Biology Answer Scheme SB025

4: BIOCATALYSIS

4: BIOCATALYSIS

OBJECTIVE QUESTIONS

1. What is cofactor?

A. Non-protein molecules that is required for proper functioning of an enzyme.

B. Proteins molecules that is required for proper functioning of an enzyme.
C. Consist of coenzyme and prosthetic group.
D. It will bind permanently to the enzyme’s active site.

2. Mg2+, Cl-, Zn2+, Fe2+, Cu2+ and Ca2+ are the examples for?

A. Inhibitor C. Metal ions

B. Prosthetic group D. Coenzyme

3. Molecule X is a non-protein molecule, and it is also a heavy metal. It will bind tightly to
the active site of an enzyme (becomes part of the enzyme). What is molecule X?

A. Coenzyme C. Inhibitor
B. Prosthetic group D. Substrate

4. The graph below shows the rates of reaction with and without inhibitors.

Rate of reaction
1 1
Curve

Curve 2

Curve 3

Substrate concentration

Which of the following is TRUE regarding the graph above?

 Biology Answer Scheme SB025
4: BIOCATALYSIS

Curve 1 Curve 2 Curve 3

A. Competitive inhibitor Non-competitive inhibitor Normal activity
B. Competitive inhibitor Non- competitive inhibitor Normal activity
C. Non-competitive inhibitor Competitive inhibitor Normal activity
D. Normal activity Competitive inhibitor Non-competitive
inhibitor
5. An enzyme increases the rate of reaction by

A. shifting the position of equilibrium of the reaction.

B. increasing the rate of random collisions of molecules.
C. lowering the activation energy.
D. supplying the energy required to start the reaction.

6. Which class of enzyme catalyzes the formation of bonds between two molecules using energy
derived from the hydrolysis of ATP?

A. Oxidoreductases C. Ligases
B. Hydrolases D. Transferases

7. What happens to an enzyme when it is denatured?

A. The activation energy is doubled.

B. The activation energy is lowered.
C. The optimal temperature for enzyme action is doubled.
D. The shape of the enzyme molecule is changed.

8. A holoenzyme consists of
I. Substrate
II. Cofactor
III. Apoenzyme

A. I only C. II and III only

B. I and II only D. I, II and III

9. An example of competitive inhibition of an enzyme is the inhibition of

A. succinate dehydrogenase by malonic acid.

B. cytochrome oxidase by cyanide.
C. hexokinase by glucose-6-phosphate.
D. carbonic anhydrase by carbon dioxide.
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10. The diagram below shows the graph for the rate of reaction against substrate concentration of an
enzyme.
Rate of Reaction

Substrate Concentration

What causes the curve to become constant after point X?

A. The end product acts as an inhibitor to the reaction.

B. All enzyme molecules are saturated with substrate.
C. All substrates are converted into products.
D. The reaction has reached the optimum level.

11. The term apoenzyme is applicable to

A. simple enzyme
B. protein part of conjugate enzyme
C. organic cofactor of a conjugate enzyme
D. inorganic cofactor of a conjugate enzyme

12. Which one of the following statements regarding enzyme inhibition is CORRECT?

A. Competitive inhibition is seen a substrate competes with an enzyme for binding to an

inhibitor protein.
B. Non-competitive inhibition of an enzyme can be overcome by adding large amount of
substrate.
C. Competitive inhibition is seen when the substrate and the inhibitor compete for
the active site on the enzyme.
D. Noncompetitive inhibition is seen when the substrate and the inhibitor compete for the
active site on the enzyme.
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13. Some enzymes covalently bind a non-protein organic molecule to the active site. The
organic molecule concerned is required if the enzyme is to catalyze a reaction on a
substrate. What is the term used for such a molecule?

A. prosthetic group C. coenzyme

B. cofactor D. enzyme activator

14. FIGURE 1 shows two types of enzyme inhibition, P and Q. Which one of the following
statements is/are CORRECT?

Inhibition Inhibition
P Q

FIGURE 1

I For inhibition P, substrate ( ) is malonic acid and inhibitor ( ) is succinic acid.

II Inhibition Q cannot be reversed by increasing substrate concentration.
III Both inhibitors of inhibition P and Q bind loosely and temporarily to enzymes.

A. I only
B. I and II only
C. II and III only
D. I, II and III

15. Which of the following are factor that caused the denaturation of enzyme?

I. Extreme pH
II. Competitive inhibitor
III. Heavy metal effects
IV. High temperature
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A. I and III
B. I and IV
C. I, II and IV
D. I, III and IV

16. Substrate concentration increases the rate of an enzymatic reaction up to a certain point,
but then has no further effect and the reaction rate levels off. This is because?

A. Excess product is not released from the active site

B. Accumulation of end product shuts down the reaction
C. Excess substrate makes the enzymes change conformation
D. All the active sites are saturated with substrate molecule

17. Which of the following descriptions best describes an induced fit?

A. The process by which an active site alters shape such that it is ready to accept a
substrate
B. The process by which a substrate adopts the correct binding conformation before
entering an active site
C. The process by which a substrate binds to an active site and alters the shape
of the active site
D. The process by which an active site alters the shape of the substrate such that it
can adopt the necessary active conformation for binding

STRUCTURED AND ESSAY QUESTIONS

4.1 PROPERTIES OF ENZYME AND MECHANISM OF ACTIONS

1. (a) Define enzyme.

[1 mark]
Globular protein/ biological catalyst that speedup the (rate of) reaction

(b) State THREE (3) properties of enzymes

[3 marks]
- Globular protein
- Highly / very / extremely specific (in action)
- Lowers the activation energy
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- Influence by optimum / very high / extremely high temperature / pH

value / enzyme concentration / cofactor / inhibitor / substrate
concentration
- Reusable // does not change at the end of the reaction
- Any THREE answer
(c) What determines the amount of product produced in an enzymatic reaction?
[2 marks]
- Amount/ concentration of substrate
- (presence of) non-competitive inhibitor

(d) What will happen to the rate of enzyme activity when the shape of enzyme’s
active site is altered? Give a reason. [2 marks]
- Decreases/ lowers // no reaction occurs
- The substrate cannot bind to active site // Enzyme-substrate complex is
not formed / the substrate is not complementary to active site

(e) Catecolase causes the browning of cut fruits like apples. An apple was bitten in
two areas; one area was exposed while another area was covered with lime juice.
Why had exposed area turned brown?
[2 marks]
- Catecolase / enzyme is active / not denatured / Enzyme reaction occurs
- Oxidation occurs / oxidize apple
(PSPM 2016/17)

2. (a) FIGURE 2 shows the influence of substrate concentration on the rate of an

enzyme catalyzed reaction working at its optimum temperature.

FIGURE 2

(i) Explain the reaction curve in FIGURE 2. [2 marks]

- At low substrate concentration, rate of reaction increases as
substrate concentration increase until reach maximum rate
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- Further increase in substrate concentration, will not increase the

rate of reaction / rate of reaction remains constant

(ii) Draw a line on the graph above if the temperature is increased starting at
point A. [1 mark]

(iii) Explain your answer in (a)ii. [2 marks]

- High temperature denatures some of the enzyme molecule.
- Rate of enzyme reaction is reduced / decreased.

(b) State THREE classes of enzyme according to IUB. [3 marks]

- Transferase - Lyase - Ligase
- Oxidoreductase - Isomerase - Hydrolase
Any THREE answers

(c) Briefly explain why high fever can be fatal to human beings? [2 marks]
● When high fever, high body temperature will denature the enzyme.
● Enzyme active site change in conformation, substrate cannot bind to
active site (of enzyme). Enzyme-catalyzed reaction does not occur.

(UPS 2009/10)
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3. (a) FIGURE 3 shows a graph of an enzyme reaction.

FIGURE 3
(i) What is meant by an enzyme? [2 marks]
A biological catalyst that speed up the rate of reaction by lowering
activation energy

(ii) Name the parts labeled R and S. [2 marks]

R : activation energy without enzyme
S : activation energy with enzyme

(iii) Explain how the active site of an enzyme can reduce the activation energy.
[2 marks]
- Bring substrate together into correct orientation / closer to each
other
- Facilitate breaking of old bond and formation of new bond between
substrate

(b) (i) How are enzymes classified? [1 mark]

Based on type of reaction it catalyzed

(ii) State ONE class of enzyme. [1 mark]

- Transferase - Lyase - Hydrolase
- Oxidoreductase - Ligase - Isomerase

(c) Malonate is the inhibitor for the enzyme succinate dehydrogenase. How would
you determine whether malonate is a competitive inhibitor or non-competitive
inhibitor? [2 marks]
● By increasing the substrate concentration.
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4: BIOCATALYSIS

● If the rate of reaction increase, malonate is a competitive inhibitor. If the

rate of reaction does not increase, malonate is a non-competitive
inhibitor.
(UPS 2010/11)

4. FIGURE 4 shows an enzyme and four other molecules.

FIGURE 4

(a) (i) Name the part labeled T. [1 mark]

Active site

(ii) Which of the two molecules, R or S is more likely to be the substrate for
the given enzyme? Give your reason. [2 marks]
● R
Dependent
● The shape of molecule R is complementary / compatible with the
shape of active site of enzyme / T

(iii) Molecules P and Q inhibit the enzyme in different ways. State briefly
how each of the molecule inhibits the enzyme. [4 marks]
P:
● is non-competitive inhibitor / allosteric inhibitors
● binds to allosteric site of enzyme
Any TWO answers
● change the shape / conformation of the active site
● substrate can no longer bind to the active site
Q:
● is competitive inhibitor
● the shape is similar / partially same to the shape of substrate / R
● Q competes with R to bind to T // Q binds to T thus, prevents
substrate / R from binds to active site of enzyme
Any TWO answers
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(b) Why amylase is unable to catalyze the conversion of a protein into amino acids?
[2 marks]
● Due to specificity of the enzyme
● Active site has specific shape
● Active site is complementary to starch / starch causes induced fit
● Protein will not bind to active site / fit active site / cannot form
enzyme-substrate complex
Any TWO answers
(UPS 2012/13)

5. FIGURE 5 shows the effect of factor X and factor Y on the rate of enzymatic reaction.

FIGURE 5

FIGURE 5

(a) (i) State the factor X and factor Y. [2 marks]

Factor X : Substrate concentration
Factor Y : Temperature

(ii) What is point Q? [1 mark]

Optimum point / Optimum temperature

(iii) What happen to the active site of enzyme at the point A to point B?
[1 mark]
All active sites are fully saturated with substrate

(iv) How do the kinetic energy of enzyme and substrate effects the reaction
rate at the point P to point Q? [3 marks]
● When the kinetic energy of enzyme and substrate increases
● The molecules move faster and more collisions occur
● The enzyme-substrate complexes are formed more frequently, the
rate of reaction increases
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(v) What happens to the enzyme at point R? [1 mark]

The enzyme is denatured

(b) State the level of protein structure that forms enzymes. [1 mark]
Tertiary / Quaternary

(c) How do enzymes speed up the rate of reactions? [1 mark]

By lowering the activation energy
(PSPM 2009/10)

6. (a) (i) Draw a graph showing rate of reaction with and without the presence of an
enzyme. [3 marks]

OR

Axis : 1 mark
Curve (with enzyme) + label : 1 mark
Curve (without enzyme) + label : 1 mark
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4: BIOCATALYSIS

(ii) What is activation energy? [1 mark]

Minimum energy required to start a chemical reaction

(iii)
How does an enzyme influence a biochemical reaction? [1 mark]
Lowering the activation energy
(PSPM 2008/2010)
7. FIGURE 6 shows an enzyme and a substrate action mechanism.

FIGURE 6

(a) Name the hypothesis of the mechanism in FIGURE 6. [1 mark]

Induced fit mechanism

(b) Describe the events that occur when the substrate binds to the active site of enzyme.
[3 marks]
- The binding of the substrate induces the enzyme to change its shape slightly.
- This lead a better fit between the active site and the substrate.
- There is also a slight alteration to the shape of substrate.

(c) How does enzyme affect the activation energy of a reaction? [1 mark]

Enzymes lowers the activation energy.

(d) What happens to the rate of reaction at the highest substrate concentration? [1 mark]

The rate of reaction become constant.

(e) State two (2) types of reversible inhibition. [2 marks]

Competitive inhibition
Non-competitive inhibition
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(f) Give one (1) example of inhibitor for each type of reversible inhibition. [2 marks]

Competitive inhibition – Malonic acid / malonate

Non-competitive inhibition – ATP / isoleucine / cyanide

8. Describe the properties of an enzyme. [8 marks]

i. All enzymes are globular proteins

ii. Act as a biological catalyst that speed up the rate of metabolic reactions
iii. by lowering the activation energy.
iv. Enzymes do not change by the reaction // are reusable.
v. The rate of enzyme reaction is maximum at optimum temperature / pH
vi. Enzyme will be denatured at extreme pH and high temperature.
vii. Enzyme may catalyze reversible reaction.
viii. Highly specific in action // only catalyze a reaction when the substrate and
active site have complementary shapes // Active site of enzyme is specific to its
substrate.
ix. Has active site for reaction
x. Required in small amount to catalyze reaction.
(PSPM 2008/2009)

9. Describe enzyme classification according to the International Union of Biochemistry

(IUB). [12 marks]

i. Oxidoreductase
ii. Catalyse the transfer of oxygen and hydrogen atoms between substrates / all
oxidation-reduction reactions / redox reactions.
iii. e.g. dehydrogenase / oxidase
iv. Transferase
v. Catalyse the transfer of a functional group from one substrate to another.
vi. e.g. transaminase / phosphorylase
vii. Hydrolase
viii. Catalyse the breakdown of chemical bond by adding water molecule.
ix. e.g. digestive enzymes: sucrose / protease / lipase
x. Lyase
xi. Catalyse the addition or removal of a chemical group.
xii. e.g. decarboxylase
xiii. Isomerase
xiv. Catalyse the rearrangement of functional group / atoms in a substrate
molecule.
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xv. e.g. isomerase / mutase

xvi. Ligase
xvii. Catalyse the formation of bonds between two substrate molecules by using
ATP energy.
xviii. e.g. synthetase
(PSPM 2010/2011)

10. With the aid of a diagram, explain activation energy in relation to the function
of enzyme.
[10 marks]
i.

ii. Labels for free energy and progress of reaction/ X and Y axis
iii. Label for activation energy/EA curve with enzyme
iv. Label for activation energy curve without enzyme
v. Activation energy is the energy that must be absorbed by the substrate to
start a chemical reaction // minimum energy required to initiate / start a
chemical reaction
vi. Without enzyme more activation energy is required to start a chemical
reaction
vii. With enzyme the activation energy is lowered
viii. By bringing the substrate close to each other (into correct orientation)
ix. Facilitate the breaking of bonds
x. enabling the reactant molecules to absorb enough energy
xi. Transition state is reached
xii. Speed up the chemical reaction / the rate of reaction
(PSPM 2016/2017)
 Biology Answer Scheme SB025
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11. Explain the mechanism of enzyme action using “induced fit” hypothesis with an aid of a
diagram. [10 marks]
(PSPM 2007/2008)
Substrate

Active site

Enzyme Enzyme-substrate complex Products

Diagram:
i. Label the substrate and enzyme.
ii. Enzyme-substrate complex: show active site of enzyme changes shape.
iii. Products formed and enzyme change to original shape.

The induced fit hypothesis:

i. The active site of enzyme is flexible / not exactly compatible to the shape of
substrate.
ii. Enzyme collides with the substrate molecule.
iii. The substrate binds to the active site
iv. To form enzyme-substrate complex.
v. The binding induces a slight change in the conformation of active site of
enzyme.
vi. Allowing the substrate fit to enzyme precisely.
vii. The active site becomes fully complementary with substrate // enzyme stretch
existing bond.
viii. Enable the enzyme to carry out their catalytic function.
ix. Product is formed and enzyme changes back to original conformation.

12. With the aid of diagram, discuss the effect of temperature on the enzymatic reaction.
[12 marks]

(Optimum temperature)

Axis –1
2/1/0
Graph – 1
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i. All enzymes work within a range of temperature specific to the organism.

ii. Increase in temperature generally lead to increases in reaction rates.
iii. At low temperature, an enzyme-catalysed reaction takes place slowly.
iv. Hydrogen bond and hydrophobic interactions are not flexible enough.
v. Induced fit mechanism is not optimum.
vi. Movement of molecules slow // decrease the chances of colliding with active
sites.
vii. As temperature increases, the movement of molecules increases // increasing
chances of colliding with active sites of enzyme molecules.
viii. Thus the reaction between substrate and enzyme is accelerated.
ix. For every 10°C rise in temperature, the rate of reaction is doubled.
x. Up to optimum temperature.
xi. Optimum temperature is the temperature at which the reaction is at the
maximum rate.
xii. Beyond the optimum temperature, decrease in reaction rates.
xiii. This is due to the denaturizing of protein structure / change the conformation
of active sites.
xiv. Resulting from the breakdown of the weak ionic bond / hydrogen bonding /
hydrophobic interaction / disulphide bridge / van der Waals interaction
xv. Substrates are no longer fit into the active sites of the enzymes.
(PSPM 2008/2009)

13. Describe how substrate concentration and pH affect the rate of enzyme-catalysed reaction.
[10 marks]
(PSPM 2007/2008)
Substrate concentration:
i. At low substrate concentration, rate of enzyme reaction increase with
increasing substrate concentration.
ii. The active site of an enzyme molecule can bind with a certain number of
substrate molecules at a given time.
iii. At high substrate concentration, there is saturation of active site // increasing
of substrate concentration has no effect on the rate of reaction
iv. The rate of reaction reaches the maximum

pH effect:
i. Most enzymes are effective only within a narrow pH range.
ii. Maximum rate of reaction occurs at optimum pH.
iii. Different enzymes have different optimum pH.
iv. Deviation from optimum pH range results in excess H+ / OH- ions in the
medium.
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v. That alters the charge/ acidic / basic / functional groups / side chains (of amino
acids) in the enzyme.
vi. Causing the hydrogen bonds / ionic bond to be broken.
vii. Change the conformation of the active site // denaturation occurs.
viii. Substrate cannot fit into the active site (to form enzyme substrate complex).
ix. Lower down the rate of reaction.

14. Explain the factors affecting enzymatic reactions.

[10 marks]
i. Temperature
ii. Rate of enzyme reaction increases with the increase in temperature
iii. For every 10ͦC rise in temperature, the rate of reaction is doubled
iv. Until it reaches the optimal temperature (35-40ͦC)
v. Enzyme will denature if the temperature exceeds optimal temperature
vi. pH
vii. Each enzyme has a specific optimal pH
viii. Extreme pH / beyond optimal pH will denature the enzyme

ix. Cofactors
x. Non protein molecule needed for enzyme to function effectively

xi. Substrate concentration

xii. The rate of reaction is directly proportional to substrate concentration // rate
of reaction increase as substrate concentration increase
xiii. High substrate concentration does not affect the rate of reaction as the active
site is saturated with substrate // The rate of reaction become constant when
the active site is saturated with substrate
(PSPM 2017/2018)
4.2 COFACTOR

15. FIGURE 7 shows an enzyme activity in a chemical reaction.

FIGURE 7
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(a) (i) Identify T. [1 mark]

Active site (of enzyme)

(ii) Name the monomer T. [1 mark]

Amino acids

(iii) What is the main function of T. [1 mark]

● Attach / binds a substrate (to form an enzymes-substrate complex)
● As enzyme’s catalytic centre / site
● Catalyze the conversion of substrate to product
Any ONE answer
(b) Molecule P is an organic molecule tightly bound to the enzyme.

(i) Identify P. [1 mark]

Prosthetic group

(ii) Give ONE example of P. [1 mark]

FADH2 / Haem / vitamins / FAD

(c) Why is P more stable compare to an enzyme? [1 mark]

P is not a protein and will not denature

(d) Give TWO factors which prevent the production of R and S. [2 marks]
● Extreme temperature // very high / low temperature
● Extreme pH / too acidic / too basic
● Presence of inhibitor
Any TWO answers

(e) (i) State the condition during which an enzyme is saturated. [1 mark]
When active sites are fully filled / occupied / bound with substrate

(ii) In what way the enzyme productivity can be increased in 10(e)(i).

[1 mark]
Add more enzymes
(PSPM 2014/15)

16. Briefly discuss the types of cofactor with appropriate examples. [8 marks]
(PSPM 2013/2014)
Definition:
i. A non-protein component of an enzyme.
ii. Required for efficiency of enzymatic reaction.
iii. May bind tightly or loosely to the enzyme.
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Three types:

i. Enzyme activators// Inorganic ions// Metal ions

ii. Binds temporarily to the enzyme
iii. Change the conformation of active site for reaction to take place / to be more
compatible with substrate
iv. To enable the formation of enzyme-substrate complex.
v. (Examples Ca2+/ Zn2+/ Mg2+/ Fe2+)

vi. Coenzyme
vii. Non-protein organic molecules
viii. Derivatives of vitamin that binds loosely / temporarily to the enzyme.
ix. Act as carrier of hydrogen atoms, electrons of molecules.
x. (Examples: NAD+/NADP+/Coenzyme A/ ATP)

xi. Prosthetic group

xii. Non-protein organic molecules
xiii. Binds permanently / tightly to the protein portion of the enzyme / apoenzyme
xiv. To form holoenzyme / become a part of enzyme.
xv. (Examples: FAD/ haem/ Flavin mononucleotide/ FMN)

Note: Marks for explanations dependent on CORRECT types.

4.3 INHIBITORS

17. FIGURE 8 shows the relationship between substrate concentration and the rate of
enzyme-catalyzed reaction under three different conditions.

FIGURE 8
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(i) State the correct label for the following reactions. [3 marks]

Enzymatic reaction without inhibitor :W

Enzyme + competitive inhibitor : X
Enzyme + non-competitive inhibitor : Y

(ii) Name the region of enzyme where the non-competitive inhibitor binds.
[1 mark]
Allosteric site
(UPS 2007/08)

18. FIGURE 9 below show two types of inhibitor of enzyme.

FIGURE 9

(a) Determine the types of inhibitor I and II. [2 marks]

Inhibitor I : competitive (inhibitor)

Inhibitor II : non-competitive (inhibitor)

(b) Give ONE example for both inhibitor I and II. [2 marks]

Inhibitor I : malonic acid / malonate

Inhibitor II : isoleucine

(c) With the present of inhibitor I, explain what happen to the rate of enzyme reaction.
[2 marks]
● Decreases / reduces
● inhibitor I prevents the substrate from binding to enzyme active site
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(d) Suggest how the effect of inhibitor I can be reduced in order to increase the rate
of enzyme reaction. [1 mark]

By increasing the substrate concentration

(UPS 2008/09)
19. FIGURE 10 shows TWO mechanisms of enzyme inhibition.

FIGURE 10

(a) State the type of inhibitor in I and J. Give a reason for your answer. [4 marks]

Inhibitor I : Competitive inhibitor

Reason : The inhibitor competes with substrate for active site of
enzyme

Inhibitor J : Non-competitive inhibitor

Reason : The inhibitor binds to allosteric site of enzyme

(b) (i) Explain what happens to the rate of reaction in the presence of the
inhibitor I. [2 marks]

● Rate of reaction is reduced / lower / decreased

● The inhibitor prevents substrate from binds to the active site of
enzyme / substrate cannot bind to active site of enzyme

(ii) Explain what happens to the rate of reaction of inhibitor I if substrate

concentration is increased? [2 marks]

● Rate of reaction increase.

● Because the chances of substrate bind to active site of enzyme is
increased
(UPS 2011/12)
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20. FIGURE 11 shows three different enzyme reaction, A and B represent two types of
inhibitors.

FIGURE 11

(a) How do enzymes speed up the rate of reactions? [1 mark]

Lower the activation energy of reactants

(b) State the type of inhibitors A and B. [2 marks]

A : competitive (inhibitor)
B : non-competitive (inhibitor)

(c) How do inhibitors A and B bind to the enzymes? [2 marks]

A : bind to the active site
B : bind to the allosteric site

(d) What happens to the rate of reactions with inhibitors A and B if the substrate
concentration is increased? [2 marks]
A : increase
B : unchanged / no changes / remains the same

(e) Draw a curve to show the effect of increasing the temperature to enzymes activity.
[2 marks]

Peak of curve
(35ºC - 45ºC) : 1 mark

Shape of curve: 1 mark

Bell-shaped & skewed to
right
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(f) State the level of protein structure that form enzyme. [1 mark]
Tertiary / Quaternary structure level
(PSPM 2006/07)
21. FIGURE 12 shows an enzyme action.

FIGURE 12

(i) Identify the sites labeled F and G. [2 marks]

F : active site
G : allosteric site

(ii)Structure H can bind to G site. What is H and how does it affect the rate
of reaction? [3 marks]
● H is non-competitive inhibitor
● When H binds to G, conformation of F changes // substrate cannot
bind to F / cannot fit to F
● Rate of reaction is decreased
(PSPM 2011/12)
22. FIGURE 13 shows the curves for enzymatic reactions.

FIGURE 13
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(a) State the nature of inhibition for curves P, Q and R [3 marks]

P : No/ without inhibition
Q : Competitive
R : Non-competitive

(b) Briefly explain the enzyme activities for curves Q and R. [4 marks]
Q : Competitive inhibitor and substrate compete for the same active site
of the enzyme.
Rate of reaction decrease // Maximum rate of reaction reached when
more substrate added.
R : Non-competitive inhibitor and substrate bind to different sites/ on
the enzyme
Rate of reaction decreases.

*dependent on Q and R for (a) BUT Rate of reaction decrease.

(c) Which curve shows an inhibition that could not be recovered by the addition of
more substrate? [1 mark]
(Curve) R

(d) Digestion of lipid occurs in small intestine and is catalyzed by lipase. Briefly
explain the consequence of eating oranges to the digestion of lipid in the small
intestine. [2 marks]
- Lipase needs alkaline medium // orange create acidic medium in the small
intestine
- Lipase is not active/ slows down the digestion / hydrolysis of lipid //
Digestion of lipid in small intestine is not affected, pancreatic juice
neutralizes stomach acid in small intestine.
(PSPM 2016/17)
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23. FIGURE 14 shows the effect of two different chemicals on the activity of enzyme A.
The temperature, pH and enzyme concentration were kept constant during this
experiment.

FIGURE 14

(a) Explain the effect of chemical B and C on the activity of enzyme A.

[4 marks]
Chemical B compete/bind for the active site of the enzyme
Chemical B reduce/decrease/slow the enzymatic rate of reaction
The enzyme’s rate of reaction reaches the maximum rate of reaction

Chemical C binds to the allosteric site of the enzyme

Chemical C reduce/decrease the enzymatic rate of reaction
The enzyme’s rate of reaction does not reach the maximum rate of reaction

(b) Based on the experiment, what is chemical B and C?

[2 marks]
Chemical B: competitive inhibitor
Chemical C: non-competitive inhibitor

(c) Give one example of each:

[2 marks]
Chemical B: Malonate / ATP
Chemical C: Cyanide/ heavy metal ions/ nerve gases/ isoleucine
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(d) Does increasing the concentration of substrate overcome the effect of chemical B
towards activity of enzyme A? Why?
[2 marks]
Yes
The probability of an enzyme-substrate collision is higher // the substrates have
greater chance of binding to the active sites

24. FIGURE 15 shows two different types of inhibitors X and Y when compared to normal
enzyme.

FIGURE 15

(a) Identify X and Y.

[2 marks]
X: Competitive inhibitor
Y: Non-competitive inhibitor

(b) Give ONE example of Y.

[1 mark]
Heavy metal / toxins / poisons / lead / mercury / isoleucine / cyanide

(c) Differentiate the structure of X and Y.

[2 marks]
X: similar to the substrate, while
Y: different structure/shape to the substrate
 Biology Answer Scheme SB025
4: BIOCATALYSIS

(d) How the activity of enzyme X and Y be optimized?

[2 marks]
X: by increasing the concentration of substrate
Y: by removing the inhibitor // decrease the concentration of inhibitor

25. Using isoleucine as an example, explain how a non-competitive inhibitor affects enzyme
activity. [5 marks]

i. Isoleucine is an inhibitor to threonine deaminase.

ii. Noncompetitive inhibitor has different shape with substrate.
iii. Non-competitive inhibitor binds to allosteric site of enzyme.
iv. The binding changes the conformation of active site.
v. Substrate cannot bind to active site of enzyme.
vi. Rate of enzyme activity decreases.
vii. This inhibition cannot be overcome by increasing the substrate
concentration.