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BUNDA CAMPUS
2018- 2019 FIRST SEMESTER QUIZ # 4
BACHELOR OF VETERINARY MEDICINE YEAR I
NAME
STUDENT NUMBER
INSTRUCTIONS
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
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
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6. Which of the following statements about an enzyme exhibiting allosteric kinetics with
cooperative interaction is false?
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
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:
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) 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
regulate.
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
reactions.
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
it.
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
compounds.
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
substrate"?
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
equation?
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.
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SECTION II SHORT ANSWER
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
O
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
marks)
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38. The graphs below show the amount of energy present during two chemical reactions.
Reaction A Reaction B
d. Of the two reactions shown, which one is more likely to start spontaneously and why? (2
marks)
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39. Michaelis-Menten kinetics is sometimes referred to as “saturation” kinetics. Why? (3
marks)
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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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