Biochem Engg PrelimExam

Sep 2.2021
I MULTIPLE CHOICE (Write the letter of the best answer)

1. A competitive inhibitor of an enzyme is usually_____.

a. a highly reactive compound b. structurally similar to enzymes c. water insoluble d. none of these

2. The types of inhibition pattern based on Michaelis-Menten equation

a. Competitive b. Non-competitive c. Uncompetitive d. All of these

3. The y-intercept in Lineweaver-Burk Plot is

a. 1/Vmax b. Vmax c. Km/ Vmax d. All of these
1 K 1 1
= m +
4. Which equation is a linearized plot of Michaleis-Menten equation v v max [ s ] v max
a. Lineweaver-Burk Plot b. Eadie-Hofstee plot c. Hanes-Woolf plot d. All of these

5. Type of competitor where binds E or ES complex other than at the catalytic site. Substrate binding unaltered, but ESI
complex cannot form products. Inhibition cannot be reversed by substrate.
a. Competitive b. Non-competitive c. Uncompetitive d. All of these

6. Type of competitor where it binds specifically, at the catalytic site, where it competes with substrate for binding in a
dynamic equilibrium- like process. Inhibition is reversible by substrate.
a. Competitive b. Non-competitive c. Uncompetitive d. All of these

7. Type of inhibitor where Km appears unaltered; Vmax is decreased proportionately to inhibitor concentration.
a. Competitive b. Non-competitive c. Uncompetitive d. All of these

8. The effect of non-competitive inhibitor to Lineweaver-Burk Plot

a. it can move the entire curve to the right b. it can change the y-intercept
c. it can change the x-intercept d. All of these

9. The rate determining step of Michaelis-Menten equation

a. The complex formation step b. The complex dissociation step to form a product
c. The product formation step d. All of these

10. The inactive form of enzyme

a. Apoenzyme b. enzyme c. holoenzyme d. co-factor

11. Which of the following is the best evidence for the lock and key theory of enzyme action?
a. Compounds similar in structure to the substrate inhibit enzyme activity
b. Enzymes are found in living organisms and speed up certain reactions
c. Enzymes speed up reactions by definite amounts d. Enzymes determine the direction of a reaction

12. A substrate binds to its enzyme at a location called the________.

13. a. coenzyme b. substrate c. active site d. holoenzyme

14. Denaturation of enzymes refer to

a. Improper arrangement of enzymes in metabolic pathway b. Loss of enzymes proper shape
b. Formation of the enzymes proper shape d. Formation of new isozyme for that enzyme

15. The building block of protein

a. Amino acids b. Nucleotides c. Fatty acids d. Monosaccharides

16. The building block of lipids

a. Amino acids b. Nucleotides c. Fatty acids d. Monosaccharides

17. Stores cellular information in the form of a code

a. Amino acids b. Nucleotides c. Fatty acids d. Monosaccharides

18. To which of the following enzymes belong?

a. Lipid b. Protein c. Nucleic acid d. Carbohydrate

19. The smallest possible sugar unit

a. Amino acids b. Nucleotides c. Fatty acids d. Monosaccharides

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20.“Blood sugar” in blood means
a.Glucose b. Fructose c. All of these d. None of these

21.Enzyme used used in breaking down sucrose

a. invertase b. glucoamylase c. all of these d. none of these

22.Decomposition of complex organic compounds to break them down to simpler organic compounds such as amino acids,
sugar and fatty acids.
a. hydrolysis b. acidogenesis c. acetogenesis d. methanogenesis

23.Zymase, a collective term for yeast enzyme is a mixture of how many different enzymes?.
a. 2 b. 4 c. 8 d. 12

24.Which of the following enzymes could break down vegetable starch

a. Diastase b. Pepsin c. All of these d. None of these

25.Coenzymes, together with certain inorganic chemicals

a. Conjugated proteins b. Glycoproteins c. enzyme cofactors d. Endo-enzymes

26.Enzymes that take part in the dissimilation and synthetic process within the cell.
a. CoEnzymes b. Glycoproteins c. enzyme cofactors d. Endo-enzymes

27. Which of the major class number of enzyme does oxidoreductases belong?
a. 1 b. 2 c. 3 d. 4

28.Which of the major class number of enzyme does lyses belong?

a. 1 b. 2 c. 3 d. 4

29.Class of enzymes which are induced.

a. mortalloenzymes b. synthesized enzymes c. holoenzymes d. apoenzymes

30.Enzymes which in most of the cases are not a part of the process taking place.
a. mortalloenzymes b. holoenzymes c. apoenzymes d. allosteric enzymes

31.The mechanism of enzymatic action involves

a. Slow degradation of the enzyme to form enzyme-substrate complex b. Temporary union of enzyme with
substrate
c. Resistance to deactivation by high temperature d. Rapid degradation of the enzyme to forma an enzyme-substrate
complex

32.Factor(s) that influence(s) enzymatic activity is (are)

a. Temperature b. pH c. Concentration, substrate & cofactors d. All of these

33.The cell walls of many gram positive bacteria can be easily destroyed by this enzyme
a. Lipase b. Lysozyme c. Pectinase d. Peroxidase

34.Which of the following is true.

a. Each enzyme has its own unique protein structure b. Each enzyme has its own unique protein shape
b. All of these d. None of these

35.Which of these is not a permanent part of an enzyme

a. Active site b. Coenzyme c. Cofactors d. Substrate

36.An additional non-protein molecule that is needed by some enzymes to help the reaction.
a. Holoenzymes b. Coenzyme c. Cofactors d. Apoenzymes

37.Cofactors that are bound and released easily are called

a. Holoenzymes b. Coenzyme c. Active site d. Apoenzymes

38.An inactive enzyme, activation of the enzyme occurs upon binding of an organic or inorganic cofactor.
a. Holoenzymes b. Coenzyme c. Cofactors d. Apoenzymes

39.Apoenzyme together with its cofactor

a. Holoenzymes b. Coenzyme c. All of these d. None of these

40.Enzyme controlled reactions proceed almost ________times faster than corresponding non-enzymatic reactions.
a. 1 hundred b. 1 thousand c. 1 million d. 1 billion

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41.Which of the following is true regarding the Lock-and-Key hypothesis
a. The substrate and active site match structurally b. The substrate and active site match chemically
c. All of these b. None of these

42.Which of the following is true regarding the Induced-Fit hypothesis

a. Substrate + enzyme, induces a change in the enzyme’s conformation
b. Active site is moulded to a precise conformation c. All of these d. None of these

43.Which of the following defines denaturing of enzymes

a. Change in shape b. Change in structure c. All of these d. None of these

44.Binding of the inhibitor causes the substrate binding site to change shape so the chemical reactions is not carried out
a. Competitive inhibitions b. Non-competitive inhibitions c. Uncompetitive inhibitions d. All of these

45.Substances which when added to the enzyme alter the enzyme in a way that it cannot accept the substrate.
a. Competitive inhibitionrs b. Non-competitive inhibitions c. Uncompetitive inhibitions d. All of these

46.The inhibitor binds only to the substrate complex, causing the decrease of Vmax and Km due to the removal of activated
complex.
a. Competitive inhibitions b. Non-competitive inhibitions c. Uncompetitve inhibition d. All of these

47.The inhibitor binds to the enzyme which prevents the enzyme to bind with the substrate thus preventing chemical reaction.
a. Competitive inhibitions b. Non-competitive inhibitions c. Substrate inhibitions d. All of these

48.Which of the following is classified as protease

a. Pepsin b. Papain c. All of these d. None of these

49.The maximum specific growth rate of an organism depends on

a. pH b. temperature c. medium composition d. all of these

50.The monod model predicts that the specific growth rate

a. will increase with the concentration of the growth limiting substrate until it reaches a maximum value
b. will decrease with the concentration of the growth limiting substrate
c. will increase with the concentration of the growth limiting substrate
d. does not depend on growth limiting substrate
\
51.Bacterial growth curve is obtained by plotting
a. number of cells versus time b. number of spores versus time
c.log of number of cells versus time d. log of number of cells survived versus time

52.The Monod Model relates

a. substrate utilized with the biomass consumption b. specific growth rate to the substrate availability
c. yield with the biomass utilization d. the biomass concentration with specific growth rate

53. A higher Ks value of Monod's equation means

a. greater affinities to substrate b. lower affinities to substrate
c. unaffected with the substrate bonding d. lower dissociation constant value

54. Which of the following is true regarding enzyme activators

a. Chemicals that help the enzyme work b. Vitamins are Activators
c. All of these d. None of these

55. Catalyze the formation of double bonds between atoms by adding or subtracting chemical groups.
a. Lyases b. Isomerases c. Ligases d. Transferases

56. Catalyze the rearrangement of chemical groups within the same molecule.
a. Lyases b. Isomerases c. Ligases d. Oxidoreductase

57. Proteolytic enzymes breakdown

a. proteins b.Fats c. Carbohydrates d. all of these

58. Catalyze the formation of a bond between two substrate molecules through the use of an energy source.
a. Lyases b. Isomerases c. Ligases d.Transferases
59. Enzyme controlled reactions proceed almost ________times faster than corresponding non-enzymatic reactions.
a. 1 hundred b. 1 thousand c. 1 million d. 1 billion
60. Which of the following is true regarding the Lock-and-Key hypothesis
a. The substrate and active site match structurally b. The substrate and active site match chemically
c. All of these b. None of these

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61. Which of the following is true regarding the Induced-Fit hypothesis
a. Substrate + enzyme, induces a change in the enzyme’s conformation
b. Active site is moulded to a precise conformation
c. All of these d. None of these
62. Which of the following defines denaturing of enzymes
a. Change in shape b. Change in structure c. All of these d. None of these
63. Binding of the inhibitor causes the substrate binding site to change shape so the chemical reactions is not carried out
a. Competitive inhibitions b. Non-competitive inhibitions c. Uncompetitive inhibitions d. All of these
64. Substances which when added to the enzyme alter the enzyme in a way that it cannot accept the substrate.
a. Competitive inhibitions b. Non-competitive inhibitions c. Uncompetitive inhibitions d. All of these
65. The inhibitor binds only to the substrate complex, causing the decrease of Vmax and Km due to the removal of activated
complex.
a. Competitive inhibitions b. Non-competitive inhibitions c. Uncompetitve inhibition d. All of these
66. The inhibitor binds to the enzyme which prevents the enzyme to bind with the substrate thus preventing chemical reaction.
a. Competitive inhibitions b. Non-competitive inhibitions c. Substrate inhibitions d. All of these
67. Which of the following reversible inhibitors bind to substrate?
a. competitive inhibitors b. noncompetitive inhibitors c. uncompetitive inhibitors d. None of
these
68. Which of the following reversible inhibitors bind to enzyme?
a. competitive inhibitors b. noncompetitive inhibitors c. uncompetitive inhibitors d. None of
these
69. Which of the following reversible inhibitors bind to a site different from the substrate binding site ?
a. competitive inhibitors b. noncompetitive inhibitors c. uncompetitive inhibitors d. None of
these

70. Based on Michaelis – Menten equation, at low substrate concentration, the rate of reaction is
a. First-order with respect to substrate b. Zero-order with respect to substrate
c. Mixed-reaction d. All of these
71. Lyzosyme is naturally found in
a. Egg white b. Tears c. Milk d. All of these
72. A competitive inhibitor is usually
a. Water insoluble b. Water soluble c. All of these d. None of these
73. Linear inhibition is sometimes called______ inhibition.
a. Complete b. Incomplete c. Partial d. Mixed.
74. The type of inhibition based on Michaelis-Menten equation are
a. Competitive b. Uncompetitive c. Non-competitive d. All of these
75. The effect of non-competitive inhibition on Lineweaver-Burk Plot is that
a. It can move the entire curve to the right b. It can change the y-intercept
c. It can change x-intercept d. All of these

76. The rate-determining step of Micahelis Menten kinetics is

a. complex formation step b. the complex dissociation step to produce product
c. the product formation step d. both a and c

77. In competitive inhibition a factor is obtained from the measurement of

a. vMax b. KM c. Y-intercept in Lineweaver-Burk plot d. None of these
78. Given an enzyme with Km is 10 mM and is 20 mM/min. If [S] is 100 mM, which of the following will be true?
a. A ten-fold increase in vMax would increase velocity ten-fold.
b. A ten-fold increase in Km would increase velocity ten-fold.
c. All of these d. None of these
79. The conformational change in an enzyme after the substrate is bound that allow the chemical reaction to proceed can be
explained by
a. Induced fit b. transition c. fit and fine d. Pasteur
80. Which of the following is classified as protease
a. Pepsin b. Papain c. All of these d. None of these
81. Which of the following reversible inhibitors are rarely encountered?
a. competitive inhibitors b. noncompetitive inhibitors c. uncompetitive inhibitors d. None of
these
82. Theory that enzymes are not shaped perfectly to the active sites of their respective enzymes.
a. The Induced Fit Theory b. The Lock and Key Theory c. All of these d. None of these
83. Which of the following is true?
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 a. Inhibitors are chemicals that reduce the rate of enzymatic reactions
b. Usually specific and work at low concentrations
c. Many drugs and poisons are inhibitors of enzymes in the nervous system.
d. All of these

84. In the Lock-and-Key theory, the key is the_______.

a. Substrate b. Enzyme c. All of these d. None of these
85. Which of the following is true regarding the Lock-and-Key Theory?
a. Only the correctly sized substrate fits into the active site of the enzyme.
b. The enzyme and substrate shape do not influence each other
c. The substrate and enzyme are already in a predetermined perfectly complementary shape.
d. All of these
86. Which of the following is true?
a. Denaturing changes the shape.
b. When an enzyme is denatured it is damaged.
c. All of these d. None of these
87. Which of these is reversible inhibitor?
a. Competitive b. Noncompetitive c. All of these d. None of these
88. Which of the following classes of enzyme does catalase belong
a. Oxydoreductases b. Transferases c. Hydrolases d. Lyases

89. Which of the following classes of enzyme does lipase belong

a. Oxydoreductases b. Transferases c. Hydrolases d. Lyases

90. Which of the following classes of enzyme does α-amylase belong

a. Oxydoreductases b. Transferases c. Hydrolases d. Lyases

91. Which of the following classes of enzyme does Pyruvate decarboxylase belong.
a. Oxydoreductases b. Transferases c. Hydrolases d. Lyases

92. Which of the following classes of enzyme whose function is joining of two molecules coupled with cleavage of a
pyrophosphate bond of ATP or similar triphosphate
a. Oxydoreductases b. Transferases c. Hydrolases d. Lyases e. Isomerases f. Ligases

93. The function of enzyme is removal of group, leaving double bond. Addition of group to double bond. Add water,
ammonia or carbon dioxide across double bonds, or remove these elements to produce double bonds
a. Oxydoreductases b. Transferases c. Hydrolases d. Lyases e. Isomerases f. Ligases

94. Hydrolysis of tannery waste for chrome recovery.

a. Alkalase b. Alkylsulfatase c. Chloroperoxidse d. Lysozyme e. Lipase

95. Coenzymes, together with certain inorganic chemicals

a. Conjugated proteins b. Glycoproteins c. enzyme cofactors d. Endo-enzymes

96. The mechanism of enzymatic action involves

a. Slow degradation of the enzyme to form enzyme-substrate complex
b. Temporary union of enzyme with substrate
c. Resistance to deactivation by high temperature
d. Rapid degradation of the enzyme to forma n enzyme-substrate complex
97. The cell walls of many gram positive bacteria can be easily destroyed by this enzyme
a. Lipase b. Lysozyme c. Pectinase d. Peroxidase
98. Which of the following is true.
a. Each enzyme has its own unique protein structure
b. Each enzyme has its own unique protein shape
c. All of these d. None of these
99. An enzyme with a KM value of 0.5mM has a reaction rate of 200 mmol/min at a substrate concentration of 0.5 mmol.
What is the maximum reaction rate that this enzyme can achieve when it is saturated with substrate?
a. 2200 mM/s b. 400 mM/s c. 1100 mM/s d. 800mM/s
v ma S 0 . 5 v ma
v= =200=
k m+S 0 . 5+0 .5
v ma=400 mM / s

100. [S] = 5Km.The ratio of Vo/Vmax when [S] = 5Km?

a. 5/6 b. 6/5 c. 25/36 d. 36/25

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 v max S
v=
k m+S
v
=200=
v 5 5
= =
v max 1+5 6

Note: 99 and 100 5pts each; Disregard # 88-93

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