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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
Multiple Choice Questions
1. Enzyme molecules with high optimum temperature will have
A less associated non-protein groups.
B less hydrophobic amino acid residues.
C more cysteine residues in their polypeptide chains.
D more peptide bonds than other enzyme molecules.
2. In an investigation to determine the effect of temperature on
the activity of an enzyme, the time taken for all the substrates to
disappear from a standard solution was recorded.
Which graph shows the result of this investigation?
A
B
C
D
3. The diagram below shows a simple metabolic pathway.
Which response shows feedback inhibition?
Metabolite Binding site of metabolite
A F Active site of enzyme 1
B F Allosteric site of enzyme 1
C I Active site of enzyme 1
D I Allosteric site of enzyme 1
F G H I
Enzyme 1 Enzyme 2 Enzyme 3
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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
4. The graph shows the results of an experiment in which samples
containing the same
concentration of enzyme and substrate were kept at different
temperatures for periods of
one, two and five hours. The quantities of product formed were
then determined.
Which of the following options best explains why the optimum
temperature is lower if the
quantity of product formed is measured after five hours rather
than one hour?
A Tertiary bonds are not broken at higher temperatures.
B The enzyme has a range of optimum temperatures.
C A longer time at high temperature denatures enzyme.
D The optimum temperature for the enzymes is 45C.
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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
5. The diagram shows an enzyme molecule with its normal
substrate and products. P and
Q are other molecules that can bind to the enzyme.
The graph shows the effect of P and Q on the rate of reaction of
the enzyme at different
substrate concentrations.
Which statement correctly describes the activity of the
enzyme?
A P is a competitive inhibitor which binds to the active site,
resulting in curve R.
B P is a non-competitive inhibitor which distorts the shape of
the enzyme, resulting in
curve S.
C Q is a competitive inhibitor which distorts the shape of the
enzyme, resulting in
curve R.
D Q is a non-competitive inhibitor which binds to the active
site, resulting in curve S.
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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
6. The monomers of both starch and cellulose are glucose
molecules. Which of the
following best explains why amylase can only break down starch
but not cellulose?
A The large number of cross-linkages between adjacent cellulose
molecules that
prevents amylase from breaking down cellulose.
B Amylase can only recognize -glycosidic linkages, which are
present in starch but
not cellulose.
C The glycosidic bonds between the monomers in cellulose are
stronger than in
starch.
D Cellulose is too large to be broken down by amylase.
7. Catalase is an enzyme that breaks down hydrogen peroxide. A
scientist discovered a
new substance X, which will decrease the rate of enzymatic
reaction of catalase when
added into the system. The addition of substrate, however, will
increase the rate of
reaction again.
From the information given above, what can you conclude about
substance X?
A It has similar molecular configuration to hydrogen
peroxide.
B It binds to a site away from the active site of the catalase
enzyme.
C It has the same configuration as the active site of
catalase.
D It increases the pH of the system.
8. The four unknown substances shown below form part of an
enzyme-catalysed pathway.
The addition of substance V results in no change in the
concentration of W, and an
accumulation of X, and a near absence of both Y and Z. Further
addition of Y results in
the formation of Z.
What does this information indicate about substance V?
A It is an inhibitor of enzyme 1
B It is an inhibitor of enzyme 2
C It is an inhibitor of enzyme 3
D It catalyses the formation of X
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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
9. Which of the following statements about the function of
enzymes is correct?
A Enzymes can speed up reaction but they cannot change the net
energy output as
the activation energy cannot be changed.
B Enzymes can speed up the reaction by increasing the activation
energy of a
reaction.
C Enzymes lower the activation energy of a reaction and change
the net energy
output.
D Enzymes lower the activation energy of a reaction but do not
change the net energy
output..
10. In an experiment using starch and amylase, the
concentrations of starch and maltose
present in the reacting mixture are measured every minute for 20
minutes. 1%
hydrochloric acid is added after 10 minutes and the mixture is
heated to 60C at 14
minutes.
Which graph represents the results of this experiment? C
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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
11. The diagram shows a metabolic pathway controlled by end
product inhibition. As the
concentration of the end product increases above the set level,
an enzyme in the
pathway leading to the end product is inhibited.
An increase in the concentration of end product 6 does not lead
to a decrease in the
synthesis of end product 9.
Which enzyme is inhibited by end product 6?
A Metabolite 1 Metabolite 2
B Metabolite 2 Metabolite 3
C Metabolite 3 Metabolite 4
D Metabolite 3 Metabolite 7
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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
12. Lactose is a disaccharide present in milk. The enzyme
-galactosidase catalyses the
breakdown of lactose to glucose and galactose.
10 cm3 of a 1% -galactosidase solution was added to 10 cm3 of
milk. The graph shows
the total amount of glucose produced over the next ten
minutes.
Then, 10 cm3 of a 2% galactosidase solution was added to 10 cm3
of milk.
Which graph shows the expected results?
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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
13. An enzyme is a globular protein held together by several
different types of chemical
bond, giving the enzyme primary, secondary and tertiary levels
of structure. Which
correctly summarises the types of bond involved in each level of
structure?
Disulfide Bonds Hydrogen Bonds Ionic Bonds Peptide Bonds
A Tertiary Secondary, Tertiary Tertiary Primary
B Primary, Tertiary Primary Secondary, Tertiary Secondary
C Secondary Secondary Tertiary Primary
D Primary Tertiary Secondary Tertiary
14. Indinavir is a commercial HIV-1 protease inhibitor
administered by doctors to treat AIDS
patients. It is supposed to act as a competitive inhibitor.
Which of the following shows the correct combination of the Km
value and maximum
velocity (Vmax) of HIV-1 protease when Indinavir is added
together with its substrate?
Km Maximum velocity (Vmax)
A Remains the same Increases
B Remains the same Decreases
C Increases Remains the same
D Decreases Decreases
15. The figure shows a series of reactions in a metabolic
pathway.
Enzyme 3 catalyses the splitting of C into D and J. Assuming
that product E is an
allosteric inhibitor of 3, which of the following would likely
happen if E were not consumed
in a subsequent reaction?
A The rate of production of D would increase.
B The rate of production of E would remain the same.
C The rate of production of L would remain the same.
D The rate of production of all products D, E, J and K would
decrease.
A 1
B 2
C 3
D 4
J 5
K 6
L
E
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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
16. Substance X (a mineral ion) is actively transported into
cells. Equal-sized samples of cells were placed in media containing
different concentrations of X for an hour. The intracellular
concentration of X was then measured. All other metabolic
conditions were maintained at the optimum level. The graph below
shows the results.
From the information given above, which one of the following
would account for the level
region of the graph labelled Y?
A A respiratory inhibitor had been introduced.
B All the active transport carriers had been operating at their
maximum rate.
C The active transport carriers had been inactivated by a
non-competitive inhibitor.
D As the internal concentration of X rose, more of the substance
X was metabolised.
17. In the following branched metabolic pathway, a dotted arrow
with a minus sign symbolizes inhibition of a metabolic step by an
end product:
Which reaction would prevail if both Q and S were present in the
cell in high
concentrations?
A L M
B M O
C L N
D R S
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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
18. When investigating enzyme/substrate interactions, which one
of the following would be
expected to show a linear relationship under constant
conditions?
A Amount of product against time, with the amount of substrate
limited.
B Rate of reaction against substrate concentration, with the
amount of enzyme
limited.
C Rate of reaction against enzyme concentration, in the presence
of excess
substrate.
D Rate of reaction against enzyme concentration, with the amount
of substrate
limited.
19. In the production of isoleucine from threonine in bacteria
(Biochemical Pathway 1 [BP
1]), the end product acts as an inhibitor of the first enzyme in
the pathway. In the
production of arginine (Biochemical Pathway 2[BP 2]), the end
product has no influence
on other enzymes in the pathway. It is reasonable to conclude
that in
A BP 1, if the production of enzyme 3 stops there would be
continuous production of
isoleucine.
B BP 2, if the production of enzyme 3 stops there would be
continuous production of
arginine.
C BP 1, providing all enzymes are present, the production of
isoleucine would be
continuous if there was a continuous supply of threonine.
D BP 2, providing all enzymes are present, the production of
arginine would be
continuous if there was a continuous supply of substrate.
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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
20. The graph shows the amount of product formed by a standard
concentration of enzyme
and a standard concentration of substrate at a temperature of 15
C.
Which graph shows the effect on the activity of the enzyme of
increasing the temperature
to 20 C?
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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
Structured Questions
1 Lysozyme is an enzyme found in many places within the human
body. It consists of a single
polypeptide folded into a complex shape. Fig. 1.1 shows a ribbon
model of lysozyme.
Fig. 1.1
(a) With reference to Fig. 1.1, describe region X. [2]
Lysozyme is one of the many hydrolytic enzymes found within a
lysosome. The lysosome enzymes
are only active over a narrow range of pH, with an optimum of pH
5. The pH of the cytoplasm is 7.2.
The internal pH of lysosomes is maintained by actively
concentrating H+ ions in the lysosome using
proton pumps.
(b) Describe how H+ ions could be moved across the lysosome
membrane. [3]
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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
(c) Explain why enzymes from a leaky damaged lysosome may not
destroy the cell contents. [2]
(d) Suggest why the lysosome membrane is not destroyed by the
enzymes in the lysosome. [2]
[Total: 9 marks]
2 Detergent is a mixture that is used for cleaning purposes.
Some of the components present in the
detergent include enzymes, preservatives, pH buffers, water
softener and oxidizers.
(a) Suggest one enzyme that may be found in detergent and state
its possible function. [1]
(b) (i) Suggest a reason why pH buffers are found in detergent.
[1]
(ii) Explain what will happen if the pH deviates from the
optimum pH for enzyme activity.[3]
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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
(c) Explain why laundry should not be washed with ice-cold
water. [3]
(d) Explain how the structure of the enzymes in the detergent is
stabilized [2].
[Total: 10 marks]
3 Fig. 4.1 below shows a model of the enzyme chymotrypsin.
Chymotrypsin catalyses the hydrolysis
of peptide bonds of proteins. The active site of chymotrypsin is
located in a slight depression on
one side of the molecule. Three amino acids form the active
site. These three amino acids are
some distance apart on the polypeptide chain but close together
in the active site.
Fig. 4.1
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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
(a) Describe how amino acid residues at different positions in
the protein may be brought together
in the active site when the enzyme is synthesised. [2]
(b) Explain how a substrate may be attached to the enzyme.
[3]
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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
Fig. 4.2 shows the effects of increasing substrate concentration
on the rate of an enzyme-catalysed
reaction at a temperature of 35C and a constant pH.
Fig. 4.2
(c) With reference to Fig. 4.2, explain why an increase in
substrate concentration at low substrate
concentrations increases the rate of reaction but an increase at
high substrate concentrations
does not have the same effect. [4]
[Total: 9 marks]
Graph 3
Graph 2 Graph 1
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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
4 Enzymatic browning is one of the most important colour
reactions that affect fruits. Cut apples
turned brown after exposure to air within minutes. This browning
reaction is catalysed by the
enzyme polyphenol oxidase (PPO), which is abundant in the flesh
of the apples. PPO converts iron-
containing phenol compounds in the presence of oxygen to melanin
in a series of polymerization
reactions. Fig. 5.1 shows the structure of the PPO enzyme.
Fig. 5.1
(a) With reference to Fig. 5.1, describe the structure of the
PPO enzyme. [3]
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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
(b) Suggest the role of PPO in melanin synthesis in apples.
[2]
Fig. 5.2 shows the results of tests to determine the optimum
temperature for the activity of PPO.
Percentage of
phenols
converted into
melanin in 10
minutes / %
Fig. 5.2
(c) With reference to Fig. 5.2,
(i) state the optimum pH and temperature for the enzyme PPO.
[1]
pH: Temperature:
(ii) account for the curve at pH 8. [4]
[Total: 10 marks]
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Anglo-Chinese Junior College Revision Package H2 & H1
Biology Enzymes
Essays
1 (a) Describe the roles of enzymes in DNA replication (KIV for
DNA & Genomics) [8] (b) Explain the effect of a competitive
inhibitor on the rate of enzyme activity. [4] 2 (a) Describe the
effects of pH and temperature on enzyme-catalyzed reactions. [8]
(b) Distinguish between competitive and non-competitive inhibition
of enzyme action. [7] (c) Explain the effect of enzyme and
substrate concentration on the rate of enzyme catalyzed
reactions. [5]