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Knowledge, Innovation, Excellence

2018- 2019 FIRST SEMESTER QUIZ # 4


Date: Thursday, 7 February 2019 Time: 08:00 – 10:00 hrs. Venue: Room AA1



 All questions should be answered in the space provided in this question booklet.
 This whole booklet should be submitted at the end of the quiz.
 There two sections; SECTION I and II
 SECTION I – Multiple choice questions
 SECTION II – Short answer questions

The Department of Veterinary Biomedical Sciences is devoted to environmental care: for

economic and ecological reasons, this exam is printed on double-side
Circle the correct answer.

1. In non-competitive enzyme action:

a) Vmax is increased
b) Apparent Km is increased
c) Apparent Km is decreased
d) Concentration of active enzyme molecule is reduced
e) None of the above

2. An allosteric enzyme influences the enzymes activity by:

a) Competing for the catalytic site with the substrate

b) Changing the specificity of the enzyme for the substrate
c) Changing the conformation of the enzyme binding to a site other than catalytic site
d) Changing the nature of the products formed
e) All of the above

3. Which of the following regulatory actions involves a reversible covalent modification of an


a) Phosphorylation of serine –OH on the enzyme

b) Allosteric modulation
c) Competitive inhibition
d) Non-competitive inhibition
e) None of the above

4. A competitive inhibitor of an enzyme has which of the following properties?

a) It is frequently a feedback inhibitor

b) It becomes covalently attached to an enzyme
c) It decreases the Vmax
d) It interferes with substrate binding to the enzyme
e) It causes irreversible inactivation of the enzyme

5. When [S] is equal to Km, which of the following conditions exist?

a) Half the enzyme molecules are bound to substrate

b) The velocity of the reaction is equal to Vmax
c) The velocity of the reaction is independent of substrate concentration
d) Enzyme is completely saturated with substrate
e) The reaction has reached equilibrium

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6. Which of the following statements about an enzyme exhibiting allosteric kinetics with
cooperative interaction is false?

a) A plot of V vs [S] has a sigmoidal shape

b) An inhibitor may increase the apparent Km
c) Lineweaver-Burk plot is useful for determining Km and Vmax
d) Removal of allosteric inhibitor may result in hyperbolic V vs [S] plot
e) Small changes in [S] produce the largest change in V when [S] = Km

7. Match the following:

A. Citrate + CoA → Acetyl-CoA + H2O + OAA

B. ATP + Acetate + CoA → AMP + Hydrophosphate + Acetyl-CoA
C. Lactate + NAD+ → Pyruvate NADH + H+
D. Acetyl-CoA + H2O → CoA + Acetic acid

1. Lyase ________
2. Oxidoreductase ________
3. Ligase ________
4. Hydrolase ________

8. An enzyme that catalyses the conversion of an aldose sugar to a ketose sugar would be
classified as one of the:

a) Transferases
b) Isomerases
c) Oxidoreductases
d) Hydrolases
e) Lyases

9. In which of the following types of enzymes an inducer is not required?

a) Inhibited enzyme
b) Cooperative enzyme
c) Allosteric enzyme
d) Constitutive enzyme
e) None of the above

10. In which of the following types of enzyme water may be added to a C=C double bond
without breaking the bond?

a) Hydrolase
b) Hydratase
c) Hydroxylase
d) Esterase
e) Oxygenase

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11. “Lock-and-key” model of enzyme action proposed by Fisher implies that:

a) The active site is flexible and adjust to substrate

b) The active site requires removal of PO4 group
c) The active site is complementary in shape to that of the substrate
d) Substrates change conformation prior to active site interaction
e) None of the above

12. In competitive inhibition which of the following kinetic effect is true?

a) Decreases both Km and Vmax

b) Increases both Km and Vmax
c) Decreases Km without affecting Vmax
d) Increases Km without affecting Vmax
e) Increases Vmax without affecting Km

13. In competitive inhibition of enzymes action:

a) The apparent Km is decreased

b) The apparent Km is increased
c) Vmax is decreased
d) Apparent concentration of enzyme molecules decreased
e) Vmax is increased

14. Enzymes increase the rates of reaction by:

a) Increasing the free energy of activation

b) Decreasing the energy of activation
c) Changing the equilibrium constant of the reaction
d) Increasing the free energy change of the reaction.
e) Decreasing the free energy change of the reaction

15. Which of the following is a factor which can affect enzyme activity?
a) availability (concentration) of enzyme and/or substrate molecules
b) Temperature
c) pH
d) Regulatory molecules
e) All of these

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16. Gastric Protease and Intestinal Protease are digestive enzymes found in humans. Which
statement best expresses the information represented in the graph shown?

a) The action of enzymes varies with pH.

b) A pH of 7 provides the optimum environment for all digestive enzymes.
c) Gastric protease is active at from pH 0 to 12.
d) Acids have a pH greater than 7.
e) All of the above.
17. Which letter represents an enzyme functioning to hydrolyze molecule "A" in the diagram

a) A
b) B
c) C
d) D
e) E
18. Select the FALSE statement below:
a) Enzymes are substrate-specific catalysts that are not used up in the reactions they
b) Enzyme concentrations in plasma are frequently used in the diagnosis of disease.
c) Enzymes are sometimes used to treat disease.
d) Coenzymes are inorganic prosthetic groups, that help to facilitate enzyme-catalyzed
e) Not all enzymes are proteins.

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19. Select the TRUE statement below:
a) Allosteric interactions may play a part in inducing enzyme activity, but not inhibiting
b) Kinases are known to shift a phosphate group from one oxygen atom to another
within the same molecule.
c) Phosphatases are known to remove phosphate groups from phosphorylated
d) Peptidases are required for the formation of peptide bonds in proteins.
e) When pyruvate is converted to lactate, NADH is formed.
20. Which one of the following enzymes is activated irreversibly?
a) Pepsinogen
b) Glycogen phosphorylase
c) Glucokinase
d) Lactate dehydrogenase
e) Hexokinase
21. Hydrolases catalyze:
a) The cleavage of bonds between carbon and some other atom by the addition of H2O
across the bond.
b) Oxidation/reduction reactions.
c) The transfer of phosphate residues from ATP to enzymes or metabolic intermediates.
d) The formation of C-O, C-S, C-C, and C-N bonds by joining two molecules together in
reactions requiring energy.
e) Phosphate removal.
22. Synthases:
a) Transfer amino groups from proteins to phospholipids.
b) Facilitate the hydrolysis of macromolecules.
c) Help to catalyze oxidation/reduction reactions.
d) Catalyze interconversion of amino acid isomers.
e) Stimulate synthesis without using ATP.
23. Enzymes which transfer phosphate from ATP to enzymes or metabolic intermediates are
referred to as:
a) Mutases.
b) Phosphorylases.
c) Kinases.
d) Phosphatases.
e) Ligases.

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24. The variable which measures the affinity of an enzyme for its substrate is:
a) k1
b) Km
c) V
d) Vmax
e) [S]
25. Temperature and pH are known to affect:
a) [S]
b) [E]
c) Km but not Vmax
d) Vmax but not Km
e) Km and Vmax
26. The maximal velocity of an enzyme-catalyzed reaction is:
a) Decreased in the presence of a competitive inhibitor.
b) Found on the x-axis of a Lineweaver-Burk plot.
c) Known as the Michaelis-Menten constant.
d) Increased in the presence of a non-competitive inhibitor.
e) Decreased in the presence of an irreversible inhibitor.
27. Which one of the following therapeutic inhibitors is considered to be a "suicide
a) Aspirin
b) Captopril
c) Coumadin
d) Edrophonium
e) Mevastatin
28. The y-intercept on a Lineweaver-Burk plot is:
a) 1/2 Vmax
b) 1/2 Km
c) 1/Vmax
d) 1/Km
e) -1/Km
29. Which one of the following is an accurate representation of the Mechaelis-Menten
a) V=Vmax +[S]/(Km -[S])
b) V=Vmax [S]/Km [S]
c) V=Vmax [S]/(Km +[S])
d) V=Vmax +[S]/Km [S]
e) V = (Vmax/[S])(Km/[S])

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30. All of the following are TRUE of competitive inhibitors, EXCEPT:
a) They are usually structural analogues of the substrate.
b) They reduce the apparent Km (Km') of the reactions they inhibit.
c) The Vmax of the enzyme-catalyzed reaction in the presence of a competitive inhibitor
usually remains unchanged from normal.
d) They are sometimes used therapeutically to control the activity of target enzymes.
e) Their effects can usually be reversed by increasing the substrate concentration.
31. Which type of enzyme inhibitor below is known to affect both Vmax and Km?
a) Irreversible
b) Uncompetitive
c) Non-competitive, reversible
d) Competitive, reversible
e) Therapeutic
32. The effectiveness of allosteric effectors in regulating metabolic pathways is based on their
ability to:
a) Change the conformation of the target enzyme(s)
b) Alter the concentration of the target enzyme(s)
c) Denature the target enzyme(s)
d) Interfere with competitive inhibitors
e) Interact with multiple substrate-binding sites on the target enzyme(s)
33. Which of the following enzymes in the anabolic pathway represented below is most likely
to catalyze the rate-limiting step in the biosynthesis of A6?

a) E1
b) E2
c) E3
d) E4
e) E5

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34. The enzyme reaction scheme below most closely depicts:

a) Non-competitive inhibition
b) Mixed inhibition
c) Uncompetitive inhibition
d) Competitive inhibition
e) Concerted feedback inhibition

35. One of the enzymes involved in glycolysis, aldolase, requires Zn2+ for catalysis. Under
conditions of zinc deficiency, when the enzyme may lack zinc, it would be referred to as the:

a) Apoenzyme.
b) Coenzyme.
c) Holoenzyme.
d) Prosthetic group.
e) Substrate.

36. Which of the following can be used to determine the rate of enzyme-catalyzed reactions.

a) Rate of disappearance of the enzyme

b) Rate of disappearance of the substrate
c) Rate of disappearance of the product
d) Change in volume of the solution
e) Increase in activation energy

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37. Consider the activity of an enzyme as shown in the graphs below. ‘Rate of Reaction’ refers
to the amount of product produced over time-it is not the concentration of product formed.

a. Based on the temperature at optimum activity for the enzyme above (graph A), in what type
of organism is this enzyme most likely found? Justify your answer. (2 marks)

b. Explain, on a molecular level, what is happening at 20OC during this reaction? 37OC? 80
C? (3 marks)

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c. Interpret the results in graph B. On a molecular level, explain the significance of
maintaining an excess of substrate in the reaction. Would you anticipate that every enzyme
will have the same rate of reaction? (3 marks)

d. Interpret the results in graph C. Explain why, unlike in graph B, the rate of reaction begins
to plateau. Include why the experimenter held the enzyme concentration constant. (3

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38. The graphs below show the amount of energy present during two chemical reactions.

Reaction A Reaction B

a. Draw an arrow on each graph to show the energy of activation. (1 mark)

b. Which of the above reactions would be considered an energy-absorbing (endergonic)

reaction? Why? (2 marks)

c. Define "activation energy". (2 marks)

d. Of the two reactions shown, which one is more likely to start spontaneously and why? (2

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39. Michaelis-Menten kinetics is sometimes referred to as “saturation” kinetics. Why? (3

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40. Write out the equation that describes the mechanism for enzyme action used as a model by
Michaelis and Menten. List the important assumptions used by Michaelis and Menten to derive
a rate equation for this reaction. (8 marks)

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