrary
units 4
0
20 25 30 35 40 45 50 55
temperature / °C
Fig. 4.2
(d) With reference to Fig. 4.2, compare the results for the enzyme activity when free in solution
and when immobilised.
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...............................................................................................................................................[4]

© UCLES 2017 9700/21/O/N/17 Paper 2 - 46
10
(e) State how the Michaelis–Menten constant (Km) is derived from Vmax for an enzyme.
...................................................................................................................................................
...................................................................................................................................................
...............................................................................................................................................[1]
(f) The Km values for starch phosphorylase were determined when free in solution and when
immobilised.
The Km values were:
• free in solution, Km = 0.34 mmol dm–3
• immobilised, Km = 0.84 mmol dm–3.
Suggest an explanation for the difference between the two values.
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...............................................................................................................................................[2]
[Total: 13]

© UCLES 2017 9700/21/O/N/17 Paper 2 - 47
9700/22/O/N/17 6
3 Hydrolytic enzymes can function within the cell or can be secreted by the cell, where they are able
to catalyse reactions.
(a) State the term used to describe an enzyme that functions within the cell.
...............................................................................................................................................[1]
(b) The rates of reaction of two different hydrolytic enzymes, enzyme G and enzyme H, were
measured at different substrate concentrations. The results are shown in Fig. 3.1.
The two enzymes have different values of the Michaelis–Menten constant (Km).
1.0
enzyme G
0.8
enzyme H
0.6
rate of reaction
/ arbitrary units 0.4
0.2
0
0 5 10 15 20 25 30 35
substrate concentration / mmol dm–3
Fig. 3.1
(i) The Km value of enzyme G is 5 mmol dm–3.
Use Fig. 3.1 to derive the Km value for enzyme H.
Show your working.
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
.......................................................................................................................................[2]
(ii) With reference to Fig. 3.1, explain how the values of Km for these enzymes provide
information about the relationship between the enzyme and their substrates.
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
.......................................................................................................................................[2]

© UCLES 2017 9700/22/O/N/17 Paper 2 - 48
9700/22/F/M/18 9
3 (b) On a commercial scale, immobilised lactase can be used to produce lactose-free milk.
One of the products of the reaction shown in Fig. 3.1 acts as an inhibitor of lactase. This is an
example of product inhibition.
(i) Suggest why product inhibition is useful in K. lactis when lactase is acting as an
intracellular enzyme, but can be a disadvantage when extracted lactase is used free in
solution for the production of lactose-free milk.
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...................................................................................................................................... [2]
(ii) Suggest how using immobilised lactase in a commercial application helps to reduce the
problem of product inhibition.
...........................................................................................................................................
...................................................................................................................................... [1]
(iii) The first large-scale production of lactose-free milk with an immobilised enzyme used
lactase trapped in cellulose triacetate fibres.
Suggest one feature of cellulose triacetate that makes it useful as an immobilising
material.
...........................................................................................................................................
...................................................................................................................................... [1]
(c) For a commercial application using an enzyme, the progress of the enzyme-catalysed
reaction needs to be studied.
Outline how the progress of an enzyme-catalysed reaction can be investigated experimentally.
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
.............................................................................................................................................. [3]

© UCLES 2018 9700/22/F/M/18 Paper 2 - 49
9700/21/M/J/18 6
3 Researchers isolated a sucrase enzyme from the bacterium Bacillus subtilis. They immobilised
the enzyme in alginate beads.
The researchers investigated the effects of temperature on the activity of the immobilised sucrase
compared with the activity of the same enzyme free in solution.
100
key
immobilised
sucrase
80 sucrase free in
solution
percentage of 60
maximum
enzyme
activity
40
20
0
40 45 50 55 60 65 70 75 80
temperature / °C
Fig. 3.1
(a) With reference to Fig. 3.1, compare the effects of temperature on the activity of immobilised
sucrase with the activity of sucrase free in solution.
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...............................................................................................................................................[4]

© UCLES 2018 9700/21/M/J/18 Paper 2 - 50
7
The researchers also investigated the effects of pH on the activity of the immobilised sucrase
compared with its activity free in solution.
100
key
immobilised
sucrase
80 sucrase free in
solution
percentage of 60
maximum
enzyme
activity
40
20
0
3.0 3.5 4.0 4.5 5.0 5.5 6.0 6.5 7.0 7.5 8.0
pH
Fig. 3.2
(b) Fig. 3.2 shows that immobilised sucrase remains active over a wider range of pH compared
with sucrase free in solution.
Suggest reasons for the higher activity of immobilised sucrase over the range of pH between
5.5 and 8.0.
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...............................................................................................................................................[2]

© UCLES 2018 9700/21/M/J/18 Paper 2 - 51
8
(c) State one variable that the researchers should keep constant in both investigations and
explain your answer in terms of enzyme action.
variable .....................................................................................................................................
...................................................................................................................................................
explanation ...............................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...............................................................................................................................................[2]
(d) There are many advantages of using immobilised enzymes in industry.
Suggest two advantages of using immobilised enzymes in industry other than remaining
active over a greater range of pH.
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...............................................................................................................................................[2]
[Total: 10]

© UCLES 2018 9700/21/M/J/18 Paper 2 - 52
9700/22/M/J/18 14
6 Enzyme inhibitors and monoclonal antibodies can be used in the treatment of disease.
(a) Mevinolin is an enzyme inhibitor that can be prescribed as a drug to reduce the concentration
of cholesterol in blood plasma.
High concentrations of cholesterol in the blood have been linked to an increased risk of
cardiovascular disease.
Mevinolin acts as a competitive inhibitor of the enzyme HMG CoA reductase. This enzyme
catalyses one of the first steps in the synthesis of cholesterol, as shown in Fig. 6.1.
HMG CoA reductase

HMG CoA mevalonic acid
Fig. 6.1
Explain how mevinolin inhibits the enzyme HMG CoA reductase.
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...............................................................................................................................................[3]

© UCLES 2018 9700/22/M/J/18 Paper 2 - 53
9700/23/M/J/18 14
5 The fig tree, Ficus carica, and the papaya tree, Carica papaya, produce a milky-looking fluid
known as latex. The latex is released when plant tissue is wounded and it is thought to act as a
defence against attack by herbivorous insects or parasitic worms.
Latex is a complex mixture of substances and the exact composition of the mixture depends on
the plant species. A group of enzymes that hydrolyse proteins, known as cysteine proteases, are
commonly found in latex.
Ficin, found in F. carica, and papain, found in C. papaya, are both cysteine protease enzymes.
These enzymes have been extracted and purified for use commercially.
(a) An investigation was carried out to compare the effect of temperature on the activity of ficin
and papain.
100
papain
80
ficin
percentage
60
of maximum
activity
40
20
0
0 10 20 30 40 45 50 55 60 70 80
temperature / °C
Fig. 5.1
(i) With reference to Fig. 5.1, describe the differences between the activity of papain
compared to the activity of ficin between 20 °C and 80 °C.
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
.......................................................................................................................................[3]

© UCLES 2018 9700/23/M/J/18 Paper 2 - 54
15
(ii) Ficin and papain have been shown to be effective in the digestion of parasitic nematodes
(roundworms).
With reference to Fig. 5.1, explain which enzyme you would select to use in an oral
medication for the treatment of human intestinal parasitic nematodes.
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
.......................................................................................................................................[1]
(b) One commercial use of the enzyme ficin is the production of Fab fragments (antigen binding
regions) of mouse IgG antibodies for use in immunological studies. The process uses
immobilised ficin to cleave (cut) the antibodies in the hinge region.
Suggest one practical advantage of using immobilised ficin for this process, rather than ficin
free in solution.
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...............................................................................................................................................[1]
(c) Streptococcus pyogenes is a bacterium that can cause a range of diseases in humans.
S. pyogenes synthesises streptopain, a cysteine protease that hydrolyses structural proteins

in human connective tissue.
(i) Streptopain is secreted to the outside of the cell.

State the term given to an enzyme that is produced by a cell and is then secreted to the
outside, where it has its action.
.......................................................................................................................................[1]
(ii) Suggest one example of a structural protein in connective tissue that can be hydrolysed
by streptopain.
.......................................................................................................................................[1]
[Total: 7]

© UCLES 2018 9700/23/M/J/18 Paper 2 - 55
9700/21/O/N/18 4
2 Fig. 2.1 shows the disaccharide lactose, which is found in milk.
CH2OH CH2OH
OH O H O H
H H
OH H O OH H
H H OH
H OH H OH
Fig. 2.1
(a) Name the type of bond that joins the two monosaccharides in lactose.
.............................................................................................................................................. [1]
(b) The enzyme lactase catalyses the breakage of the bond between the two monosaccharides
in lactose.
(i) Name the type of reaction that breaks this bond.
...................................................................................................................................... [1]
(ii) Some people do not produce the enzyme lactase, so cannot digest lactose.
The presence of lactose in the lumen of the intestine reduces the volume of water
absorbed into the blood, resulting in diarrhoea.
Suggest why the presence of lactose in the intestine reduces the volume of water
absorbed.
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...................................................................................................................................... [2]

© UCLES 2018 9700/21/O/N/18 Paper 2 - 56
5
(c) Enzymes, such as lactase, are often immobilised for use in the food industry.
A scientist carried out an investigation to determine the effects of temperature on the activity
of lactase when it was immobilised and when it was free in solution.
The scientist produced alginate beads containing lactase for use in this investigation. The
beads varied in size. The scientist selected small beads for the investigation and put them
into a glass column.
(i) Suggest the advantage of using small beads rather than large beads.
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...................................................................................................................................... [2]

© UCLES 2018 9700/21/O/N/18 Paper 2 - 57
6
(ii) Fig. 2.2 shows the results of the investigation to determine the effects of temperature on
the activity of lactase when it was immobilised, I, and when it was free in solution, F.
100
Key
I immobilised
90 lactase
F lactase free
in solution
80
70
60
percentage
of maximum
activity
50
40
30
20
10
0 F
0 10 20 30 40 50 60 70
temperature / °C
Fig. 2.2

© UCLES 2018 9700/21/O/N/18 Paper 2 - 58
7
With reference to Fig. 2.2, compare the effect of temperature on the activity of immobilised
lactase, I, and lactase free in solution, F.
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...................................................................................................................................... [3]
[Total: 9]

© UCLES 2018 9700/21/O/N/18 Paper 2 - 59
9700/22/O/N/18 5
Cardiac glycosides have an effect on the movement of ions into and out of cardiac muscle cells.
The outcome is an increased ability for the cells to contract.
(c) Investigations into the action of the cardiac glycoside oleandrin, extracted from N. oleander,
have shown that it acts to prevent the correct functioning of Na/K‑ATPase, a membrane
transport protein.
Na/K‑ATPase has a role as an enzyme and as a transport molecule.
• ATPase is an enzyme that catalyses the hydrolysis of ATP to ADP and inorganic
phosphate.
• Energy released from this hydrolysis is used to transport sodium ions (Na+) out of
cardiac muscle cells and potassium ions (K+) into the cells.
(i) Explain what is meant by the hydrolysis of ATP.
...........................................................................................................................................
...........................................................................................................................................
...................................................................................................................................... [2]
(ii) Name the type of transport mechanism involved in the transport of Na+ and K+ across
the cell surface membrane of cardiac muscle cells.
...................................................................................................................................... [1]
(iii) Oleandrin is a non‑competitive reversible inhibitor of ATPase.
Describe the mode of action of oleandrin and explain how this will affect ion movement
through Na/K‑ATPase transport proteins of the cell surface membranes of cardiac
muscle cells.
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...........................................................................................................................................
...................................................................................................................................... [4]

© UCLES 2018 9700/22/O/N/18 Paper 2 - 60
9700/22/F/M/19 4
2 In mammalian red blood cells, carbonic anhydrase has an important role in the transport of carbon
dioxide.
Carbonic anhydrase is an enzyme.
(a) Outline the features of an enzyme.
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
...................................................................................................................................................
............................................................................................................................................. [4]

© UCLES 2019 9700/22/F/M/19 Paper 2 - 61
9700/21/M/J/19 8
3 Neutrase® is an enzyme that is used to hydrolyse proteins in solution. When the enzyme is mixed
with a 2% protein solution the reaction mixture changes from white to colourless.
A student carried out an experiment to find the effect of copper sulfate and potassium sulfate on
the activity of Neutrase®.
The student made four reaction mixtures in test-tubes A to D. Test-tubes A to C contained equal
volumes of protein solution and 0.1 cm3 of solutions of copper sulfate or potassium sulfate.
Test-tube D contained the same volume of protein solution and 0.1 cm3 of water.
0.5 cm3 of a 1% Neutrase® solution was added to test-tube A and immediately placed into a
colorimeter. The colorimeter was used to measure the intensity of light that is absorbed by the
solution (absorbance) over 100 seconds. The procedure was repeated with the other reaction
mixtures, B, C and D.
1.4
A 0.05 mol dm–3 copper sulfate
1.2
B 0.01 mol dm–3 copper sulfate
1.0
0.8
absorbance C 0.01 mol dm–3 potassium sulfate
0.6
D water
0.4
0.2
0.0
0 10 20 30 40 50 60 70 80 90 100
time / s
Fig. 3.1
(a) (i) Suggest and explain why measuring the absorbance of the reaction mixture over 100 s
is a suitable method for determining the activity of Neutrase®.
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© UCLES 2019 9700/21/M/J/19 Paper 2 - 62
9
(ii) With reference to Fig. 3.1:
• describe the effects of copper sulfate solution and potassium sulfate solution on the
activity of Neutrase®
• suggest explanations for the effects that you have described.
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..................................................................................................................................... [5]
(b) Neutrase® can be immobilised in alginate. Immobilised Neutrase® is used in the food industry
to produce foods with high nutritional content.
Explain the advantages of using immobilised enzymes, such as Neutrase®, compared with
using the same enzymes free in solution.
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............................................................................................................................................. [2]
[Total: 9]

© UCLES 2019 9700/21/M/J/19 Paper 2 - 63
14
9700/22/M/J/19
6 Catalase is an enzyme that catalyses the breakdown of hydrogen peroxide, which is a waste
product of cell metabolism.
The reaction catalysed by catalase is shown in Fig. 6.1.
catalase
2H2O2 2H2O + O2
Fig. 6.1
(a) A student carried out two experiments to investigate the progress of the reaction shown in
Fig. 6.1. Potato tissue was used as the source of the enzyme.
Six pieces of potato were cut, each measuring 20 mm × 10 mm × 10 mm.
In the first experiment, hydrogen peroxide solution was added to three of the pieces of potato
tissue and the progress of the reaction was measured.
Fig. 6.2 shows how the first experiment was set up.
syringe containing
H2O2 solution
potato
Fig. 6.2
(i) Suggest how the progress of the reaction could be measured.
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[2]
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© UCLES 2019 9700/22/M/J/19 Paper 2 - 64
15
(ii) In the second experiment, the student cut each of the three remaining pieces of potato to
obtain six pieces, each measuring 10 mm × 10 mm × 10 mm.
Using exactly the same conditions, the student measured the progress of the reaction
and obtained different results to the first experiment.
Explain why the results of the second experiment were different from the results of the
first experiment.
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..................................................................................................................................... [2]
(b) The student then investigated the effect of temperature on the activity of catalase.
On Fig. 6.3, sketch a curve to show how temperature affects the activity of an enzyme such
as catalase.
rate of
reaction
temperature / °C
Fig. 6.3
[1]
[Total: 5]

© UCLES 2019 9700/22/M/J/19 Paper 2 - 65
9700/23/M/J/19 14
(c) Carbonic anhydrase is an enzyme found in red blood cells which has an important role in the
transport of respiratory gases.
Explain why a non-competitive inhibitor of carbonic anhydrase will reduce the supply of
oxygen to actively respiring tissues.
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[Total: 10]

© UCLES 2019 9700/23/M/J/19 Paper 2 - 66

3 Enzymes Paper 2 - N-MQ

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A LEVEL Biology

Classified by Adeel Ahmad

Classified by Adeel Ahmad 3. Enzymes

aspects of protein structure shown

aspects of protein structure not shown

progress of the reaction

Classified by Adeel Ahmad 3. Enzymes

Suggest and explain how this inhibitor would function.

Classified by Adeel Ahmad 3. Enzymes

ara-ATP is a chemical that affects DNA polymerase activity.

In an investigation, the effect of different concentrations of ATP on the rate of DNA

The results of the investigation are shown in Fig. 5.1.

rate of DNA synthesis 4

Classified by Adeel Ahmad

(i) Explain the mode of action of enzymes.

Classified by Adeel Ahmad 3. Enzymes

Fig. 4.2 is a graph showing the results of the investigation.

With reference to Fig. 4.2, describe the results of the investigation.

Classified by Adeel Ahmad

The enzyme catalyses the following reaction:

Quinone is then immediately further oxidized in air to a brown-coloured substance. Catechol

A student investigated the rate of this reaction under different conditions.

Classified by Adeel Ahmad 3. Enzymes

(b) Explain the results shown in Fig. 4.1. For

Suggest an explanation for this observation.

Classified by Adeel Ahmad 3. Enzymes

Classified by Adeel Ahmad 3. Enzymes

Classified by Adeel Ahmad 3. Enzymes

Classified by Adeel Ahmad 3. Enzymes

Classified by Adeel Ahmad 3. Enzymes

Classified by Adeel Ahmad 3. Enzymes

If not treated, this disease is characterised by large fluctuations in the concentration of

(i) Explain how ascorbase acts to inhibit these membrane-bound enzymes.

Classified by Adeel Ahmad 3. Enzymes

Classified by Adeel Ahmad 3. Enzymes

Explain the effects of a non-competitive inhibitor on the rate of enzyme activity.

Classified by Adeel Ahmad

Classified by Adeel Ahmad 3. Enzymes

Explain this result.

Classified by Adeel Ahmad 3. Enzymes

Classified by Adeel Ahmad 3. Enzymes

Classified by Adeel Ahmad 3. Enzymes

Classified by Adeel Ahmad 3. Enzymes

(d) Angiotensin is a polypeptide produced in the body to raise blood pressure.

10 amino acid polypeptide: Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu

This drug is a competitive inhibitor of ACE.

Explain how this drug acts as a competitive inhibitor.

Classified by Adeel Ahmad 3. Enzymes

Classified by Adeel Ahmad 3. Enzymes

Classified by Adeel Ahmad 3. Enzymes

The results are shown in Fig. 3.1.

Classified by Adeel Ahmad 3. Enzymes

(d) Metal ions can act as a non-competitive inhibitor of catalase.

Explain how copper ions can act as a non-competitive inhibitor.

Classified by Adeel Ahmad 3. Enzymes

The results are shown in Fig. 4.1.

(ii) Explain why the activity of phosphatase at pH 1 is very low.

Classified by Adeel Ahmad 3. Enzymes

(i) State one way of immobilising an enzyme.

Classified by Adeel Ahmad 3. Enzymes

State the correct term to match each of the statements A to E.

D The term for enzymes that function outside cells.

Classified by Adeel Ahmad 3. Enzymes