BIOMOLECULES
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1. The protein part of enzyme is known as
A) Holoenzyme B) Apoenzyme C) Isoenzyme D) All of these
2. The tightly bound non-proteinaceous organic compound in enzyme, is
A) coenzyme B) prosthetic group C) cofactor D) apoenzyme
3. Select the correct statement:
A) Prosthetic groups are inorganic compounds
B) Coenzymes are organic compounds which are tightly bound to the apoenzyme
C) Metal ions cannot act as cofactors
D) NAD+ and NADP+ act as coenzymes
4. Co-enzyme is
A) always a protein. B) often a metal
C) always an inorganic compound D) often a vitamin
5. Which of the following enzymes has organic co-factor?
A) Peroxidase B) Carbonic anhydrase C) Catalase D) Both (1) and (3)
6. Which one is the co-factor of carbonic anhydrase?
A) Fe B) Zn C) Cu D) Mg
7. Which of the following statements is correct?
(1) Biocatalysts accelerate the rate of a given metabolic reaction (2) Biocatalysts are generally protein
(3) Enzyme catalyst differ from inorganic catalyst (4) All of these
8. Which of the following statements are incorrect w.r.t. inorganic catalysts?
(1) They do not occur in living cells (2) They are not specific for any reaction
(3) They get damaged at high temperature (4) They work efficiently at high pressure
9. Enzymes catalyse biochemical reactions by
(1) Lowering the activation energy (2) Increasing the activation energy
(3) Establishing stable bonds with substrate (4) Increasing temperature
10. Read the following :
(a) Low temperature preserves the enzyme (b) Enzyme activity increases above optimum temperature
(c) Enzyme gets denatured at high temperature(d) Competitive inhibitor competes with the product formed
Which of the following statement are true?
(1) (a) & (c) (2) (b) & (d) (3) (c) & (d) (4) (a) & (b)
11. Enzymes catalysing the breakdown of larger molecules into smaller molecules are
(1) Hydrolases (2) Isomerases (3) Ligase (4) Both (1) & (3)
12. Michaelis constant (Km) value of enzyme is substrate concentration at which velocity of reaction is
(1) Vmax (2) One thirdVmax (3) Half Vmax (4) One fifth Vmax
13. The enzyme that catalyses the conversion of glucose-6-phosphate into fructose-6- phosphate is
(1) A ligase (2) An isomerase (3) A lyase (4) A hydrolase
14. Study the following statements :
(a) The substrate binds to the active site of the enzyme
(b) Enzymes isolated from thermophilic organisms get denatured at 50°C
(c) The active site of enzyme breaks the chemical bonds of the product
(d) Prosthetic groups are tightly bound to the apoenzyme
Select the option which includes all correct statements :
(1) (a) & (c) (2) (c) & (d) (3) (b) & (c) (4) (a) & (d)
15. All enzymes are proteins, except
(1) Trypsin (2) Pepsin (3) Steapsin (4) Ribozyme and Ribonuclease-P
16. Electron transferring enzymes belong to
(1) Transferases (2) Oxidoreductases (3) Lyases (4) Isomerases
17. Proteins which catalyse biochemical reactions in the living world are known as
(1) Enzymes (2) Hormones (3) Antibodies (4) Receptor
18. Ribozymes are _______ that behave like enzymes
(1) Proteins (2) Ribonucleic acids (3) Oligosaccharide (4) Simple lipids
19. The most abundant enzyme in the biosphere is
(1) Collagen (2) RuBisCO (3) Trypsin (4) Insulin
20. Organic compounds that are tightly bound to apoenzyme is
(1) Prosthetic group (2) Apoenzyme (3) Metal ions (4) Co-enzymes
21. Many elements are found in living organisms either free or in the form of compounds. One of the
following is not found in living organisms.
1. Silicon 2. Magnesium 3. Iron 4. Sodium
22. The number of ends in a glycogen molecule would be
1. equal to the number of branches plus one 2. Equal to the number of branch points
3. One 4. (Two) - one on the left side and another on the right side
23. What does X and Y represents the structures provided ?
1. A = Adenylic acid , Y=Guanine 2. X – Uridine , Y = Uridylic acid
3. X = Thymidylic acid , Y = Adenine 4. X = Adenylic acid , Y = Adeninie
24. The inhibitor which does not resemble the substrate in structure and binds to the enzyme at the site other
than active site is called
1. Non – competitive inhibitor 2. Activator 3. Substrate analogue 4. Competitive inhibitor
25. Which of the following is not incorrect?
1. Blood glucose concentration in a normal healthy individual is 0.045 – 0.050 mM
2. Living state (of all organisms) is a non – equilibrium steady – state to be able to perform work
3. As living organisms work continuously, they always reach equilibrium
4. Living state is possible in few cases without metabolism
26. Choose the incorrect one:
1. Some nucleic acid can behave as enzymes (e.g., ribozymes)
2. An active site of an enzyme is a crevice or pocket into which the substrate fits
3. Inorganic catalyst work efficiency at low temperatures while enzymes get damaged at low temperatures
4. All are incorrect
27. In the graphical representation of Michaelis – Menten kinetics X represents :
1. Concentration of active mass of the substrate at which the rate of reaction is 1/2 Vmax
2. Concentration of enzyme – substrate complex at which the rate of reaction is 1/2 Vmax
3. Concentration of product at which the rate of reaction is Vmax
4. Concentration is enzyme at which the rate of reaction is 1/2 Vmax
28. Identify X and Y in the newly synthesized polypeptide chain given below :
1. X = -NH2,Y = -COOR 2. X = -NH2,Y = -COOH
3. X = -COOH,Y = -NH2 4. X = -COOR,Y = -NH2
29. Choose the odd one out with respect to polymer :
1. Protein 2. Lipids 3. Polysaccharides 4. Nuclei acids
30. ________ is the most abundant protein in animal world and ______ is the most abundant protein in the
whole biosphere.
1. Insulin , PEP – case 2. Insulin , RuBisCO
3. Collagen , PEP-case 4.Collagen, RuBisCO
31. Read the following statements
(i) During peptide bond formation dehydration occur
(ii) During glycosidic bond formation dehydration occurs
(iii) In a nucleic acid a phosphate moiety links the 3’ carbon of one sugar of one nucleotide to the 5’ carbon
of the sugar of the succeeding nucleotide
(iv) The bond between the phosphate and hydroxyl group of sugar is an ester bond
(v) The backbone of DNA is formed by sugar-phosphate-sugar chain where the nitrogenous bases face
outside
How many of the above statements are correct ?
1. Four 2. Five 3. One 4. Two
32. Identify the amino acids marked as A , B and C :
1. A = Alanine , B = Serine , C = Glycine 2. A = Glycine , B = Serine , C = Arginine
3. A = Glutamic acid , B = Serine , C = Alanine 4. A = Glycine , B = Serine , C = Alanine
33. All enzymes catalysing inter-conversion of optical, geometric or positional isomers are Includes under
1) Lyases 2) Ligases 3) Isomerases 4) Transferases
34. Select the correct statement
1) Prosthetic groups are inorganic compounds
2) Coenzymes are organic compounds which are tightly bound to the apoenzyme
3) Metal ions cannot act as cofactors 4) NAD and NADP act as coenzymes
35. Many coenzymes are derived from
1) Inorganic molecules 2) Metals 3) Hormones 4) Vitamins
36. A metabolic pathway is not:
1) A multistep reaction 2) An uncatalyzed reaction
3) A multienzyme reaction 4) Dependent on pH & temperature
37. What is ture regarding peroxidases and catalases?
1) Both have coenzymes, derivative of vitamin B
2) Both have haem that becomes associated during catalytic reaction
3) They have no cofactor
4) They have haem as prosthetic group
38. The protein part of holoenzyme is known as
1) Holoenzyme 2) Apoenzyme 3) Isoenzyme 4) All of these
39. To catalyze chemical reactions in a cell, enzymes must have:
1) Substrate specificity 2) Active sites 3) Tertiary structure 4) All
40. Find out the correct sequence of following steps of enzyme catalyzed reactions:
(A) Substrate fits into the active site (B) Breaking and making of bonds
(C) Substrate induced change in shape of active site/enzyme
(D) Formation of EP – complex (E) Enzyme and substrate are in close proximity
(F) Release of products and enzyme is freed.
1) A, E, D, B, C, F 2) A, C, E, B, D, F 3) A, C, E, D, B, F 4) A, B, D, E, C, F
41. The enzymes which catalyse the joining of two molecules are:
1) Lyases 2) Ligases 3) Isomerases 4) Transferases
42. Enzymes increase rate of a reaction by:
1) Increasing activation energy 2) Increasing the Km
3) By decreasing the activation energy 4) By decreasing Vmax
43. If a product level is above to substrate level in a graph plotted between progress of an enzyme reaction on
X- axis and potential energy on Y- axis. It indicates:
1) Exothermic reaction 2) Endothermic reaction
3) Spontaneous reaction 4) more than one option is correct
44. Which of the following is a correct expression of an enzyme catalyzed reaction?
1) E + S ↔ES → EP → E + P 2) E + S→ ES → EP ↔ E + P
3) E + S → ES ↔ EP → E + P 4) E + S↔ EP→ E + P
45. Activation energy is calculated from:
1) Energy difference between substrate and product
2) Energy difference between substrate and it’s transition state
3) Difference in rate of reaction between two enzymes
4) Difference in activation energy between two enzymes
46. The most important property of an enzyme is its
1) Composition 2) Thermal denaturation 3) Specificity 4) Solubility
47. Mark the correct statement
1) NAD & NADP are coenzymes that are derivative of vitamin B
2) Catalytic activity is lost when the cofactor is removed from enzyme
3) In carboxypeptidases the metallic ions are of zinc
4) All of these
48. At optimal pH and temperature enzyme activity is:
1) Minimum 2) Maximum 3) Average 4) Zero
49. Denaturation of enzymes is caused by:
1) Extreme Ph 2) High temperature 3) Low temperature 4) Both 1 and 2
50. Which of the following structure is not affected by denaturation of enzymes?
1) Primary 2) Secondary 3) Tertiary & Quaternary 4) Both 2 & 3
51. Non-protein part of holoenzyme is known as
1) Holoenzyme 2) Apoenzyme 3) Coenzyme 4) All of these
52. The factors affecting enzyme activity are:
1) pH & temperature 2) Concentration of substrate
3) Concentration of enzyme 4) more than one option is correct
53. When cofactor is combined with apoenzyme, it is called
1) Cofactor 2) Holoenzyme 3) Substrate enzyme complex 4) Vitamin A
54. Carbonic anhydrase is a:
1) Homopolymer of amino acids 2) Heteropolymer of amino acids
3) Homopolymer of nucleotides 4) Heteropolymer of nucleotides
55. The effect of pH and temperature on enzyme activity gives rise to:
1) A parabolic curve 2) A hyperbolic curve 3) A bell- shaped curve 4) A standard curve
56. The C-C, C-X and P-N bonds are degraded by:
1) Oxido-reductases 2) Ligases 3) Hydrolases 4) Lyases
57. Vmax of an enzymatic reaction indicates:
1) Enzymes are denatured 2) There are free enzymes to bind with substrate
3) Limiting of the substrate 4) There are no free enzymes to bind with substrate
58. Enzyme activity becomes maximum and remains constant in a reaction after reaching to Vmax. How the
enzyme activity is increased to a higher value again?
1) By increasing the number of substrate molecules 2) By decreasing the number of substrate molecules
3) By increasing the number of enzyme molecules 4) By decreasing the number of enzyme molecules
59. In a graph of substrate concentration versus enzyme activity, Km value is calculated from:
1) Concentration of substrate corresponding to Vmax/2
2) Concentration of substrate corresponding to Vmax
3) Concentration of enzyme corresponding to Vmax/2
4) Concentration of enzyme corresponding to Vmax
60. The catalytic efficiency of two enzymes can be compared by:
1) Vmax 2) Km 3) Activation energy 4) Transition state
61. The enzymes which link C-O, C-S, C-N and P-O bonds belong to:
1) Class- 1 2) Class- 2 3) Class- 5 4) Class- 6
62. In enzyme catalyzed reactions, the transition state is:
(1) The most stable (2) Possesses the highest energy (3) The product (4) Both 2 and 3
63. In a competitive enzyme inhibition, inhibitor binds with:
1) Active site 2) Inhibitor site 3) Allosteric site 4) any where to the enzyme
64. Bacterial pathogens are controlled by:
1) Competitive enzyme inhibition 2) Non-competitive enzyme inhibition
3) Uncompetitive enzyme inhibition 4) Feedback inhibition
65. The number of classes and sub-classes present, respectively in the classification of enzymes:
1) 6 & 10- 15 2) 6 & 4- 13 3) 5 & 10- 14 4) 5 & 4- 13
66. Enzymes which catalyse group transfer [other than hydrogen] reactions belong to:
1) Class- 6 2) Class- 4 3) Class– 2 4) Class- 1
67. Enzymes which degrade peptide bonds in proteins are:
1) Oxido-reductases 2) Hydrolases 3) Lyases 4) Ligases
68. Enzymes which catalyse elimination reactions, leaving double bonds[c=c] are called:
1) Lyases 2) Ligases 3) Isomerases 4) Transferases
69. Metal ions cofactors for their activity form
1) coordination bonds with side chains at the active site
2) one or more co-ordination bonds with the substrate
3) phosphodiester bonds with side chains at the active site 4) 1 & 2
70. In the absence of Zn, carboxipeptidase is called
1) Holoenzyme 2) Cofactor 3) Apoenzyme 4) Coenzyme
71. Which of the following describes the given graph correctly?
1) Endothermic reaction with energy A in presence of enzyme and B in absence of enzyme
2) Exothermic reaction with energy A in presence of enzyme and B in absence of enzyme
3) Endothermic reaction with energy A in absence of enzyme and B in presence of enzyme
4) Exothermic reaction with energy A in absence of enzyme and B in presence of enzyme
72. Which one of the following statements is incorrect?
1) The presence of the competitive inhibitor decreases the Km of the enzyme for the substrate
2) A competitive inhibitor reacts reversibly with the enzyme to form an enzyme-inhibitor complex
3) In competitive inhibition, the inhibitor molecule is not chemically changed by the enzyme
4) The competitive inhibitor does not affect the rate of breakdown of the enzyme-substrate complex
73. Substituted methanes are
1) Amino acids 2) Proteins 3) Nucleic acid 4) Polysaccharides
74. Number of carbon atoms in arachidonic acid including carboxyl carbon is
1) 16 2) 19 3) 20 4) 15
75. The glycerol is
1) Monohydroxy propane 2) Dihydroxy propane
3) Trihydroxy propane 4) Tetrahydroxy propane
76. Cl3CCOOH is chemical formula for
1) Palmitic acid 2) Trichloro acetic acid 3) Stearic acid 4) Acetic acid
77. The pair of elements are relatively abundant in living organisms than in earth’s crust
1)Carbon, Sodium 2) Oxygen, Silicon 3) Carbon, Hydrogen 4) Carbon, Magnesium
78. While carrying out analysis for inorganic compounds present in a given sample
1) All the carbon compound are reduced
2) All the inorganic compounds are oxidised to gaseous form
3) Ash obtained on burning of sample contains inorganic compounds and water vapour
4)All the carbon compounds are oxidised to gaseous form and are removed
79. Study the following diagrams
Which of the following statements is incorrect regarding above amino acids?
1) They are α -amino acids
2) They have equal number of amino and carboxylic groups
3) Alanine has the simplest structure out of the three amino acids
4)‘R’ group in serine is hydroxyl methyl group while in alanine is methyl group
80. Ash analysis gives
1) Total water in a sample 2) Total organic matter in a sample
3) Total macromolecular weight 4) Inorganic compound except water
81. Structure of amino acids may changes due to
1) Ionizable nature 2) PH of solution 3) Number of ‘R’ functional groups 4) All the given
82. Number of carbon atoms presents in ‘R’ functional group of simplest amino acid
1) Zero 2) One 3) Two 4) Sixteen
83. Match the following lists
List A List B
A. Neutral aminoacid P. Lysine
B. Acidic aminoacid Q. Tyrosine
C. Aromatic amino acid R. Valine
D. Basic amino acid S. Phenylalanine
T. Glutamic acid
ABCD
1) R S P Q 2) S T R P 3) P R T S 4) R T Q P
84. Nuleoside becomes Nucleotide when
1) Dehydrated 2) Phosphate group is esterified 3) Dephosphorylated 4) Sulphate is esterified
85. Which of the following is not a nitrogen base
1) Adenine 2) Guanine 3) Cytosine 4) Thiamine
86. The elements found in all proteinaceous aminoacids are
1) C, H, O, Si 2) C, H, O, N 3) C, N, O, K 4) C, H, O, S
87. Which of the following is a lectin?
1) Cholesterol 2) Concanavalin- A 3) GLUT-4 4) Cellulose
88. Cellulose is polymer of.
1) Ribose 2) Glucose 3) Fructose 4) Xylulose
89. Find aromatic amino acid form the below
1) Glutamic acid 2) Lysine 3) Arginine 4) Tyrosine
90. Quarternary structure is present in ______
1) haemoglobin 2) histone 3) globulin 4) elastin
91. The bond between phosphate and hydroxyl group of sugar in nucleic acid is _______
1) glycosidic bond 2) peptide bond 3) ester bond 4) none of these
92. Ribozyme is a/an
1) enzyme whose cofactor is RNA 2) RNA with enzyme activity
3) enzyme by which RNA is formed 4) conjugated protein having ribose sugar
93. Which one of the following statement is correct, with reference to enzymes?
1) Holoenzyme = Apoenzyme + Co-factor 2) Coenzyme = Apoenzyme + Holoenzyme
3) Holoenzyme = Coenzyme + Co-factor 4) Apoenzyme = Holoenzyme + Coenzyme
94. Inulin is a polymer of
1) glucose 2) galactose 3) fructose 4) arabinose
95. 5 – methyl uracil
(1) Is present in both DNA and RNA (2) Is present in RNA only
(3) Is a chemical name for thymine (4) Is a type of purine
96. The nitrogenous bases are linked to sugar moiety and project facing inside from the backbone more or
less at an angle of (ds DNA)
1) 360 2) 180 3) 90 4) 45
97. Ribonucleotides are observed in all except
1) Codons 2) Anticodons 3) Ribozyme 4) PBR 322
98. The bonds present in Adenylic acid are/is
1) N-glycosidic bond, Phosphoester bond 2) Phosphodiester bond, N-glycosidic bond
3) N-Glycosidic bond only 4) Phosphodiester bond, Glycosidic bond
99. In competitive inhibition
1) Inhibitor resembles the substrate in molecular structure
2) There is competition between substrates and inhibitors to occupy active site
3) Binding of the inhibitors to active site declines the enzyme action
4) All of these
100. A typical fat molecule is made up of
1) one glycerol and one fatty acid molecule 2) three glycerol and three fatty acid molecules
3) three glycerol molecules and one fatty acid molecule 4) one glycerol and three fatty acid molecules.