Biocatalysis

CHAPTER 4: BIOCATALYSIS (PYQ)

PSPM II 2016/2017
1. (a) Define enzyme. [1 mark]
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(b) State three (3) properties of enzymes. [3 marks]

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(c) What determines the amount of product produced in an enzymatic reaction? [2 marks]
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(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]
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(e) Catecolase causes the browning of cut fruits like apples. An apple was bitten in two areas;
one area wascexposed while another area was covered with lime juice. Why had the
exposed area turned brown? [2 marks]
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PSPM II 2011/2012
2. (a) (i) Draw a graph showing the changes of energy with and without the presence of an
enzyme.
[3 marks]

Biology Unit, KMJ 71

 Biocatalysis

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

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(iii) How does enzyme influence a biochemical reaction? [1 mark]

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(b) FIGURE 1 shows an enzyme action.

FIGURE 1
(i) Identify the sites labeled F and G. [2 marks]

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(ii) Structure H can bind to G site. What is H and how does it affect the rate of reaction?
[3 marks]
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UPS I 2009/2010

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

enzyme catalyzed reaction working at its optimum temperature.

Biology Unit, KMJ 72

 Biocatalysis

FIGURE 2

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

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

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

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

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(c) Briefly explain why high fever can be fatal to human beings? [2 marks]

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PSPM I 2009/2010

4. FIGURE 3 shows the effect of factor X and factor Y on the rate of enzymatic reaction.

Biology Unit, KMJ 73

 Biocatalysis

FIGURE 3
(a) (i) State the factor X and factor Y. [2 marks]

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

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(iii) What happens to the active site of enzyme at the point A to point B? [1 mark]

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(iv)How do the kinetic energy of enzyme and substrate effects the reaction rate at the
point P to point Q? [3 marks]

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(v) What happens to the enzyme at point R? [1 mark]

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

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

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Biology Unit, KMJ 74

 Biocatalysis

UPS I 2010/2011

5. (a) FIGURE 4 shows a graph of an enzyme reaction.

FIGURE 4

(i) What is meant by an enzyme? [2 marks]

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

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(iii)Explain how the active site of an enzyme can reduce the activation energy. [2 marks]

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

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

Biology Unit, KMJ 75

 Biocatalysis

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(c) Malonate is the inhibitor for the enzyme succinate dehydrogenase. How would you
determine whether malonate is a competitive inhibitor or noncompetitive inhibitor?
[2 marks]
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PSPM II 2014/2015
6. FIGURE 5 shows an enzyme activity in a chemical reaction.

FIGURE 5
(a) (i) Identify T. [1 mark]

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

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

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(b) Molecule P is an organic molecule tightly bound to the enzyme.

(i) Identify P. [1 mark]

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

Biology Unit, KMJ 76

 Biocatalysis

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

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(d) Give TWO factors which prevent the production of R and S. [2 marks]

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(e) (i) State the condition during which an enzyme is saturated. [1 mark]

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(ii) In what way the enzyme productivity can be increased in (e)(i)? [1 mark]

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UPS II 2012/2013
7. FIGURE 6 shows an enzyme and four other molecules.

FIGURE 6
(a) (i) Name the part labeled T. [1 mark]

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(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]

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Biology Unit, KMJ 77

 Biocatalysis

(iii) Molecules P and Q inhibit the enzyme in different ways. State briefly how each of the
molecule inhibits the enzyme. [4 marks]

P: __________________________________________________________________

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Q: ________________________________________________________________________

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(b) There are two hypotheses on the mechanism of enzyme action which are ‘lock and key’
and ‘induced fit’. How do these hypotheses differ in terms of the enzyme’s active site?
[1 mark]
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(c) Why amylase is unable to catalyze the conversion of a protein into amino acids?
[2 marks]
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UPS I 2007/2008
8. (a) FIGURE 7 shows two models for enzyme-substrate action.

FIGURE 7
(i) Name the P and Q models. [2 marks]

Biology Unit, KMJ 78

 Biocatalysis

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(ii) Give the main differences between the P and Q models. [2 marks]

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(iii)How does the formation of enzyme-substrate (E+S) complex reduce the activation
energy? Explain. [2 marks]

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(b) FIGURE 8 shows the relationship between substrate concentration and the rate of
enzyme-catalysed reaction under three different conditions.

FIGURE 8

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

Enzymatic reaction without inhibitor : ____________________________

Enzyme + competitive inhibitor : ____________________________

Enzyme + noncompetitive inhibitor : ____________________________

(ii) Name the region of enzyme where the noncompetitive inhibitor binds. [1 mark]

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Biology Unit, KMJ 79
 Biocatalysis

PSPM I 2006/2007

9. FIGURE 9 shows three different enzyme reactions. A and B represent two types of inhibitors.

FIGURE 9

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

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

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

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(d) What happens to the reaction with inhibitors A and B if the substrate concentration is
increased? [2 marks]

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Biology Unit, KMJ 80

 Biocatalysis

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

(f) State the level of protein structure that form enzyme. [1 mark]

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UPS I 2008/2009

10. FIGURE 10 shows two types of enzyme inhibitor.

FIGURE 10
(a) Identify the type of inhibitor I and II. [2 marks]

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

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Biology Unit, KMJ 81

 Biocatalysis

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(c) In the presence of inhibitor I, explain what will happen to the rate of enzyme reaction.
[2 marks]
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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]

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(e) Explain how irreversible inhibitors cause permanent damage to enzymes. [3 marks]

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PSPM II 2018/2019

11. FIGURE 11 shows two different types of inhibitors, X and Y when compared to normal
enzyme.

FIGURE 11

(a) Identify X and Y. [2 marks]

Biology Unit, KMJ 82

 Biocatalysis

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(b) Give one (1) example of Y. [1 mark]

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(c) Differentiate the structure of X and Y. [2 marks]

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(d) How the activity of enzyme X and Y be optimized? [2 marks]

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PSPM II 2007/2008

12. (a) Describe how substrate concentration and pH affect the rate of enzyme-catalysed
reaction. [10 marks]
(b) Explain the mechanism of enzyme action using “induced fit” hypothesis with an aid of a
diagram. [10 marks]

PSPM II 2008/2009

13. (a) Describe the properties of an enzyme. [8 marks]

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

PSPM II 2010/2011

14. (a) Describe enzyme classification according to the International Union of Biochemistry
(IUB). [12 marks]
(b) Explain the different types of cofactor. [8 marks]

PSPM II 2013/2014

Biology Unit, KMJ 83

 Biocatalysis

15. (a) Explain the mechanism of enzyme action using ‘lock and key’ hypothesis and ‘induced
fit’ hypothesis. [10 marks]
(b) Briefly discuss the types of cofactor with appropriate examples. [10 marks]

PSPM II 2015/2016

16. (a) Describe the properties of enzyme and how pH can affect the rate of enzyme-catalysed
reaction. [12 marks]
(b) Explain the mechanism of enzyme action based on ‘lock and key’ hypothesis and
‘induced fit’ hypothesis. [8 marks]

Biology Unit, KMJ 84

 Biocatalysis

CHAPTER 4: BIOCATALYSIS (TUTORIAL)

MULTIPLE CHOICE QUESTIONS

1. Enzymes…
A. bind their substrates at active sites.
B. can bind to cofactors such as metal ions that participate in enzyme reactions.
C. are composed primarily of polypeptides, which are polymers of amino acids.
D. all statements are true.

2. The graph shows energy changes during an uncatalysed chemical reaction.

Which graph shows the energy changes when it is catalysed by an enzyme?

3. How does an enzyme increase the rate of reaction?

A. By shifting the equilibrium point of reaction.
B. By supplying the energy required to start the reaction.
C. By increasing the rate of random collision of molecules.
D. By bringing the reactant molecules to the correct orientation.

4. In the graph reaction rate against substrate concentration, the reason that the curve reaches a
plateau, and does not increase any further at high substrate concentration is that…

Biology Unit, KMJ 85

 Biocatalysis

A. there is a competitive inhibitor present.

B. there is a noncompetitive inhibitor present.
C. the active site is saturated with substrate.
D. all substrate has been converted to product.
5. The graph below shows the effect of temperature on enzyme-catalysed reaction with the amount
of substrate remaining constant.

The decrease in the rate of reaction in X is caused by…

A. the insufficient substrate to fit into all the active site.
B. the breaking of hydrogen and ionic bonds in the enzyme.
C. the competition between the substrate and product for the active site.
D. the hydrolysis of peptide bonds and disulphide bridges in the enzyme.

6. Malonic acid could inhibit the action of succinic dehydrogenase on succinic acid because…
A. Malonic acid could react with succinic acid.
B. Malonic acid could bind at the active site of succinic dehydrogenase.
C. Succinic acid could bind at the active site of succinic dehydrogenase.
D. Succinic acid could not bind at the active site of succinic dehydrogenase.

7. The graph below shows the rate of reaction with and without an inhibitor.

Which of the following is true regarding the above graph ?

Curve 1 Curve 2 Curve 3

A. Competitive inhibitor Noncompetitive Normal activity
inhibitor
Biology Unit, KMJ 86
 Biocatalysis

B. Competitive inhibitor Normal activity Noncompetitive

inhibitor
C. Noncompetitive Competitive inhibitor Normal activity
inhibitor
D. Normal activity Competitive inhibitor Noncompetitive
inhibitor
8. An allosteric enzyme…
A. is an important energy-carrying nucleotide.
B. raises the activation energy of the chemical reaction it catalyzes.
C. carries out either oxidation reaction or reduction reaction but not both.
D. has an active site where substrate molecules bind and another site that binds with
intermediate or end-product molecules.

9. Which of the following is an example of feedback inhibition in a metabolic pathway?

A. A noncompetitive inhibitor binds irreversibly to the substrate.
B. There is competition between two enzymes for a common substrate.
C. An enzyme-controlled reaction slows down as end product accumulates.
D. Variations in enzyme concentration affect the rate of the reaction it catalyses.

10. Hydrolases are one important class of enzyme that catalyze the…
A. conversions between isomers.
B. oxidation-reduction reactions.
C. splitting a molecule using water.
D. reaction in which double bonds are formed.

STRUCTURED QUESTIONS

1. FIGURE 1 shows a progress of a reaction that involves an enzyme.

FIGURE 1

a) Identify A, B and C.

Biology Unit, KMJ 87

 Biocatalysis

A: ___________________________________________________________

B: ___________________________________________________________

C: ___________________________________________________________
[3 marks]
b) Define the meaning of enzyme.

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[2 marks]

c) State the role of enzyme. According to your answer, describe the importance of enzyme
in living organism.

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[2 marks]

d) State the type of reaction occurs in the FIGURE 1.

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[1 mark]
e) Suggest what would happen to the rate of reaction if :-

i. the concentration of substrate is reduced? _____________________

ii. the temperature rise from 15°C to 25°C? _____________________

[2 marks]
2. FIGURE 2 below shows the structure of an enzyme.

Biology Unit, KMJ 88

 Biocatalysis

FIGURE 2

a) List THREE properties of enzyme.

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[3 marks]
b) Give ONE difference between active site and allosteric site of an enzyme.

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[1 mark]

c) Describe briefly, the mechanism of enzyme action.

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[3 marks]

d) Explain how heating beyond the optimum temperature affect the rate of reaction.

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[2 marks]

Biology Unit, KMJ 89

 Biocatalysis

e) List ONE other factor that affect the rate of enzyme reaction.

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[1 mark]

ESSAY QUESTIONS

1. a) Explain the mechanism of enzyme action using ‘induced fit’ hypothesis with an
aid of a diagram. (PSPM 1
2007/2008)
[10 marks]

b) What is meant by cofactors? By giving appropriate examples, explain types

and functions of cofactors.
[10 marks]

Biology Unit, KMJ 90