New Hodder Cambridge A Level Biology 2E 2020 - SAMPLE Chapter

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International AS & A Level
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Second edition
CJ Clegg
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Cambridge
International
AS & A Level
Biology
Second edition
C J Clegg
482876_Cam_AS_A_Level_Biology_001-013.indd 1 29/07/19 9:46 PM

Contents
Contents
Introduction
AS LEVEL
1 Cell structure
1.1 The microscope in cell studies
1.2 Cells as the basic units of living organisms
2 Biological molecules
2.1 Testing for biological molecules
2.2 Carbohydrates and lipids
2.3 Proteins
2.4 Water
3 Enzymes
3.1 Mode of action of enzymes
3.2 Factors that affect enzyme action
4 Cell membranes and transport

4.1 Fluid mosaic membranes
4.2 Movement of substances into and out of cells
5 The mitotic cell cycle

5.1 Replication and division of nuclei and cells
5.2 Chromosome behaviour in mitosis
6 Nucleic acids and protein synthesis

6.1 Structure of nucleic acids and replication of DNA
6.2 Protein synthesis
7 Transport in plants
7.1 Structure of transport tissues
7.2 Transport mechanisms
8 Transport in mammals
8.1 The circulatory system
8.2 Transport of oxygen and carbon dioxide
8.3 The heart

9 Gas exchange and smoking
9.1 The gas exchange system
10 Infectious disease
10.1 Infectious diseases
10.2 Antibiotics
11 Immunity
11.1 The immune system
11.2 Antibodies and vaccination
A LEVEL
12 Energy and respiration

12.1 Energy
12.2 Respiration
13 Photosynthesis
13.1 Photosynthesis as an energy transfer process
13.2 Investigation of limiting factors
14 Homeostasis
14.1 Homeostasis in mammals
14.2 Homeostasis in plants
15 Control and co-ordination

15.1 Control and co-ordination in mammals
15.2 Control and co-ordination in plants
16 Inherited change
16.1 Passage of information from parent to offspring
16.2 The roles of genes in determining the phenotype
16.3 Gene control
17 Selection and evolution

17.1 Variation
17.2 Natural and artificial selection
17.3 Evolution
18 Classification, biodiversity and conservation

18.1 Classification
18.2 Biodiversity
18.3 Conservation

19 Genetic technology
Contents
19.1 Principles of genetic technology

19.2 Genetic technology applied to medicine
19.3 Genetically modified organisms in agriculture
Answers
Index
Acknowledgements
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AS Level
3 Enzymes

Enzymes are essential for
life to exist. Their mode of
Learning Outcomes
action and the factors that By the end of this topic, you should be able to:
affect their activity are 3.1.1 state that enzymes are globular proteins that catalyse reactions
explored in this topic. Prior inside cells (intracellular enzymes) or are secreted to catalyse
knowledge for this topic
is an understanding that
reactions outside cells (extracellular enzymes)
an enzyme is a biological 3.1.2 explain the mode of action of enzymes in terms of an active site,
catalyst that increases enzyme-substrate complex, lowering of activation energy and
the rate of a reaction and enzyme specificity, including the lock-and-key hypothesis and the
remains unchanged when
induced-fit hypothesis
the reaction is complete.
3.1.3 investigate the progress of enzyme-catalysed reactions by
There are many
opportunities in this measuring rates of formation of products using catalase and rates
topic for students to gain of disappearance of substrate using amylase
experience of carrying out
practical investigations and
analysing and interpreting
their results.
There are many different enzymes, each one specific to a particular reaction.
This specificity is the key to understanding the efficient functioning of cells
and living organisms.
Introducing enzymes and their role in metabolism

Enzymes are globular proteins that catalyse the many thousands of metabolic
reactions taking place within cells and organisms. Metabolism is the name we
give to these chemical reactions of life. The molecules involved are collectively
called metabolites. Many of these metabolites are made in organisms. Other
metabolites have been imported from the environment, such as from food
substances taken in, water and the gases carbon dioxide and oxygen.
Metabolism actually consists of chains (linear sequences) and cycles of enzyme-
catalysed reactions, such as we see in respiration, photosynthesis, protein
synthesis and many other pathways. These reactions may be classified as one
of just two types, according to whether they involve the build-up or breakdown
of organic molecules:
» In anabolic reactions, larger molecules are built up from smaller molecules.
Examples of anabolism are the synthesis of proteins from amino acids and
the synthesis of polysaccharides from simple sugars.
» In catabolic reactions, larger molecules are broken down. Examples of
catabolism are the digestion of complex foods and the breakdown of sugar in
respiration (Figure 3.1).
5

synthesis of complex
Enzymes as globular proteins
3
molecules used in growth
and development and in In Topic 2 we saw that the tertiary structure of globular proteins is typically
metabolic processes,
e.g. proteins, spherical. In these molecules their linear chain of amino acids (primary
polysaccharides, structure) is precisely folded and held in a globular, three-dimensional shape
lipids, hormones, growth
factors, haemoglobin, containing a-helices and b-sheets. Also, the R-groups of the amino acids
chlorophyll present on the exterior of the molecule are hydrophilic groups, making the
anabolism: protein water soluble. Remember, this structure contrasts with that of the
energy-requiring fibrous proteins, such as collagen.
reactions, i.e.
endergonic
3 Enzymes
reactions Enzymes as biological catalysts

sugars, A catalyst is a molecule that speeds up a chemical reaction but remains
amino acids,
fatty acids, unchanged at the end of the reaction. Most chemical reactions do not occur
nutrients
i.e. smaller spontaneously. In a laboratory or in an industrial process, chemical reactions
organic
molecules may be made to occur by applying high temperatures, high pressures, extremes
of pH and by keeping a high concentration of the reacting molecules. If
catabolism
energy-releasing these drastic conditions were not applied, very little of the chemical product
reactions, would be formed. In contrast, in cells and organisms, many of the chemical
i.e. exergonic
reactions reactions of metabolism occur at exactly the same moment, at extremely
release of simple
low concentrations, at normal temperatures and under the very mild, almost
substances, neutral, aqueous conditions we find in cells.
e.g. small inorganic
molecules, CO2, H2O, How is this brought about?
mineral ions
▲ Figure 3.1 Metabolism: For a reaction between two molecules to occur, there must be a successful
an overview collision between them. The molecules must collide with each other in the right
way and at the right speed (Figure 3.2). If the angle of collision is not correct,
the molecules bounce apart. Alternatively, if the speed of the collision is wrong
or the impact is too gentle, for example, then there will be insufficient energy
for the rearrangement of electrons. Only if the molecules are lined up and
collide with the correct energies does a reaction occur.
The ‘right’ conditions happen so rarely that the reaction does not happen to a
significant extent normally. If we introduce extreme conditions, such as those
listed above, we can cause the reaction to happen. On the other hand, if we
introduce an enzyme for this particular reaction, then the reaction occurs at
great speed. Enzymes are amazing molecules in this respect.
Where do enzymes operate?

Some enzymes are exported from cells, such as the digestive enzymes. Enzymes
like these, that are parcelled up, secreted and work externally are called
extracellular enzymes. However, many enzymes remain within the cells and
work there. These are intracellular enzymes. They are found inside organelles,
in the membranes of organelles, in the fluid medium around the organelles (the
cytosol) and in the cell surface membrane.
Enzymes control metabolism

There is a huge array of enzymes that facilitate the chemical reactions of
the metabolism. Since these reactions can only take place in the presence of
specific enzymes, we know that if an enzyme is not present then the reaction it
catalyses cannot occur.
Many enzymes are always present in cells and organisms but some enzymes are
produced only under particular conditions or at certain stages. By making some
enzymes and not others, cells can control what chemical reactions happen
in the cytoplasm. Sometimes it is the presence of the substrate molecule
6

that triggers the synthesis of the enzyme. In Chapter 4 we see how protein
3
synthesis (and therefore enzyme production) is directly controlled by the cell
nucleus.
How enzymes work

So, enzymes are biological catalysts made of protein. They speed up the rate of
a chemical reaction. The general properties of catalysts are:
» they are effective in small amounts
» they remain unchanged at the end of the reaction.

The presence of enzymes enables reactions to occur at incredible speeds, in an
orderly manner, yielding products that the organism requires, when they are
needed. Sometimes reactions happen even though the reacting molecules are
present in very low concentrations.
CH2OH
1 The reaction: hydrolysis of sucrose
oxygen bridge from water
to form glucose and fructose O
CH2OH
1 HO
OH CH2OH O CH2OH
O O O
HO +
2
OH OH OH
HO HOH 2C HOH 2C
HO OH
H O
water H OH HO OH
sucrose glucose fructose
sucrose sucrose sucrose

2 Random collision possibilities:
when sucrose and water collide at
the wrong angle
water
water water
sucrose sucrose sucrose

when sucrose and water collide at
the wrong speed
These events are what happens at

most random collisions
water water
water
For the reaction to occur, sucrose sucrose glucose

and water must collide in
just the right way – glucose and
fructose are formed
Under normal conditions this

water fructose
happens so infrequently that
it is an insignificant event
3 In the presence of one molecule of the enzyme sucrase (invertase),

approximately 3.0 × 104 molecules of sucrose are hydrolysed each minute!
▲ Figure 3.2 Can a reaction occur without an enzyme?

Enzymes lower the activation energy
3 As molecules react, they become unstable, high-energy intermediates, but

they are in this state only momentarily. We say they are in a transition state
because the products are formed immediately. The products have a lower
energy level than the substrate molecules. Energy is needed to raise molecules
to a transition state and the minimum amount of energy needed to do this is
called the activation energy (Figure 3.3). It is an energy barrier that has to
be overcome before the reaction can happen. Enzymes work by lowering the
amount of energy required to activate the reacting molecules.
3 Enzymes
A model of what is going on is the boulder (the substrate) perched on a slope,

prevented from rolling down by a small hump (the activation energy) in front
of it. The boulder can be pushed over the hump. Alternatively, the hump can be
dug away (the activation energy can be lowered), allowing the boulder to roll
and shatter at a lower level (into the products).
‘boulder on hillside’ model of activation energy without a catalyst, this

amount of energy needs
triggering the fall,
to be put in to start the effect of catalyst
either by pushing
reaction
or by removing
the hump (the
enzyme way)
activation energy
energy
free energy change
products
(at lower
energy level)
reactant products
▲ Figure 3.3 Activation energy
The enzyme has an active site

In a reaction catalysed by an enzyme, the starting substance is called the
substrate. It is converted to the product. The way an enzyme works is for the
substrate molecule to become attached to (we say ‘bind to’) the enzyme at
a specially formed pocket in the enzyme – very briefly. This binding point is
called the active site. The active site takes up a relatively small part of the
total volume of the enzyme.
So, an enzyme (E) works by binding to its substrate (S) molecule at a specially
formed pocket in the enzyme. This concept is referred to the ‘lock and key’
hypothesis of enzyme action. As the enzyme and substrate form a complex
(E–S), the substrate is raised in energy to a transition state and then breaks
down into products (Pr) plus unchanged enzyme (Figure 3.4).
E + S → E – S → Pr + E

The sequence of steps to an enzyme-catalysed reaction:
3
enzyme + substrate E–S complex product + enzyme available for reuse
(substrate raised to
transition state)
substrate molecule –
E + S E–S Pr + E the key
active site (here

the substrate
molecule is held

and reaction occurs) – enzyme–substrate
the lock enzyme
complex
(large protein
molecule)
substrate
product molecule now at
molecules transition state
▲ Figure 3.4 The lock and key hypothesis of enzyme action
Enzymes are typically large globular protein molecules. Most substrate

molecules are quite small molecules by comparison. Even when the
substrate molecules are very large, such as certain macromolecules like the
polysaccharides, only one bond in the substrate is in contact with the active
site of the enzyme.
Enzymes are highly specific

Enzymes are highly specific in their action. They catalyse only one type of
reaction or only a very small group of very similar reactions.
This means that an enzyme ‘recognises’ a very small group of substrate
molecules or even only a single type of molecule. This is because the active
site where the substrate molecule binds has a precise shape and distinctive
chemical properties (meaning the presence of particular chemical groups and
bonds). Only particular substrate molecules can fit to a particular active site.
All other substrate molecules are unable to fit and so cannot bind.
Question 1 Explain why the shape of globular proteins that are enzymes is important in
enzyme action.
Catalysis by ‘induced fit’

We have seen that enzymes are highly specific in their action. This makes them
different from most inorganic catalysts. Enzymes are specific because of the
way they bind with their substrate at a pocket or crevice in the protein. The
‘lock and key’ hypothesis, however, does not fully account for the combined
events of ‘binding’ and simultaneous chemical change observed in most
enzyme-catalysed reactions.
At the active site, the arrangement of certain amino acid molecules in the
enzyme exactly matches certain groupings on the substrate molecule, enabling
the enzyme–substrate complex to form. As the complex is formed, an essential,
critical change of shape is caused in the enzyme molecule. It is this change of
shape that is important in momentarily raising the substrate molecule to the
transitional state. It is then able to react (Figures 3.5 and 3.6).

With a transitional state achieved, other amino acid molecules of the active site
3
bring about the breaking of particular bonds in the substrate molecule, at the
point where it is temporarily held by the enzyme. It is because different enzymes
have different arrangements of amino acids in their active sites that each enzyme
catalyses either a single chemical reaction or a group of closely related reactions.
polypeptide of 49 amino acid residues,
making up a simple enzyme
substrate
3 Enzymes
active site (pocket/crevice

in the protein molecule)
The amino acids in a

protein have different
roles.
The substrate molecule
combines (temporarily)
with the enzyme by
inducing a change in
shape of the enzyme
molecule.
the ‘induced fit’ process plays a
part in bringing about the chemical
changes, which are the enzyme-
catalysed reaction
some amino acid residues
match certain groupings on the
substrate molecule, enabling the
enzyme–substrate complex to form,
3 e.g. residues 3–4–5 and 24–25–26
4
5 other amino acid
residues are ‘reactive’,
substrate
i.e. catalytic residues
that induce the
41
breaking of bonds,
20 and the formation
Specificity: of product(s),
24 25 26
• Some amino acid residues allow a e.g. 20 and 41
particular substrate molecule to ‘fit’.
• Some amino acid residues bring about other amino acid residues interact to form the
particular chemical changes. three-dimensional structure of the enzyme
▲ Figure 3.5 The induced fit hypothesis of enzyme action
slight change in
shape of active
site as substrate
molecule fits,
glucose
and reaction
+ ATP takes place
two polypeptide
chains make up
the enzyme
hexokinase
(computer-generated
molecular model)
▲ Figure 3.6 Computer-generated image of the induced fit hypothesis in action

10

Naming enzymes
Many enzymes have a name based on the name of their substrate, with the
ending -ase added. For example, lactase hydrolyses lactose and amylase
hydrolyses amylose.
3
Other enzymes have been given names that tell us little or nothing about
what they do, such as many of the enzymes of digestion, for example, pepsin,
trypsin and rennin.
Today, systematic naming of enzymes is based on an agreed classification of

enzymes and on the name of the substrate catalysed. These types of name are
long and detailed and are outside the scope of this book. They are used in the
communications of enzymologists but not in everyday usage. However, you are
already familiar with certain enzymes. For example, the enzymes that catalyse
the formation of two products from a larger substrate molecule by a hydrolysis
reaction are classified as ‘hydrolases’. Can you name a hydrolase?
Question 2 a Define the term ‘catalyst’.

b List two differences between inorganic catalysts and enzymes.
SUMMARY
n Metabolism, all the chemical reactions of life, consists and key hypothesis). Enzymes work by lowering the
of anabolic reactions, the build up of complex activation energy needed for a reaction to occur.
molecules from smaller ones, e.g. protein synthesis, n A slight change in shape of the substrate molecule
and catabolic reactions, the breakdown of complex when it binds to the active site helps raise the
molecules, e.g. oxidation of sugar in respiration. molecule to a transition state (the induced fit
n All reactions of metabolism are made possible by hypothesis), from which the products may form.
enzymes. Enzymes are biological catalysts and The enzyme is released for reuse.
most are made of globular protein. An enzyme n The rate of an enzyme-catalysed reaction is found
is highly specific to the type(s) of substrate by measuring the disappearance of the substrate or
molecule and type of reaction that it catalyses. the accumulation of the product in a given period
n Enzymes work by forming a temporary complex of time. The initial rate of reaction is taken since
with a substrate molecule at a special part of the the reaction rate falls with time under experimental
enzyme surface, called the active site (the lock conditions.
Examination practice questions

1 The enzyme sucrase catalyses the breakdown of the glycosidic bond in sucrose.
A student investigated the effect of increasing the concentration of sucrose
on the rate of activity of sucrase.
Ten test tubes were set up with each containing 5 cm3 of different concentrations
of a sucrose solution. The test tubes were placed in a water bath at 40°C for
10 minutes. A flask containing a sucrase solution was also put into the water bath.
After 10 minutes, 1 cm3 of the sucrase solution was added to each test tube.
The reaction mixtures were kept at 40°C for a further 10 minutes.
After 10 minutes, the temperature of the water bath was raised to boiling
point. Benedict’s solution was added to each test tube. The time taken for a
colour change was recorded and used to calculate rates of enzyme activity.
The results are shown in the graph on the next page.
a i Name the type of reaction catalysed by sucrase. [1]
ii Explain why the temperature of the water was raised to boiling point. [2]
b Describe and explain the results shown in the graph. [5]
[Total: 8]
11

12
rate of enzyme activity/arbitrary units

10
2
3 Enzymes
0
0 20 40 60 80 100
concentration of sucrose/g dm–3
Cambridge International AS and A Level Biology 9700, Paper 21 Q4 June 2011
2 a Describe how enzymes take part in chemical reactions. [4]

Starch phosphorylase is an enzyme found in plant cells. In potato tuber cells,
the enzyme takes part in the breakdown of starch when the tuber begins to
grow.
starch phosphorylase
starch + phosphate ions glucose-1-phosphate
A student investigated the effect of pH on this reaction using two buffer

solutions.
The student prepared four test tubes, A to D, as shown in the table and
described below.
The student made an extract of potato tissue that contained the enzyme.
Some of this extract was boiled.
A solution of potassium dihydrogen phosphate was added to some tubes as a
source of phosphate ions.
The test tubes were left for 10 minutes in a water bath at 30 °C and then
samples were tested with iodine solution.
b i State what the student would conclude from a positive result with
iodine solution. [1]
ii Explain why the student boiled some of the extract in this
investigation. [2]
c Explain the results shown in the table below. [4]
[Total: 11]
Test Contents Results

tube Volume of Volume of Volume of pH of Enzyme with iodine
starch glucose-1- potassium buffer extract solution
solution/cm3 phosphate dihydrogen solution after
solution/cm3 phosphate 10 minutes
solution/cm3
A 2 0.5 6.5 unboiled negative
B 2 0.5 2.0 unboiled positive
C 2 0.5 6.5 boiled positive
D 2 6.5 boiled negative
12

3 The diagram shows
3
an apparatus used in
an investigation using
substrate solution
immobilised enzymes. It is
not expected that you will
immobilised enzyme in
have done this investigation. burette
A solution of a substrate
was poured into a burette
containing an enzyme
immobilised onto alginate

beads. The liquid passing liquid collected
from burette
through the burette was
collected into a beaker
and the concentration of
substrate and the concentration of the product measured. The table shows
the results obtained by five students.
Enzyme concentration Enzyme concentration

0.2 g dm−3 0.4 g dm−3 0.2 g dm−3 0.4 g dm−3
Substrate concentration/g dm−3 Product concentration/g dm−3
Repeat 1 Repeat 2 Repeat 1 Repeat 2 Repeat 1 Repeat 2 Repeat 1 Repeat 2
Student A 24 26 14 13 32 33 60 64
Student B 25 22 12 12 34 39 60 63
Student C 22 23 10 13 35 32 59 61
Student D 18 24 11 12 34 33 62 68
Student E 25 28 13 18 30 32 65 64
b Identify two variables and explain how each might be controlled. [2]
c On a copy of the table above, indicate by placing a circle around the value,
two results that are anomalous. [2]
d A student drew the following conclusion from this investigation:
Doubling the enzyme concentration doubled the rate of reaction of the
enzyme.
i State one way in which the evidence in the table above supports the
conclusion. [1]
ii State two ways in which the reliability of the results might be
improved. [2]
[Total: 7]
13
482876_Cam_AS_A_Level_Biology_001-013.indd 13 31/07/19 9:22 AM

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482876_Cam_AS_A_Level_Biology_001-013.indd 1 29/07/19 9:46 PM

4 Cell membranes and transport

5 The mitotic cell cycle

6 Nucleic acids and protein synthesis

482876_Cam_AS_A_Level_Biology_001-013.indd 2 29/07/19 9:46 PM

12 Energy and respiration

15 Control and co-ordination

17 Selection and evolution

18 Classification, biodiversity and conservation

482876_Cam_AS_A_Level_Biology_001-013.indd 3 29/07/19 9:46 PM

19.1 Principles of genetic technology

482876_Cam_AS_A_Level_Biology_001-013.indd 4 29/07/19 9:46 PM

3.1 Mode of action of enzymes

Introducing enzymes and their role in metabolism

482876_Cam_AS_A_Level_Biology_001-013.indd 5 29/07/19 9:46 PM

reactions Enzymes as biological catalysts

Where do enzymes operate?

Enzymes control metabolism

482876_Cam_AS_A_Level_Biology_001-013.indd 6 29/07/19 9:46 PM

How enzymes work

3.1 Mode of action of enzymes

sucrose sucrose sucrose

sucrose sucrose sucrose

These events are what happens at

For the reaction to occur, sucrose sucrose glucose

Under normal conditions this

3 In the presence of one molecule of the enzyme sucrase (invertase),

▲ Figure 3.2 Can a reaction occur without an enzyme?

482876_Cam_AS_A_Level_Biology_001-013.indd 7 29/07/19 9:46 PM

3 As molecules react, they become unstable, high-energy intermediates, but

A model of what is going on is the boulder (the substrate) perched on a slope,

‘boulder on hillside’ model of activation energy without a catalyst, this

free energy change

The enzyme has an active site

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active site (here

3.1 Mode of action of enzymes

▲ Figure 3.4 The lock and key hypothesis of enzyme action

Enzymes are typically large globular protein molecules. Most substrate

Enzymes are highly specific

Catalysis by ‘induced fit’

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active site (pocket/crevice

The amino acids in a

▲ Figure 3.5 The induced fit hypothesis of enzyme action

▲ Figure 3.6 Computer-generated image of the induced fit hypothesis in action

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3.1 Mode of action of enzymes

Question 2 a Define the term ‘catalyst’.

Examination practice questions

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rate of enzyme activity/arbitrary units

Cambridge International AS and A Level Biology 9700, Paper 21 Q4 June 2011

2 a Describe how enzymes take part in chemical reactions. [4]

2 a Describe how enzymes take part in chemical reactions. [4]