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Luxor World School BIOLOGY – AS LEVEL

STRUCTURED QUESTIONS 3 ENZYMES

1. The enzyme glucose 6-phosphate dehydrogenase (G6PD) is composed of two identical polypeptide chains.

(a) Students investigated the activity of two forms of G6PD, J and K, at different concentrations of substrate. K
is a form of the enzyme that results from a mutation that changes one amino acid in the polypeptide.

The results are shown in Fig. 3.1.

(i) Use Fig. 3.1 to complete Table 3.1 by stating:

• the Vmax and the Km for enzymes J and K
• the units for Vmax and Km

(ii) With reference to Fig. 3.1 and Table 3.1, describe the effect of the mutation on the activity of G6PD
and suggest an explanation for this effect.
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(b) In certain conditions, G6PD may also exist as four identical polypeptide chains rather than two
identical polypeptide chains. Explain why both of these types of G6PD have all four levels of protein
structure.
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2. Lysosomes are cell structures that contain enzymes known as acid hydrolases.

Fig. 6.1 shows some processes that occur in animal cells.

(a) Name the cell structures labelled A and E.

A ...............................................................................................................................................
E ............................................................................................................................................... [2]

(b) State the function of the structures labelled

F. ................................................................................................................................................... ..........................
................................................................................................................... [1]

(c)Name the process by which bacteria are taken into the cell at
C. ............................................................................................................................................. [1]

(d) With reference to the processes occurring at B and at D in Fig. 6.1, outline the role of acid hydrolases in
lysosomes.
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(e) Carrier proteins in the membranes of lysosomes maintain a lower pH than the surrounding cytoplasm by
moving hydrogen ions. Suggest how the carrier proteins maintain the lower pH within the lysosomes.

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3. Fig. 5.1 is a transmission electron micrograph showing parts of two plant cells. The function of the middle
lamella is cell-to-cell adhesion. The middle lamella is composed of a polysaccharide known as pectin.

Pectin interacts with the polysaccharides cellulose and hemicellulose in the cell walls of the plant cells so that
the cell walls are held close together, as shown in Fig. 5.1

(a) Cell structure X in Fig. 5.1 is a cytoplasmic channel with strands of cytoplasm passing through the cell walls
of the two cells. Name cell structure X and state one function of this cell structure.
Name .........................................................................................................................................
Function ..................................................................................................................................... ......................
....................................................................................................................... [2]

(b) Researchers have discovered that pectin is synthesised within the Golgi body. Golgi vesicles containing
pectin are moved to the cell surface membrane for release.
(i) Suggest why researchers would not have investigated ribosomes as being the possible location for the
synthesis of pectin.
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(ii) Name the mechanism that is used to transport pectin out of the
cell. ..................................................................................................................................... [1]

Juices that are extracted commercially from fruits can be made less cloudy by the breakdown of the cell wall
using the enzymes cellulase, pectinase and xylanase:

• cellulase hydrolyses cellulose

• pectinase hydrolyses pectin
• xylanase hydrolyses hemicellulose.

(b) Fig. 5.2 is a graph showing the effect of cellulose concentration on the activity of cellulase, which is used in
making fruit juice less cloudy.
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Describe and explain the curve shown in Fig.

5.2. ................................................................................................................................................... .................
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(c) Ultrasound is one possible method that can be used to destroy microorganisms that contaminate fruit
juices. Ultrasound is the term given to sound waves that are out of the range of human hearing.

An investigation was carried out into the effect of ultrasound on the activity of cellulase, pectinase and
xylanase used in fruit juice manufacture. For each enzyme, the effect of ultrasound was compared with no
ultrasound on the:

• maximum rate of reaction (Vmax)

• Michaelis-Menten constant (Km)
• catalytic efficiency (Vmax /Km)

Table 5.1 summarises the results. A higher Vmax /Km indicates a higher catalytic efficiency.

(i) In terms of changes in the interaction between enzyme and substrate when ultrasound is
used, suggest explanations for the lower Km for pectinase and the higher Vmax for xylanase,
as shown in Table 5.1.

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(ii) Explain whether the data shown in Table 5.1 supports the recommendation that ultrasound
can be used in the manufacture of fruit
juices. ........................................................................................................................................... .
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[Total: 11]
4. HIV protease is an enzyme composed of two identical polypeptide chains. Each polypeptide chain is 99 amino
acids long. During translation, the amino acids are joined by peptide bonds to form the polypeptide chain.
(a) Describe how a polypeptide of HIV protease is produced by the process of
translation. ................................................................................................................................................... ...........
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(b) The synthesised polypeptide has a primary protein structure and can form a tertiary protein
structure after translation. There are more bond types in the tertiary structure.
Compare the peptide bond formed during translation with the types of bond made during
tertiary structure formation.
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(d) Some polypeptides are translated as part of one long polyprotein chain.
After translation, enzymes cut the polyprotein into separate functioning proteins.

HIV protease cuts a polyprotein that has been produced within the host cells of actively replicating HIV.
The separate proteins are required in the replication of the virus.

Fig. 3.1 shows how the two polypeptide chains of HIV protease form an enzyme with an active site
enclosed by flaps, forming the flap region.

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(i) The flap region of HIV protease is flexible. With reference to Fig. 3.1, suggest and explain how the
mechanism of action of HIV protease can be described as an induced
fit. ........................................................................................................................................... .............
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(ii) Indinavir is one of the therapeutic drugs used in HIV anti-retroviral therapy (ART). It is similar to
the polyprotein substrate of HIV protease. Suggest and explain how indinavir acts as a therapeutic
drug.
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[Total: 12]
5. A tyrosine kinase receptor (TKR) is a protein complex found in the cell surface membrane of mammalian cells.
TKR has two components involved in the process of cell signalling:

• a receptor for the signalling molecule (ligand)

• an enzyme that catalyses the transfer of a phosphate group from ATP to an intracellular protein.

Fig. 3.1 is a diagram to show how TKR is involved in cell signaling.

(a) Most enzymes are specific to one reaction. With reference to Fig. 3.1, explain how the structure of an
enzyme provides its
specificity. ................................................................................................................................................... ......

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The drug GNF-5 is used in the treatment of some cancers. GNF-5 affects the activity of TKR by binding to
the enzyme component of the complex.

Researchers investigated the effect of GNF-5 on the activity of TKR using different concentrations of ATP
solution.

In an experiment the activity of TKR was measured with no GNF-5 and with GNF-5. The results are shown
in Fig. 3.2.

(b) The researchers concluded that GNF-5 acts as an inhibitor of the enzyme component of TKR and that it is a
competitive inhibitor. Use Fig. 3.2 to provide evidence for these
conclusions. ................................................................................................................................................... ...
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(c) A mutation of the gene coding for TKR results in changes to the enzyme component of TKR. This altered
form of TKR is known as T315L.

The effect of GNF-5 on the activity of T315L was also investigated.

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The results of this investigation are shown in Fig. 3.3.

Use Fig. 3.2 and Fig. 3.3 to:

(i) State how the activity of T315L differs from TKR when no GNF-5 was
present. ........................................................................................................................................... ..........
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(ii) State how the effect of GNF-5 on T315L differs from the effect of GNF-5 on
TKR. ........................................................................................................................................... ................
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[Total: 8]
6. The enzyme carbonic anhydrase has been found in a wide range of organisms and acts as a catalyst in many
tissues.

Studies have shown that there are differences in the protein structure of the enzyme and differences in the
number and organisation of introns and exons of the gene coding for the enzyme.

All carbonic anhydrase enzymes catalyse the same reversible reaction, shown in Fig. 4.1.

(a) With reference to Fig. 4.1, name X and Y.

X ...............................................................................................................................................
Y ............................................................................................................................................... [2]

(b) Carbonic anhydrase enzymes can have different primary structures. Suggest how all carbonic anhydrase
enzymes can catalyse the same reaction, even though they have different primary
structures. ................................................................................................................................................... .....

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(c) Genes coding for proteins in eukaryotes consist of introns and exons. Outline the similarities and
differences between the introns and the exons of genes coding for proteins such as carbonic
anhydrase. ................................................................................................................................................... ...........
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All mammals have the same type of carbonic anhydrase, known as α-carbonic anhydrase. Many different
forms, or isoforms, of α-carbonic anhydrase have been identified in mammals. There are 15 isoforms of α-
carbonic anhydrase (CA) in humans. Cells of different tissues have one or more isoforms. Within cells the
isoforms may be in different locations. (d) Red blood cells contain two isoforms, CA1 and CA2. Suggest the
location of CA1 and CA2 in red blood cells and give a reason for your
answer. ................................................................................................................................................... ................
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(e) Isoform CA6 forms part of human breast milk. Mammary gland cells package CA6 in Golgi vesicles for
release from the cells. Name the transport mechanism associated with CA6
secretion. ............................................................................................................................................. [1]

(f) Human CA isoforms in some epithelial cells in the eye have a role in the formation of the clear fluid of the
eye known as aqueous humour. Overactivity of the enzyme may lead to a harmful increase of pressure
within the eye and cause a condition known as glaucoma.

Acetazolamide is a therapeutic drug that can be used in the treatment of glaucoma. It acts as a reversible
non-competitive inhibitor.

Describe the mechanism of action of acetazolamide as a reversible non-competitive inhibitor of carbonic

anhydrase.
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[Total: 12]
7. (a) The induced-fit hypothesis and the lock-and-key hypothesis are used to describe the mode of action of
enzymes. Explain the induced-fit
hypothesis. ................................................................................................................................................... ...........
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(c) Radish plants contain the enzyme peroxidase that catalyses the breakdown of hydrogen peroxide.

Students investigated the effect of increasing the concentration of hydrogen peroxide on the activity of
peroxidase extracted from radish.
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The results of their investigation are shown in Fig. 4.1.

(i) Explain the effect of increasing the concentration of hydrogen peroxide on the initial rate of
reaction as shown in Fig. 4.1.
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(ii) The students determined the Km for radish peroxidase as 0.10mmoldm–3. With reference to Fig.
4.1, describe how they determined the
Km. ........................................................................................................................................... ...........
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(d) A further investigation found that the Km for carbonic anhydrase is 12mmoldm–3. Describe the role of
carbonic anhydrase in the transport of carbon
dioxide. ................................................................................................................................................... ..........
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[Total: 11]

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