KEY KNOWLEDGE 3

REGULATION OF
BIOCHEMICAL
PATHWAYS IN
PHOTOSYNTHESIS AND
CELLULAR RESPIRATION
 FROM THE STUDY DESIGN
 the general structure of the biochemical pathways in
photosynthesis and cellular respiration from initial reactant to final
product
 the general role of enzymes and coenzymes in facilitating steps in
photosynthesis and cellular respiration
 the general factors that impact on enzyme function in relation to
photosynthesis and cellular respiration: changes in temperature,
pH, concentration, competitive and non-competitive enzyme
inhibitors
BIOCHEMICAL PATHWAYS
 METABOLISM
 Cell chemistry : biochemistry

 Understanding of…..

Carbohydrates
Lipids
Proteins
Nucleic acids

 Anabolic, endergonic, uphill, energy needing (eg. Photosynthesis and muscle development)

 Catabolic, exergonic, downhill, energy releasing (eg. Respiration, protein digestion)

 ATP cycle is the ‘go-between’

 Biochemical reactions in small ‘manageable’ steps

 Biochemical pathway is many small reactions leading to an overall ‘outcome’

 EXERGONIC REACTIONS
 These reactions release energy.
This refers
to the  They are also referred to as
ENERGY
catabolic reactions.
 Larger molecules are broken
down into smaller, less
complex molecules.

This refers to  Eg: cellular respiration, oxidation

the
MOLECULES
reactions (the addition of oxygen or removal of

electrons).
ENDERGONIC REACTIONS


These reactions require
energy.
 They are also referred to as
anabolic reactions.
 Smaller molecules are
combined to build larger,
more complex molecules.

 Eg: photosynthesis, reduction

reactions (the removal of oxygen or addition
ENDERGONIC VS EXERGONIC

1. Where does the energy go in an exergonic reaction?

2. Where does the energy come from in an exergonic reaction?
3. Which profile would fit photosynthesis?
4. Which profile would fit cellular respiration
 ENZYMES
 Most are protein
 Specific
 Lock and key
 Reusable
 Optimal conditions
 Drive metabolism

EXAMPLES
 Amylase = breaks down starch into glucose
 Lipase = breaks down lipids into fatty acids
 Protease = breaks down protein into amino acids
 Glucose 6 Phosphate Dehydrogenase =
_________________________________
 So the –ase helps identify an enzyme and the prefix helps identify
the reaction
 ENZYMES – WHAT ARE THEY?
 Large, globular proteins
 Specific three -dimensional conformation.
 Active site is a very specific area of the protein
which recognizes and binds to the substrate.
 “Shape determines function”
 Folding of polypeptide and R group exposure
determines the
active site
properties.
 MECHANISM OF ENZYME
ACTION
 Substrates have
specific shapes to
fit into the active
sites.
 Enzyme-substrate
complex formed,
then dissociates.
 Product is formed
and enzyme is
unaltered.
The substrate must be a complementary
shape to the active site.
NOT the same shape
 enzyme
A B
Label on the diagram

1. The enzyme
2. The active site
3. The substrate
4. The product(s)
5. The enzyme substrate
complex
 Enzymes: Catalase case study
 Catalyses the breakdown of hydrogen peroxide, (H O ) a toxic by product of
2 2

metabolic reactions, to the harmless substances, water and oxygen

 At a rate of 40 million reactions per enzyme per second!

Energy
No catalyst =
Substrate Input of 71kJ energy required

Product
With catalase
= Input of 8 kJ energy required

Progress of reaction
 FACTS
 When a reaction takes place the atoms in the substrate are
rearranged. Existing bonds are broken and new bonds are formed.
 For this to happen the substrates absorb energy (activation
energy) so that the bonds can break. When the new bonds form
energy is either released or more is absorbed.

CONDITIONS
 Optimum temperature and pH
 Enzyme concentration
 Substrate concentration
 Co enzymes
 Co factors
 What is
PH pH?
The concentration of hydrogen
ions in a litre of solution.
 Each individual enzyme Low pH = more acidic (high H+)

catalyzes a specific
reaction.
 The rate of these
enzymatic reactions is
highest at an optimal pH.

 The optimal pH is
dependent on the type
of enzyme and the
location where the
reaction occurs.
 EXAMPLE: PH
 Salivary amylase breaks down starch into
maltose at the neutral pH of the mouth: pH 7
 Pepsin requires the acidic pH of the stomach
to digest protein into smaller : pH 2-4
 A change in pH from the optimum changes
the enzyme shape and affect its ability to
combine with the substrate.
DENATURATION AT LOW PH
 Reducing agents
disrupt disulphide
bonds.
 They DO NOT break
or disrupt the
peptide bonds.
 TEMPERATURE
 Enzymes have an optimum
temperature range – this is
usually the temperature of
the environment that they
are found in.
 HOW DOES TEMPERATURE
AFFECT ENZYME ACTIVITY?
 As temperature increases molecules become
more excited and collide more often.
 This increase in collision increases the
opportunity for a substrate to bump into its
enzyme.
 However, if the temperature becomes too high
the structure of the protein is permanently
changed. The enzyme is said to have denatured.
This is often irreversible.
 Many enzymes denature at around 45 degrees celsius, however, some
bacteria have enzymes which function at much higher temperatures.
 If the temperature is too low, there will be little enzyme activity, but
 DENATURATION
Label on the diagram

1. An alpha helix
2. A beta sheet
3. Where disulphide bonds may hold the functional
protein together
 DENATURATION
At what
temperature
does this
enzyme begin
to denature?

In exam questions, don’t assume the enzyme is a

human/mammal enzyme and therefore has an optimal
temperature of 37 degrees. Read the question carefully.
 EXAMPLE: TEMPERATURE.
 In this experiment, the enzyme catechol oxidase,
found in plants, causes the browning of plant
tissue (here, potato).
 Which temperature saw the highest degree of
enzyme activity?
 ENZYME/SUBSTRATE
CONCENTRATION.
 Increasing substrate concentration increases
reaction rate, increasing the number of collisions
between the enzyme and the substrate resulting in
more enzyme-substrate complexes.
 Eventually, the substrate concentration will be
high enough to fill up or saturate all of the active
sites on the enzyme.
 At this point, the maximum rate of reaction has
been reached.
 Label on the graph

1. Independent variable
2. Dependent variable
3. The point of saturation
 COENZYMES
• A coenzyme is defined as an organic molecule that binds to the active
sites of certain enzymes to assist in the catalysis of a reaction.
• Coenzymes can function as intermediate carriers of factors (electrons,
hydrogen, energy) during these reactions or be transferred between
enzymes as functional groups
• Examples are ATP/ADP, NADH/NAD, NADPH/NADP
• ATP/ADP: Energy transfer (where is the energy in ATP?)
• NAD/NADH: Hydrogen transfer in cellular respiration (where is the H?)
• NADP/NADPH: Hydrogen transfer in photosynthesis (where is the H?)
• Structure not important
 THE ATP CYCLE
Cellular uses for ATP

Called: ___________ B: ___________

A: ___________
Adenosine-P-P-P
M: ___________

Energy input Energy release

Respiration

Adenosine-P-P Pi

Called: ___________
 Label on the diagram

1. What would be the purpose of ATP being a coenzyme

in the reaction below?
2. What would be the purpose of NADPH being the
coenzyme in the reaction below?
1. Describe the trend shown in the graph below

2. Explain the trend shown in the graph below

1. Describe the trend shown in the graph below

2. Explain the trend shown in the graph below

 ENZYME
CONDITIONS Label on the diagram

1. The enzymes optimal conditions

2. Where enzymes are denatured
3. Where collisions between enzyme and substrate are
low
4. Where collisions are high and active site is functional
 ENZYME
CONDITIONS
Graph and interpretation

1. Draw a graph showing enzyme activity with increased

substrate
2. Show on the graph where saturation is occurring
3. Show where not all active sites are occupied
4. If enzyme concentration was doubled how would the graph
look
ENZYMES OF PHOTOSYNTHSESIS
AND CELLULAR
Indicate on the RESPIRATION
diagram

1. At least 10 enzymes….you may need to conduct some

research
2. Circle a substrate that is also a product
3. What part of photosynthesis is one of the cycles?
______________
4. What part of respiration is one of the cycles?
________________
GLYCOLYSIS AND PENTOSE
PHOSPHATE PATHWAY

Indicate on the diagram

1. Glucose to Pyruvate = glycolysis (label

it)
2. Glycolysis occurs in the cytosol (label it)
3. Why do we need ribulose 5 phosphate
for?
___________________________________
4. What is the name of G6PD (research it)
___________________________________
5. People with favism lack G6PD, how
might this effect them?
_________________________________
 How

1. Does
phenylalanine
convert to tyrosine?
2. Does eating low fat
yoghurt help PKU
sufferers?
3. Can albinism
happen without
suffering PKU?
4. How does
alkaptonuria occur?
 ENZYME CONTROL
Key words: pyruvate, complementary, enzyme, slow,
allosteric
Add the key words from the key above into the correct space below
 Competitive inhibition

Inhibitor has a ______________ shape to the active site of the enzyme

 Non competitive inhibition

Inhibitor binds to an ___________ site which causes a change in the shape of the active site
 The diagram below could represent end product inhibition in glycolysis

The end product of glycolysis (_________) has a shape that will bind to enzyme 1 causing a
change in
shape of the ____________, which will _________ the production of the end product
 TYPES OF INHIBITION
Competitive Inhibition Non-Competitive Inhibition

 Shape of inhibitor similar to  Or Allosteric Inhibition

the substrate  Does not bind to Active Site.
 Blocks Active Site Binds to another site and
 Slows reaction, but can changes conformational shape
of enzyme.
eventually be removed, so
is reversible  Tends to affect overall rate of
reaction as not removed easily,
therefore often irreversible
 EXAMPLES: INHIBITION:
 Penicillin – inhibits enzyme action in bacteria
(and eventually kills it), so for this reason helpful
for humans with bacterial infections.
 Aspirin is an analgesic (anti-pain), anti-
inflammatory, and antipyretic (fever-reducing)
medicine that works by inhibiting the production
of messengers (called prostaglandins) that act on
the central nervous system. This occurs because
aspirin inactivates the COX-2 enzyme (by binding
to the active site) necessary to make these
messengers.
 INHIBITION

1. What is 1, 2, 3 (LHS) and the Electron Transport Chain (RHS)

2. Why is the diagram on the LHS non competitive?
3. What would make these inhibitors reversible or irreversible?
4. If a reversible competitive inhibitor is present, how would increasing
the substrate concentration effect the reaction
 IMPACT OF INHIBITION ON
METABOLISM
1. How would data such as shown in the graph be experimentally
gained?
2. Why does a competitive inhibitor lose its effect at high substrate
concentrations
3. Why does a non competitive inhibitor have more of an effect than
competitive inhibitors at high substrate concentrations?
 WHY IS ENZYME (PROTEIN)
STRUCTURE IMPORTANT?
Each enzyme (protein) molecule has a
characteristic 3D shape that results from coiling
and folding of the polymer chain.

The function of a protein depends upon the shape

of the molecule. For example the molecule on the
left (an enzyme: lipase) has a complementary
shape to the middle molecule (the substrate:
triglyceride). A diet drug (competitive inhibitor:
Xenical) was available initially in 1999.
THE RESULTS OF A TRIAL STUDY FOR
THE DIET DRUG XENICAL
Analysis of the study

‘Drug taken orally with

food’

1. Why 2 groups?

2. How would the 2

groups be treated

3. How successful?

4. What problems may

Have arisen?
 MULTIPLE CHOICE QUESTIONS
Scientists have found microorganisms living in
springs of boiling water. Many of these have been
classified as prokaryotic.
An enzyme from these microorganisms were
investigated over a range of temperatures. The
results obtained were plotted and are shown in the
following graph.
The temperature at
point X is most
likely

A. 10 degrees
B. 37 degrees
C. 57 degrees
D. 100 degrees
ATP (adenosine triphosphate) is essential to every living cell
because

A it captures energy from the breakdown of glucose and ADP

(adenosine diphosphate).
B exergonic and endergonic reactions could not take place
without it.
C it stores energy in a form that is instantly available to the cell.
D it stores energy released during the breakdown of ADP.

A series of chemical reactions that happen in a particular order

and are controlled by enzymes is referred to as a

A metabolic reaction
B metabolic pathway
C metabolism
D endergonic reaction
 SHORT ANSWER QUESTION
Glucose-6-phosphate dehydrogenase (G6PD) deficiency (commonly called favism) is a disease that can cause anaemia and
renal failure. It can be triggered from eating broad beans. G6PD catalyses the conversion of Glucose 6 Phosphate to
6 Phosphogluconate, which is the first step in the pentose phosphate pathway and links into glycolysis.
This pathway amongst other products forms the 5- carbon sugar, ribose.
(i) What is the main biomolecular importance is ribose
______________________________________________________________(1 mark)
(ii) What is the cellular location where G6PD is synthesized?
_____________________________________________________________(1 mark)
The gene that encodes for G6PD is 18,500 nucleotides in length.
(iii) How many nucleotides in total span the G6PD gene?
___________________________________________________________(1 mark)

The active form of the G6PD protein is made up of either two or four identical subunits
(iv) What level of arrangement is this referring to?
___________________________________________________________(1 mark)
When
The there are
diagram sufficient
across showsgrounds to suspect
the sequence favism,
of steps a direct
involved in test called the spot
the fluorescent
"Beutler
test. fluorescent spot test" is available.

c) (i) Describe the type of test result seen in an individual with favism
________________________________________________________ (1
mark)
(ii) Explain why a person without favism would produce a different result.

________________________________________________________________
_

__________________________________________________________(2
marks)