Hello friends in today's article we see the MCQ's of Enzyme In biotechnology. In MCQ's of Enzyme include there metabolism activity MCQ's in biotechnology. So let's begin
Enyzmes MCQ’s In Biotechnology
1. The compound which has the lowestdensity is
(A) Chylomicron
(B)
β-Lipoprotein
(C)
α-Lipoprotein
(D) pre
β-Lipoprotein
2. Non steroidal anti inflammatory drugs, such as
aspirin act by inhibiting the activity of the enzyme:
(A) Lipoxygenase
(B) Cyclooxygenase
(C)
Phospholipase A2
(D) Lipoprotein
lipase
3. From arachidonate, synthesis of prostaglandins is
catalysed by
(A) Cyclooxygenase
(B)
Lipoxygenase
(C) Thromboxane
synthase
(D) Isomerase
4. A Holoenzyme is
(A) Functional
unit
(B) Apo enzyme
(C) Coenzyme
(D) All of these
5. Gaucher’s disease is due to the deficiency of the
enzyme:
(A)
α-Fucosidase
(B)
β-Galactosidase
(C) β-Glucosidase
(D)
Sphingomyelinase
6. Neimann-Pick disease is due to the deficiency of
the enzyme:
(A)
Hexosaminidase A and B
(B) Ceramidase
(C) Ceramide
lactosidase
(D) Sphingomyelinase
7. Krabbe’s disease is due to the deficiency of the
enzyme:
(A) Ceramide
lactosidase
(B) Ceramidase
(C) β-Galactosidase
(D) GM1
β-Galactosidase
8. Fabry’s disease is due to the deficiency of the
enzyme:
(A) Ceramide trihexosidase
(B)
Galactocerebrosidase
(C) Phytanic
acid oxidase
(D)
Sphingomyelinase
9. Farber’s disease is due to the deficiency of the
enzyme:
(A)
α-Galactosidase
(B) Ceramidase
(C)
β-Glucocerebrosidase
(D)
Arylsulphatase A.
10. A synthetic nucleotide analogue, used in organ
transplantation as a suppressor of immunologic rejection of grafts is
(A)
Theophylline
(B) Cytarabine
(C) 4-Hydroxypyrazolopyrimidine
(D)
6-Mercaptopurine
11. Example of an extracellular enzyme is
(A) Lactate
dehydrogenase
(B) Cytochrome
oxidase
(C) Pancreatic lipase
(D) Hexokinase
12. Enzymes, which are produced in inactive form in
the living cells, are called
(A) Papain
(B) Lysozymes
(C) Apoenzymes
(D) Proenzymes
13. An example of ligases is
(A) Succinate thiokinase
(B) Alanine racemase
(C) Fumarase
(D) Aldolase
14 An example of lyases is
(A) Glutamine
synthetase
(B) Fumarase
(C)
Cholinesterase
(D) Amylase
15. Activation or inactivation of certain key regulatory
enzymes is accomplished by covalent modification of the amino acid:
(A) Tyrosine
(B) Phenylalanine
(C) Lysine
(D) Serine
16. The enzyme which can add water to a carbon-carbon
double bond or remove water to create a double bond without breaking the bond
is
(A) Hydratase
(B) Hydroxylase
(C) Hydrolase
(D) Esterase
17. Fischer’s ‘lock and key’ model of the enzyme
action implies that
(A) The active
site is complementary in shape to that of substance only after interaction.
(B) The active site is complementary in shape to
that of substance
(C) Substrates
change conformation prior to active site interaction
(D) The active
site is flexible and adjusts to substrate
18. From the Lineweaver-Burk plot of Michaelis-Menten
equation, Km and Vmax can be determined when V is the reaction velocity at
substrate concentration S, the X-axis experimental data are expressed as
(A) 1/V
(B) V
(C) 1/S
(D) S
19. A sigmoidal plot of substrate concentration ([S])
verses reaction velocity (V) may indicate
(A)
Michaelis-Menten kinetics
(B) Co-operative binding
(C) Competitive
inhibition
(D) Non-competitive
inhibition
20. The Km of the enzyme giving the kinetic
data as below is
(A) -0.50
(B) -0.25
(C) +0.25
(D) +0.33
21. The kinetic effect of purely competitive inhibitor
of an enzyme
(A) Increases Km without affecting Vmax
(B) Decreases Km without
affecting Vmax
(C) Increases Vmax
without affecting Km
(D) Decreases Vmax
without affecting Km
22. If curve X in the graph (below) represents no
inhibition for the reaction of the enzyme with its substrates, the curve
representing the competitive inhibition, of the same reaction is
(A) A
(B) B
(C) C
(D) D
23. An inducer is absent in the type of enzyme:
(A) Allosteric
enzyme
(B) Constitutive enzyme
(C)
Co-operative enzyme
(D) Isoenzymic
enzyme
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24. A demonstrable inducer is absent in
(A) Allosteric
enzyme
(B) Constitutive enzyme
(C) Inhibited
enzyme
(D)
Co-operative enzyme
25. In reversible non-competitive enzyme activity
inhibition
(A) Vmax
is increased
(B) Km is increased
(C) Km
is decreased
(D) Concentration of active enzyme is reduced
26. In reversible non-competitive enzyme activity
inhibition
(A) Inhibitor
bears structural resemblance to substrate
(B) Inhibitor lowers the maximum velocity attainable
with a given amount of enzyme
(C) Km
is increased
(D) Km
is decreased
27. In competitive enzyme activity inhibition
(A) The structure of inhibitor generally
resembles that of the substrate
(B) Inhibitor
decreases apparent Km
(C) Km
remains unaffective
(D) Inhibitor
decreases Vmax without affecting Km
28. In enzyme kinetics Vmax reflects
(A) The amount of an active enzyme
(B) Substrate
concentration
(C) Half the
substrate concentration
(D) Enzyme
substrate complex
29. In enzyme kinetics Km implies
(A) The substrate concentration that gives one
half Vmax
(B) The dissocation
constant for the enzyme substrate comples
(C)
Concentration of enzyme
(D) Half of the
substrate concentration required to
achieve Vmax
30. In competitive enzyme activity inhibition
(A) Apparent Km
is decreased
(B) Apparent Km is increased
(C) Vmax
is increased
(D) Vmax
is decreased
31. In non competitive enzyme activity inhibition,
inhibitor
(A) Increases Km
(B) Decreases Km
(C) Does not effect Km
(D) Increases Km
32. An enzyme catalyzing oxidoreduction, using oxygen
as hydrogen acceptor is
(A) Cytochrome oxidase
(B) Lactate dehydrogenase
(C) Malate
dehydrogenase
(D) Succinate
dehydrogenase
33. The enzyme using some other substance, not oxygen
as hydrogen acceptor is
(A) Tyrosinase
(B) Succinate dehydrogenase
(C) Uricase
(D) Cytochrome
oxidase
34. An enzyme which uses hydrogen acceptor as
substrate is
(A) Xanthine
oxidase
(B) Aldehyde oxidase
(C) Catalase
(D) Tryptophan
oxygenase
35. Enzyme involved in joining together two substrates
is
(A) Glutamine synthetase
(B) Aldolase
(C) Gunaine
deaminase
(D) Arginase
36. The pH optima of most of the enzymes is
(A) Between 2
and 4
(B) Between 5 and 9
(C) Between 8
and 12
(D) Above 12
37. Coenzymes are
(A) Heat stable, dialyzable, non protein organic
molecules
(B) Soluble,
colloidal, protein molecules
(C) Structural
analogue of enzymes
(D) Different
forms of enzymes
38. An example of hydrogen transferring coenzyme is
(A) CoA
(B) NAD+
(C) Biotin
(D) TPP
39. An example of group transferring coenzyme is
(A) NAD+
(B) NADP+
(C) FAD
(D) CoA
40. Cocarboxylase is
(A) Thiamine
pyrophosphate
(B) Pyridoxal
phosphate
(C) Biotin
(D) CoA
41. A coenzyme containing non aromatic hetero ring is
(A) ATP
(B) NAD
(C) FMN
(D) Biotin
42. A coenzyme containing aromatic hetero ring is
(A) TPP
(B) Lipoic acid
(C) Coenzyme Q
(D) Biotin
43. Isoenzymes are
(A) Chemically, immunologically and
electrophoretically different forms of an enzyme
(B) Different
forms of an enzyme similar in all properties
(C) Catalysing
different reactions
(D) Having the
same quaternary structures like the enzymes
44. Isoenzymes can be characterized by
(A) Proteins
lacking enzymatic activity that are necessary for the activation of enzymes
(B) Proteolytic enzymes activated by hydrolysis
(C) Enzymes
with identical primary structure
(D) Similar
enzymes that catalyse different reaction
45. The isoenzymes of LDH
(A) Differ only
in a single amino acid
(B) Differ in
catalytic activity
(C) Exist in 5 forms depending on M and H monomer
contents
(D) Occur as
monomers
46. The normal value of CPK in serum varies between
(A) 4-60 IU/L
(B) 60-250
IU/L
(C) 4-17
IU/L
(D) >
350 IU/L
47. Factors affecting enzyme activity:
(A)
Concentration
(B) pH
(C) Temperature
(D) All of these
48. The normal serum GOT activity ranges from
(A) 3.0-15.0
IU/L
(B) 4.0-17.0 IU/L
(C) 4.0-60.0
IU/L
(D) 0.9-4.0
IU/L
49. The normal GPT activity ranges from
(A) 60.0-250.0
IU/L
(B) 4.0-17.0
IU/L
(C) 3.0-15.0 IU/L
(D) 0.1-14.0
IU/L
50. The normal serum acid phosphatise activity ranges
from
(A) 5.0-13.0 KA units/100 ml
(B) 1.0-5.0 KA
units/100 ml
(C) 13.0-18.0
KA units/100 ml
(D) 0.2-0.8
KA units/100 ml
51. The normal serum alkaline phosphatise activity
ranges from
(A) 1.0-5.0
KA units/100 ml
(B) 5.0-13.0 KA units/100 ml
(C) 0.8-2.3
KA units/100 ml
(D) 13.0-21.0
KA units/100 ml
52. In early stages of myocardial ischemia the most sensitive
indicator is the measurement of the activity of
(A) CPK
(B) SGPT
(C) SGOT
(D) LDH
53. Serum acid phosphatase level increases in
(A) Metastatic carcinoma of prostate
(B) Myocardial
infarction
(C) Wilson’s
disease
(D) Liver
diseases
54. Serum alkaline phosphatase level increases in
(A)
Hypothyroidism
(B) Carcinoma
of prostate
(C) Hyperparathyroidism
(D) Myocardial
ischemia
55. Serum lipase level increases in
(A) Paget’s
disease
(B) Gaucher’s
disease
(C) Acute pancreatitis
(D) Diabetes
mellitus
56. Serum ferroxidase level decreases in
(A) Gaucher’s
disease
(B) Cirrhosis
of liver
(C) Acute
pancreatitis
(D) Wilson’s disease
57. The isoenzymes LDH5 is elevated in
(A) Myocardial
infarction
(B) Peptic
ulcer
(C) Liver disease
(D) Infectious
diseases
58. On the third day of onset of acute myocardial
infarction the enzyme elevated is
(A) Serum AST
(B) Serum CK
(C) Serum LDH
(D) Serum ALT
59. LDH1 and LDH2 are elevated
in
(A) Myocardial infarction
(B) Liver
disease
(C) Kidney
disease
(D) Brain
disease
60. The CK isoenzymes present in cardiac muscle is
(A) BB and MB
(B) MM and MB
(C) BB only
(D) MB only
61. In acute pancreatitis, the enzyme raised in first
five days is
(A) Serum amylase
(B) Serum
lactic dehydrogenase
(C) Urinary
lipase
(D) Urinary
amylase
62. Acute pancreatitis is characterised by
(A) Lack of
synthesis of zymogen enzymes
(B) Continuous release of zymogen
enzymes into the gut
(C) Premature activation of zymogen enzymes
(D)
Inactivation of zymogen enzymes
63. An example of functional plasma enzyme is
(A) Lipoprotein lipase
(B) Amylase
(C)
Aminotransferase
(D) Lactate
dehydrogenase
64. A non-functional plasma enzyme is
(A)
Psudocholinesterase
(B) Lipoprotein
lipase
(C) Proenzyme
of blood coagulation
(D) Lipase
65. The pH optima for salivary analyse is
(A) 6.6-6.8
(B) 2.0-7.5
(C) 7.9
(D) 8.6
66. The pH optima for pancreatic analyse is
(A) 4.0
(B) 7.1
(C) 7.9
(D) 8.6
67. The pH optima for sucrase is
(A) 5.0-7.0
(B) 5.8-6.2
(C) 5.4-6.0
(D) 8.6
68. The pH optima for maltase is
(A) 1.0-2.0
(B) 5.2-6.0
(C) 5.8-6.2
(D) 5.4-6.0
69. The pH optima for lactase is
(A) 1.0-2.0
(B) 5.4-6.0
(C) 5.0-7.0
(D) 5.8-6.2
70. The substrate for amylase is
(A) Cane sugar
(B) Starch
(C) Lactose
(D) Ribose
71. The ion which activates salivary amylase activity is
(A) Chloride
(B) Bicarbonate
(C) Sodium
(D) Potassium
72. The pancreatic amylase activity is increased in
the presence of
(A)
Hydrochloric acid
(B) Bile salts
(C) Thiocyanate
ions
(D) Calcium
ions
73. A carbohydrate which can not be digested in human
gut is
(A) Cellulose
(B) Starch
(C) Glycogen
(D) Maltose
74. The sugar absorbed by facilitated diffusion and
requiring Na independent transporter is
(A) Glucose
(B) Fructose
(C) Galactose
(D) Ribose
75. In the intestine the rate of absorption is highest
for
(A) Glucose and galactose
(B) Fructose
and mannose
(C) Fructose
and pentose
(D) Mannose and
pentose
76. Glucose absorption is promoted by
(A) Vitamin A
(B) Thiamin
(C) Vitamin C
(D) Vitamin K
77. The harmone acting directly on intestinal mucosa
and stimulating glucose absorption is
(A) Insulin
(B) Glucagon
(C) Thyroxine
(D) Vasopressin
78. Given that the standard free energy change (∆G°)
for the hydrolysis of ATP is-7.3 K cal/mol and that for the hydrolysis of
Glucose 6-phosphate is -3.3 Kcal/mol, the ∆G° for the phosphorylation of
glucose is Glucose + ATP → Glucose 6-Phosphate + ADP.
(A) -10.6
Kcal/mol
(B) -7.3
Kcal/mol
(C) -4.0 Kcal/mol
(D) +4.0
Kcal/mol
79. At low blood glucose concentration, brain but not
liver will take up glucose. It is due
to the
(A) Low Km of hexokinase
(B) Low Km of glucokinase
(C) Specificity
of glucokinase
(D) Blood brain
barrier
80. In the reaction below, Nu TP stands for NuTP +
glucose → Glucose 6-Phosphate+ NuDP.
(A) ATP
(B) CTP
(C) GTP
(D) UTP
81. In the figures shown below, fructose
1,6-biphosphate is located at point:
(A) A
(B) B
(C) C
(D) D
82. The enzyme of the glycolic pathway, sensitive to
inhibiton by fluoride ions is
(A) Hexokinase
(B) Aldolase
(C) Enolase
(D) Pyruvate
kinase
83. In glycolytic pathway, iodacetate inhibits the
activity of the enzyme:
(A)
Phosphotriose isomerase
(B) Glyceraldehyde-3-phosphate dehydrogenase
(C) Pyruvate
kinase
(D)
Phosphofructokinase
84. In the glycolytic pathway, enolpyruvate is
converted to ketopyruvate by
(A) Pyruvate
kinase
(B) Phosphoenolpyruvate
(C) Pyruvate
dehydrogenase
(D)
Spontaneously
85. In erythrocytes, 2, 3-biphosphoglycerate is
derived from the intermediate:
(A)
Glyeraldehyde-3-phosphate
(B) 1,
3-Biphosphoglycerate
(C) 3-Phosphoglycerate
(D) 2-Phosphoglycerate
86. 2, 3-Biphosphoglycerate in high concentrations,
combines with hemoglobin,causes
(A)
Displacement of the oxyhemoglobin dissociation curve to the left
(B) Displacement of the oxyhemoglobin
dissociation curve to the right
(C) No change
in oxy hemoglobin dissociation curve
(D) Increased
affinity for oxygen
87. Erythrocytes under normal conditions and microorganisms
under anaerobic conditions may accumulate
(A) NADPH
(B) Pyruvate
(C)
Phosphoenolpyruvate
(D) Lactate
88. Enzymes leading to the high energy phosphorylation
of substrates during glycolysis include which of the following?
(A)
Phosphoglycerate kinase (B)
Enolase
(C) Pyruvate
Kinase
(D) Glyceraldehyde-3-phosphate dehydrogenase
89. Lineweaver - Burk double reciprocal plot is
related to
(A) Substrate
concentration
(B) Enzyme
activity
(C) Temperature
(D) Both (A) and (B)
90. Phosphofructokinase key enzyme in glycolysis is
inhibited by
(A) Citrate and ATP
(B) AMP
(C) ADP
(D) TMP
91. One of the enzymes regulating glycolysis is
(A) Phosphofructokinase
(B)
Glyceraldehyde-3-phosphate dehydrogenase
(C)
Phosphotriose isomerase
(D)
Phosphohexose isomerase
92. Hexokinase is inhibited in an allosteric manner by
(A) Glucose-6-Phosphate
(B)
Glucose-1-Phosphate
(C)
Fructose-6-phosphate
(D) Fructose-1,
6-biphosphate
93. A reaction which may be considered an isomerisation
is
(A) Glucose 6-Phosphate fructose 6 phosphate
(B) 3-Phosphoglycerate 2-phosphoglycerate
(C) 2-phosphoglycerate phosphoenolpyruvate
(D) Pyruvate Lactate
94. The net number of ATP formed per mole of glucose
in anaerobic glycolysis is
(A) 1
(B) 2
(C) 6
(D) 8
95. Pyruvate dehydrogenase a multienzyme complex is
required for the production of
(A) Acetyl-CoA
(B) Lactate
(C)
Phosphoenolpyruvate
(D)
Enolpyruvate
96. Dietary deficiency of thiamin inhibits the activity
of the enzyme:
(A) Pyruvate
kinase
(B) Pyruvate dehydrogenase
(C)
Phosphofructokinase
(D) Enolase
97. Pyruvate dehydrogenase activity is inhibited by
(A) Mercury
(B) Zinc
(C) Calcium
(D) Sodium
98. In the normal resting state of humans, most of the
blood glucose burned as fuel is consumed by
(A) Liver
(B) Adipose
tissue
(C) Muscle
(D) Brain
99. All the enzymes of glycolysis pathway are found in
(A) Extramitochondrial soluble fraction of the
cell
(B)
Mitochondria
(C) Nucle
(D) Endoplasmic
reticulum
100. Most major metabolic pathways are considered
mainly either anabolic or catabolic. Which of the following pathway is most
correctly considered to be amphibolic?
(A) Citric acid cycle
(B)
Gluconeogenesis
(C) Lipolysis
(D) Glycolysis
101. The enzymes of the citric acid cycle are located
in
(A) Mitochondrial matrix
(B)
Extramitochondrial soluble fraction of the cell
(C) Nucleus
(D) Endoplasmic
reticulum
102. The initial step of the citric acid cycle is
(A) Conversion
of pyruvate to acetyl-CoA
(B) Condensation of acetyl-CoA with oxaloacetate
(C) Conversion
of citrate to isocitrate
(D) Formation
of α -ketoglutarate catalysed by isocitrate dehydrogenase
103. The substance which may be considered to play a
catalytic role in citric acid cycle is
(A) Oxaloacetate
(B) Isocitrate
(C) Malate
(D) Fumarate
104. An enzyme of the citric acid cycle also found
outside the mitochondria is
(A) Isocitrate
dehydrogenase
(B) Citrate
synthetase
(C) α-Ketoglutarate dehydrogenase
(D) Malate
dehydrogenase
105. The reaction catalysed by α-ketoglutarate
dehydrogenase in the citric acid cycle requires
(A) NAD
(B) NADP
(C) ADP
(D) ATP
106. If all the enzymes, intermediates and cofactors
of the citric acid cycle as well as an excess of the starting substrate
acetylCoA are present and functional in an organelle free solution at the
appropriate pH, which of the following factors of the citric acid cycle would
prove to be rate limiting ?
(A) Molecular
oxygen
(B) Half life of enzyme
(C) Turnover of
intermediates
(D) Reduction of cofactors
107. In TCA cycle, oxalosuccinate is converted to
α-ketoglutarate by the enzyme:
(A) Fumarase
(B) Isocitrate dehydrogenase
(C) Aconitase
(D) Succinase
108. The enzyme -ketoglutarate dehydrogenase in the
citric acid cycle requires
(A) Lipoate
(B) Folate
(C) Pyridoxine
(D) Inositol
109. The example of generation of a high energy
phosphate at the substrate level in the citric acid cycle is the reaction:
(A) Isocitrate α-Ketoglutarate
(B) Succinate α-fumarate
(C) Malate α-oxaloacetate
(D) Succinyl CoA α-Succinate
110. Fluoroacetate inhibits the reaction of citric
acid cycle:
(A) Isocitrate α-Ketoglutarate
(B) Fumarate α-Malate
(C) Citrate α-cis-aconitate
(D) Succinate α-fumarate
111. Formation of succinyl-CoA from α-Ketoglutarate is
inhibited by
(A)
Fluoroacetate
(B) Arsenite
(C) Fluoride
(D) Iodoacetate
112. The number of ATP molecules generated for each
turn of the citric acid cycle is
(A) 8
(B) 12
(C) 24
(D) 38
113. Oxidation of one molecule of glucose yields
(A) 12 ATP
(B) 24 ATP
(C) 38 ATP
(D) 38 ATP
114. Which of the following intermediates of metabolism
can be both a precursor and a product of glucose?
(A) Lactate
(B) Pyruvate
(C) Alanine
(D) Acetyl-CoA
115. Mitochondrial membrane is freely preamble to
(A) Pyruvate
(B) Malate
(C)
Oxaloacetate
(D) Fumarate
116. The reaction of Kreb’s cycle which does not
require cofactor of vitamin B group is
(A) Citrate isocitrate
(B) α
-Ketoglutarate succinate
(C) Malate oxaloacetate
(D) Succinate fumarate
117. The coenzyme not involved in the formation of
acetyl-CoA from pyruvate is
(A) TPP
(B) Biotin
(C) NAD
(D) FAD
118. A carrier molecule in the citric acid cycle is
(A) Acetyl-CoA
(B) Citrate
(C) Oxaloacetate
(D) Malate
119. A specific inhibitor for succinate dehydrogenase
is
(A) Arsenine
(B) Arsenite
(C) Citrate
(D) Fluoride
120. The rate of citric acid cycle is controlled by
the allosteric enzyme:
(A) Aconitase
(B) Fumarase
(C) Fumarase
(D) Malate
dehydrogenase
121. In the erythrocytes, the net production of ATP
molecules by the Rapport-Leubering pathway is
(A) 0
(B) 2
(C) 4
(D) 8
122. The ratio that most closely approximates the
number of net molecules of ATP formed per mole of glucose utilized under
aerobic conditions to the net number formed under anaerobic conditions is
(A) 4:1
(B) 13:1
(C) 18:1
(D) 24:1
123. The pathway of glycogen biosynthesis involves a
special nucleotide of glucose. In the reaction below, NuDP stands for NuDP
Glucose + glycogenn → NuDP + glycogenn+1
(A) ADP
(B) GDP
(C) UDP
(D) CDP
124. Glucose 6-phosphate is converted to glucose
1-phosphate in a reaction catalysed by the enzyme phosphoglucomutase, which is
(A)
Phosphorylated
(B) Dephosphorylated
(C)
Phosphorylated-dephosphorylated
(D)
Phosphorylated-dephosphorylatedrephosphorylated
125. The glycogen content of the liver is upto
(A) 6%
(B) 8%
(C) 10%
(D) 12%
126. In glycogenesis a branch point in the molecule is
established by the enzyme
(A) Amylo[1→ 4][1→ 6] transglucosidase
(B) α [1→ 4] α
[1→ 4] Glucan transferase
(C) Amylo [1→
6] glucosidase
(D) Glycogen
synthase
127. In glycogenolysis, the enzyme which transfers a
trisaccharide unit from one branch to the other exposing 1→ 6 branch point is
(A) Phosphorylase
(B) α-[1→ 4]→ α-[1→ 4]→ Glucan transferase
(C) Amylo [1→
6] glucosidase
(D) Amylo[1→
4]→ [1→ 6] transglucosidase
128. In the synthesis of glycogen from glucose the
reversible step is
(A) Glucose →
glucose 6-phosphate
(B) Glucose 6-phosphate → glucose 1-phosphate
(C) Glucose
1-phosphate → UDP glucose
(D) UDP glucose
→ glycogen
129. The enzyme glucose-6-phosphatase which catalyses
the conversion of glucose 6-phosphate to glucose is not found in
(A) Liver
(B) Muscle
(C) Intestine
(D) Kidney
130. Allosteric activator of glycogen synthase is
(A) Glucose
(B) Glucose-6-Phosphate
(C) UTP
(D)
Glucose-1-phosphate
131. Action of glycogen synthase is inhibited by
(A) Insulin
(B) Glucose
(C) Mg2+
(D) Cyclic AMP
132. The hormone activating the glycogen synthase
activity is
(A) Insulin
(B) Glucagon
(C) Epinephrine
(D) ACTH
133. Characteristic features of active site are
(A) Flexible in
nature
(B) Site of
binding
(C) Acidic
(D) Both (A) and (B)
134. Von Gierke’s disease is characterized by the
deficiency of
(A) Glucose-6-phosphatase
(B) α -1 → 4
Glucosidase
(C) 1→ 6
Glucosidase
(D) Liver
phosphorylase
135. Cori disease (Limit dextrinosis) is caused due to
absence of
(A) Branching
enzyme
(B) Debranching enzyme
(C) Glycogen
synthase
(D)
Phosphorylase
136. Mc Ardle’s syndrome is characterized by the
absence of
(A) Liver
phosphorylase
(B) Muscle phosphorylase
(C) Branching
enzyme
(D) Debranching
enzyme
137. Pompe’s disease is caused due to deficiency of
(A) Lysosomal α-1→4 and 1→6-glucosidase
(B)
Glucose-6-phosphatase
(C) Glycogen
synthase
(D)
Phosphofructokinase
138. Amylopectinosis is caused due to absence of
(A) Debranching
enzyme
(B) Branching enzyme
(C) Acid
maltase
(D)
Glucose-6-phosphatase
139. Her’s disease is characterized by deficiency of
(A) Muscle
phosphorylase
(B) Liver phosphorylase
(C) Debranching
enzyme
(D) Glycogen
synthase
140. Tarui disease is characterized by the deficiency
of the enzyme:
(A) Liver
phosphorylase
(B) Muscle
phosphorylase
(C) Muscle and erythrocyte phosphofructokinase
(D) Lysosomal
acid maltase
141. The hexose monophosphate pathway includes the
enzyme:
(A) Maltase
dehydrogenase
(B) Hexokinase
(C)
α-Ketoglutarate dehydrogenase
(D) Glucose-6-phosphate dehydrogenase
142. The hydrogen acceptor used in pentose phosphate
pathway is
(A) NAD
(B) NADP
(C) FAD
(D) FMN
143. The enzymes of the pentose phosphate pathway are
found in the
(A) Cytosol
(B)
Mitochondria
(C) Nucleus
(D) Endoplasmic
reticulum
144. In pentose phosphate pathway,
D-ribulose-5-phosphate is converted to D-ribose-5-phosphate by the enzyme:
(A) Fumarase
(B) Ketoisomerase
(C) G-6-PD
(D) Epimerase
145. The transketolase enzyme in the pentosephosphate
pathway requires the B vitamin.
(A) Pantothenic
acid
(B) Thiamin
(C) Riboflavin
(D) Nicotinic
acid
146. Xylulose-5-phosphate serves as a donar of active
glycolaldehyde, the acceptor is
(A) Erythrose 4-phosphate
(B) Ribose
5-phosphate
(C)
Glyceraldehyde 3-phosphate
(D)
Sedoheptulose 7-phosphate
147. Pentose phosphate pathway is of significance
because it generates
(A) NADPH for reductive synthesis
(B) Regenerates glucose 6-phosphate
(C) Generates
fructose 6-phosphate
(D) Forms
glyceraldehyde 3-phosphate
148. The pentose phosphate pathway protects
erythrocytes against hemolysis by assisting the enzyme:
(A) Superoxide
dismutase
(B) Catalase
(C) Glutathionic peroxidase
(D) Cytochrome
oxidase
149. Hemolytic anemia is caused by the deficiency of
certain enzymes of the pentose
phosphate pathway, the principal enzyme involved is
(A) Glucose-6-phosphate dehydrogenase
(B) Aldolase
(C) Fructose 1,
6-bisphosphatase
(D)
Phosphohexose isomerase
150. The sites for gluconeogenesis are
(A) Liver and kidney
(B) Skin and
pancreas
(C) Lung and
brain
(D) Intestine
and lens of eye
151. An enzyme involved in gluconeogenesis is
(A) Pyruvate
kinase
(B) Pyruvate carboxylase
(C) Hexokinase
(D)
Phosphohexose isomerase
152. The enzyme pyruvate carboxylase is present in
(A) Cytosol
(B) Mitochondria
(C) Nucleus
(D) Golgi
bodies
153. The enzyme phosphoenolpyruvate carboxykinase
catalyses the conversion of oxaloacetate to phosphoenolpyruvate requires
(A) ATP
(B) ADP
(C) AMP
(D) GTP
154. The enzyme glucose 6-phosphatase is present in
(A) Liver
(B) Muscle
(C) Adipose
tissue
(D) Brain
155. In
gluconeogensis, an allosteric activator required in the synthesis of
oxaloacetate from bicarbonate and pyruvate, which is catalysed by the enzyme
pyruvate carboxylase is
(A) Acetyl CoA
(B) Succinate
(C) Isocitrate
(D) Citrate
156. The number of ATP molecules required to convert 2
molecules of lactate into glucose in mammalian liver is
(A) 2
(B) 4
(C) 5
(D) 6
157. For conjugation with many enogenous and exogenous
substances before elimination in urine, the uronic acid pathway provides
(A) Active glucuronate
(B) Gulonate
(C) Xylulose
(D) Xylitol
158. UDP
glucose is converted
to UDP glucurronate, a reaction
catalysed by UDP glucose dehydrogenase requires
(A) NAD+
(B) FAD
(C) NADP
(D) FMN
159. Pentosuria is a rare hereditary disease is
characterized by increased urinary excretion of
(A) L-xylulose
(B) Xylitol
(C) Xylulose
5-phosphate
(D) Ribose
5-phosphate
160. The enzyme involved in essential pentosuria is
(A) Reductase
(B) Hydroxylase
(C) Isomerase
(D) Racemase
161. Galactose is synthesized from glucose in
(A) Mammary gland
(B) Intestine
(C) Kidney
(D) Adipose
tissue
162. Galactose is readily converted to glucose in
(A) Liver
(B) Intestine
(C) Kidney
(D) Adipose
tissue
163. Galactose 1-phosphate is converted to uridine
diphosphate galactose, the reaction is catalysed by the enzyme:
(A)
Glactokinase
(B) Galactose 1-phosphate uridyl transferase
(C) Uridine
diphospho galactose 4-epimerase
(D) UDP glucose
pyrophosphorylase
164. The best known cause of galactosemia is the
deficiency of
(A) Galactose 1-phosphate and uridyl transferase
(B)
Phosphoglucomutase
(C)
Galactokinase
(D) Lactose
synthase
165. Conversion of fructose to sorbitol is catalysed
by the enzyme:
(A) Sorbitol dehydrogenase
(B) Aldose
reductase
(C)
Fructokinase
(D) Hexokinase
166. A specific fructokinase present in liver has a
very high affinity for its substrate because
(A) Km
for fructose is very high
(B) Km for fructose is very low
(C) Activity is
affected by fasting
(D) Activity is
affected by insulin
167. Insulin has no effect on the activity of the
enzyme:
(A) Glycogen
synthetase
(B) Fructokinase
(C) Pyruvate
kinase
(D) Pyruvate
dehydrogenase
168. The pathogenesis of diabetic cataract involves
accumulation of
(A) Galactose
(B) Mannitol
(C) Sorbitol
(D) Pyruvate
169. Hereditary fructose intolerance involves the
absence of the enzyme:
(A) Aldalose B
(B)
Fructokinase
(C) Triokinase
(D)
Phosphotriose isomerase
170. Essential fructosuria is characterized by the
lack of the hepatic enzyme:
(A)
Phosphohexose isomerase
(B) Aldalose A
(C) Aldolase B
(D) Fructokinase
171. In normal individuals glycosuria occurs when the
venous blood glucose concentration exceeds
(A) 5-6 mmol/L
(B) 7-8 mmol/L
(C) 8.5-9
mmol/L
(D) 9.5-10 mmol/L
172. Phlorizin inhibits
(A) Renal tubular reabsorption of glucose
(B) Glycolysis
(C) Gluconeogenesis
(D)
Glycogenolysis
173. Renal glycosuria is characterized by
(A)
Hyperglycemia
(B)
Hyperglycemia with glycosuria
(C) Normal blood glucose level with glycosuria
(D)
Hyperglycemia with ketosis
174. Acute hemolytic anemia in person’s sensitive to
the Fava beans is due to the deficiency of the enzyme:
(A) Pyruvate
dehydrogenase
(B) G-6-PD
(C) Aconitase
(D)
Transketolase
175. Acute hemolytic episode after administration of
antimalarial, primaquin, is due to deficiency of the enzyme:
(A) 6-Phosphogluconate dehydrogenase
(B) Glucose-6-phosphate dehydrogenase
(C) Epimerase
(D)
Transketolase
176. The pH optima of gastric lipase is
(A) 3.0-6.0
(B) 1.0-2.0
(C) 8.0
(D) 8.6
177. The optimum pH of pancreatic lipase is
(A) 2.0
(B) 4.0
(C) 6.0
(D) 8.0
178. Gastric lipae is activated in the presence of
(A) Bile salts
(B) Cu++
(C) K+
(D) Na+
179. An example of enzyme inhibition:
(A) Reversible
inhibition
(B) Irreversible inhibition
(C) Allosteric
inhibition
(D) All of these
180. The formation of ∆2-trans-enoyl-CoA
from acyl-CoA requires the enzyme:
(A) Acyl-CoA
synthetase
(B) Acyl-CoA dehydrogenase
(C) 3-Hydroxy
acyl-CoA dehydrogenase
(D) Thiolase
181. In β-oxidation 3-ketoacyl-CoA is splitted at the
2, 3 position by the enzyme:
(A) Hydratase
(B)
Dehydrogenase
(C) Reducatse
(D) Thiolase
182. Fatty acids with odd number of carbon atoms yield
acetyl-CoA and a molecule of
(A)
Succinyl-CoA
(B) Propionyl-CoA
(C) Malonyl-CoA
(D)
Acetoacetyl-CoA
183. For each of the first 7-acetyl-CoA molecules
formed by α-oxidation of palmitic acid, the yield of high energy phosphates is
(A) 12
(B) 24
(C) 30
(D) 35
184. The net gain of ATP/mol of palmitic acid on
complete oxidation is
(A) 88
(B) 105
(C) 129
(D) 135
185.
ω-oxidation is normally a very minor pathway and is brought by
hydroxylase enzymes involving
(A) Cytochrome
a
(B) Cytochrome
b
(C) Cytochrome c
(D) Cytochrome
p-450
186.
α-Oxidation i.e., the removal of one carbon at a time from the carboxyl
end of the molecule has been detected in
(A) Brain tissue
(B) Liver
(C) Adipose
tissue
(D) Intestine
187. In β-oxidation, the coenzyme for acyl-CoA
dehydrogenase is
(A) FMN
(B) NAD
(C) NADP
(D) FAD
188. The coenzyme involved in dehydrogenation of
3-hydroxy acyl-CoA is
(A) FAD
(B) FMN
(C) NAD
(D) NADP
189.
The concentration of ketone bodies in the blood does not normally exceed
(A) 0.2 mmol/L
(B) 0.4
mmol/L
(C) 1
mmol/L
(D) 2
mmol/L
190. In humans under normal conditions loss of ketone
bodies via urine is usually less than
(A) 1 mg/24 hr
(B) 4 mg/24
hr
(C) 8 mg/24
hr
(D) 10
mg/24 hr
191. The structure which appears to be the only organ
to add significant quantities of ketone bodies to the blood is
(A) Brain
(B) Erythrocytes
(C) Liver
(D) Skeletal
muscle
192. The starting material for ketogenesis is
(A) Acyl-CoA
(B) Acetyl-CoA
(C) Acetoacetyl-CoA
(D) Malonyl-CoA
193. Enzymes responsible for ketone body formation are
associated mainly with the
(A) Mitochondria
(B) Endoplasmic
reticulum
(C) Nucleus
(D) Golgi
apparatus
194. The synthesis of 3-hydroxy-3-methylglutaryl-CoA
can occur
(A) Only in
mitochondria of all mammalian tissues
(B) Only in the cytosol of all mammalian
tissue
(C) In both cytosol and mitochondria
(D) In
lysosomes
195. In the pathway leading to biosynthesis of
acetoacetate from acetyl-CoA in liver,
the immediate precursor of aceotacetate is
(A) Acetoacetyl-CoA
(B) 3-Hydroxybutyryl-CoA
(C) 3-Hydroxy-3-methyl-glutaryl-CoA
(D) 3-Hydroxybutyrate
196. Ketone bodies serve as a fuel for
(A) Extrahepatic tissues
(B) Hepatic
tissues
(C)
Erythrocytes
(D)
Mitochondria
197. In extra hepatic tissues, one mechanism for
utilization of acetoacetate involves
(A) Malonyl-CoA
(B) Succinyl-CoA
(C)
Propionyl-CoA
(D) Acetyl-CoA
198. Ketosis reflects
(A) Increased
hepatic glucose liberation
(B) Increased fatty acid oxidation
(C) Increased
carbohydrate utilisation
(D) Incresed
gluconeogenesis
199. Ketosis is associated with the disease:
(A) Nephritis
(B) Diabetes mellitus
(C) Edema
(D) Coronary
artery diseases
200. The main pathway for denovo synthesis of fatty
acids occur in
(A) Cytosol
(B)
Mitochondria
(C) Microsomes
(D) Nucleus
201. Chain elongation of fatty acids in mammalian
liver occurs in
(A) Nucleus
(B) Ribosomes
(C) Lysosomes
(D) Microsomes
202. Acetyl-CoA is the principal building block of
fatty acids. It is produced within the mitochondria and does not diffuse
readily into cytosol. The availability of acetyl CoA involves
(A) Carnitine
acyl transferase
(B) Pyruvate dehydrogenase
(C) Citrate lyase
(D) Thiolase
203. The synthesis of fatty acids is often termed
reductive synthesis.
(A) NADP+
(B) NADH
(C) FADH2
(D) NADPH
204. The protein, which is in fact a multifunctional
enzyme complex in higher organism is
(A) Acetyl
transacylase
(B) Malonyl
transacylase
(C) 3-Hydroxy
acyl-ACP dehyratase
(D) Fatty acid synthase
205.
The fatty acid synthase complex catalyses
(A) 4 sequential enzymatic steps
(B) 6 sequential
enzymatic steps
(C) 7
sequential enzymatic steps
(D) 8
sequential enzymatic steps
206. The main source of reducing equivalents (NADPH)
for lipogenesis is
(A) Pentose phosphate pathway
(B) Citric acid
cycle
(C) Glycolysis
(D)
Glycogenolysis
207. In fatty acids synthase of both bacteria and
mammals, ACP (acyl carrier protein) contain the vitamin:
(A) Thiamin
(B) Pyridoxine
(C) Riboflavin
(D) Pantothenic acid
208. Carboxylation of acetyl-CoA to malonyl CoA
requires the enzyme:
(A) Acetyl-CoA carboxylase
(B) Pyruvate
carboxylase
(C) Acetyl
transacylase
(D) Acyl
CoA-synthetase
209. The rate limiting reaction in the lipogenic
pathway is
(A) Acetyl-CoA carboxylase step
(B) Ketoacyl
synthase step
(C) Ketoacyl
reductase step
(D) Hydratase
step
210. Conversion of fatty acyl-CoA to an acylCoA
derivative having 2 more carbon atoms involves as acetyl donar:
(A) Acetyl-CoA
(B)
Succinyl-CoA
(C)
Propionyl-CoA
(D) Malonyl-CoA
211. A cofactor required for the conversion of
acetyl-CoA to malonyl-CoA in extramitochondrial fatty acid synthesis is
(A) Biotin
(B) FMN
(C) NAD
(D) NADP
212. The glycerol for fatty acid esterification in
adipocytes is
(A) For the most part, derived from glucose
(B) Obtained
primarily from phosphorylation of glycerol by glycerol kinase
(C) Formed from
gluconeogenesis
(D) Formed from
glycogenolysis
213. In the biosynthesis of triglycerides from
glycerol 3-phosphate and acyl-CoA, the first intermediate formed is
(A) 2-Monoacylglycerol
(B) 1,
2-Diacylglycerol
(C) Lysophosphatidic
acid
(D) Phosphatidic acid
214. The
enzyme glycerol kinase is low activity in
(A) Liver
(B) Kidney
(C) Intestine
(D) Adipose tissue
215. The common precursor in the biosynthesis of
triacylglycerol and phospholipids is
(A) 1, 2-Diacylglycerol phosphate
(B) 1-Acylglycerol
3-phosphate
(C) Glycerol
3-phosphate
(D) Dihydroxyacetone
phosphate
216. Synthesis of polyunsaturated fatty acids involves
the enzyme systems:
(A) Acyl transferase and hydratase
(B) Desaturase
and elongase
(C)
Ketoacyl-CoA reductase and hydratase
(D)
Dihydroxyacetone phosphate
217. The desaturation and chain elongation system of
polyunsaturated fatty acid are enhanced by
(A) Insulin
(B) Glucagon
(C) Epinephrine
(D) Thyroxine
218. Higher rate of lipogenesis is associated with
(A) High proportion of carbohydrate in diet
(B) Restricted
caloric intake
(C) High fat
diet
(D) Deficiency
of insulin
219. Example of enzyme specificity:
(A) Stereo
specificity
(B) Reaction
specificity
(C) Substrate
specificity
(D) All of these
220. Phospholipase C attacks the ester bond liberating
1, 2-diacylglycerol and a phosphoryl base at position
(A) 1
(B) 2
(C) Both
(A) and (B)
(D) 3
221. Synthesis of phosphatidylinositol by transfer of
inositol to CDP diacylglycerol is catalysed by the enzyme:
(A) CTP
phosphatidate cytidyl transferase
(B)
Phosphatidate phosphohydrolase
(C) CDP-diacylglycerol inositol transferase
(D) Choline
kinase
222. Synthesis of sphingosine requires the cofactor
(A) NAD
(B) NADP
(C) NADPH+
(D) ATP
223. Ceramide is formed by the combination of
sphingosine and
(A) Acetyl-CoA
(B) Acyl-CoA
(C) Malonyl-CoA
(D)
Propionyl-CoA
224. The amino alcohol sphingosine is synthesized in
(A)
Mitochondria
(B) Cytosol
(C) Nucleus
(D) Endoplasmic reticulum
225. The output of free fatty acids from adipose
tissue is reduced by
(A) Insulin
(B) Glucagon
(C) Growth
hormone
(D) Epinephrine
226. The principal action of insulin in adipose tissue
is to inhibit the activity of the
(A) Hormone sensitive lipoprotein lipase
(B) Glycerol phosphate acyltransferase
(C) Acetyl-CoA
carboxylase
(D) Pyruvate
dehydrogenase
227. In non shivering thermogenesis
(A) Glucose is
oxidized to lactate
(B) Fatty acids uncouple oxidative phosphorylation
(C) Ethanol is
formed
(D) ATP is
burned for heat production
228. Brown adipose tissue is
(A) A prominent
tissue in human
(B) Characterised by high content of mitochondria
(C) Associated
with high activity of ATP synthase
(D) Characterised
by low content of cytochromes
229. Fatty
liver is caused due to accumulation of
(A) Fatty acids
(B) Cholesterol
(C)
Phospholipids
(D) Triacylglycerol
230. A
lipotropic factor is
(A) Choline
(B) Palmitic
acid
(C) Calcium
(D) Vitamin C
231. Fatty liver is also caused by
(A) CH3Cl
(B) CCl4
(C) Na2SO4
(D) Riboflavin
232. All the
enzymes involved in the synthesis of cholesterol are found in
(A)
Mitochondria
(B) Golgi
apparatus
(C) Nucleus
(D) Endoplasmic reticulum and cytosol
233. The
source of all the carbon atoms in cholesterol is
(A) Acetyl-CoA
(B) Bicarbonate
(C)
Propionyl-CoA
(D)
Succinyl-CoA
234. Two
molecules of acetyl-CoA condense to form acetoacetyl-CoA catalysed by
(A) Thiolase
(B) Kinase
(C) Reductase
(D) Isomerase
235. Acetoacetyl-CoA
condenses with one more molecule of acetyl-CoA to form
(A) Mevalonate
(B)
Acetoacetate
(C)
β-Hydroxybutyrate
(D) 3-Hydroxy 3-methyl-glutaryl-CoA
236. HMG-CoA is converted to mevalonate by reduction
catalysed by
(A) HMG-CoA
synthetase
(B) HMG-CoA reductase
(C) Mevalonate
kinase
(D) Thiolase
237. For reduction enzyme HMG-CoA reductase requires
cofactor:
(A) NADPH
(B) NADP
(C) NAD
(D) FAD
238. In the
biosynthesis of cholesterol, the step which controls the rate and locus of
metabolic regulation is
(A) Geranyl
pyrophosphate farnesyl pyrophosphate
(B) Squalene →
lanosterol
(C) HMG CoA → mevalonate
(D) Lanosterol
→ 1, 4-desmethyl lanosterol
239. The
cyclisation of squalene in mammals results in the direct formation of the
sterol.
(A) Cholesterol
(B) Lanosterol
(C) Sistosterol
(D) Zymosterol
240. In the
biosynthesis of cholesterol, the rate limiting enzyme is
(A) Mevalonate
kinase
(B) HMG-CoA synthetase
(C) HMG-CoA reductase
(D) Cis-prenyl
transferase
241. Cholesterol
by a feed back mechanism inhibits the activity of
(A) HMG-CoA synthetase
(B) HMG-CoA reductase
(C) Thilase
(D) Mevalonate
kinase
242. The
activity of HMG-CoA reductase is inhibited by
(A) A fungal inhibitor mevastatin (B) Probucol
(C) Nicotinic
acid
(D) Clofibrate
243. Hypolipidemic
drugs reduce serum cholesterol and triacylglycerol. The effect of clofibrate is
attributed to
(A) Block in
absorption from G.I.T.
(B) Decrease in secretion of triacylglycerol and
cholesterol containing VLDL by liver
(C) Block in
the reabsorption of bile acids
(D) Decreased
synthesis of cholesterol
244. In
biosynthesis of cholesterol triparanol inhibits the activity of the enzyme:
(A) ∆24 Reductase
(B)
Oxidosqualene-lanosterol cyclase
(C) Isomerase
(D) Squalene
epoxidase
245. HMG-CoA
reductase activity is increased by administration of the hormone:
(A) Insulin
(B) Glucagon
(C) Epinephrine
(D)
Glucocorticoids
246. The principal sterol excreted in feces is
(A) Coprostanol
(B) Zymosterol
(C) Lanosterol
(D) Desmosterol
247. The
principal rate limiting step in the biosynthesis of bile acids is at the
(A) 7-Hydroxylase reaction
(B) 12
α-Hydroxylase reaction
(C) Conjugation
reaction
(D) Deconjugation
reaction
248. Hypercholesterolemia
is found in
(A) Xanthomatosis
(B)
Thyrotoxicosis
(C) Hemolytic
jaundice
(D)
Malabsorption syndrom
249. Hypocholesterolemia
is found in
(A) Thyrotoxicosis
(B) Diabetes
mellitus
(C) Obstructive
jaundice
(D) Nephrotic
syndrome
250. The
major source of extracellular cholesterol for human tissue is
(A) Very low
density lipoprotein
(B) High
density lipoprotein
(C) Low density lipoprotein
(D) Albumin
251. Correct
ordering of lipoprotein molecules from lowest to the greater density is
(A) LDL, IDL,
VLDL, chylomicron
(B) Chylomicron, VLDL, IDL, LDL
(C) VLDL, IDL,
LDL, chylomicron
(D) LDL, VLDL,
IDL, chylomicron
252. In
Hurler’s syndrome, urine shows the presence of
(A) Keratan
sulphate I
(B) Chondroitin
sulphate
(C) Dermatan sulphate and heparan sulphate
(D) Keratan
sulphate II
253. Defective enzyme in Hunter’s syndrome is
(A)
α-L-iduronidase
(B) Iduronate sulphatase
(C)
Arylsulphatase B
(D) C-acetyl
transferase
254. In
Hunter’s syndrome
(A) There is
progressive corneal opacity
(B) Keratan sulphate is excreted in the
urine
(C) Enzyme
defective is arylsulphatase B
(D) Hearing loss is perceptive
255. An
important feature of Von-Gierke’s disease is
(A) Muscle
cramps
(B) Cardiac
failure
(C) Hypoglycemia
(D) Respiratory
alkalosis
256. The
affected organ in Mc Ardle’s syndrome is
(A) Liver
(B) Kidney
(C) Liver and
Heart
(D) Skeletal muscle
257. Refsum’s disease is due to deficiency of the
enzyme:
(A) Pytantate-α-oxidase
(B) Glucocerebrosidase
(C)
Galactocerebrosidase
(D) Ceramide
trihexosidase
258. An important finding in Refsum’s disease is
(A)
Accumulation of ceramide trihexoside in the kidney
(B) Accumulation of phytanic acid in the blood
and tissues
(C)
Accumulation of gangliosides in brain and spleen
(D) Skin
eruptions
259. α-Galactosidase
enzyme is defective in
(A) Tay-sach’s
disease
(B) Refsum’s
disease
(C) Sandhoff’s
disease
(D) Fabry’s disease
260. The
hypothesis to explain enzyme-substrate complex formation:
(A) Lock and
key model
(B) Induced fit
theory
(C) Proenzyme theory
(D) Both (A)
and (B)
261. An
important finding in Tay-sach’s disease is
(A) Renal
failure
(B) Accumulation of gangliosides in brain and spleen
(C) Cardiac
failure
(D) Anemia
262. The
enzyme deficient in Krabbe’s disease is
(A)
Hexosaminidase A
(B)
Arylsuphatase A
(C) β-Galactosidase
(D)
α-Fucosidase
263. The enzyme
ceramidase is deficient in
(A) Farber’s disease
(B) Fabry’s
disease
(C) Sandhoff’s
disease
(D) Refsum’s
disease
264. Niemann-Pick
disease is due to deficiency of the enzyme
(A) Ceramidase
(B)
Glucocerebrosidase
(C)
Galactocerebrosidase
(D) Sphingomyelinase
265. Wolman’s
disease is due to deficiency of
(A) Cholesteryl ester hydrolase
(B)
Hexosaminidase A
(C)
α-Fucosidase
(D)
Arylsulphatase A
266. The
enzyme deficient in Sandhoff’s disease is
(A)
α-Fucosidase
(B) Hexosaminidase A and B
(C)
β-Galactosidase
(D)
β-Glucosidase
267. Jamaican
vomiting sickness is due to inactivation of the enzyme
(A) Pyruvate
carboxylase
(B) Acyl-Co-A
synthetase
(C) Acyl-Co-A dehydrogense
(D) Thiolase
268. Zellweger’s
syndrome is due to inherited absence of
(A) Peroxisomes
(B)
Phospholipase A1
(C) Acyl-Co-A
dehydrogenase
(D) Thiolase
269. Bassen-Kornzweig
syndrome is due to
(A) Absence of
Apo-C-II
(B) Defect in Apo-B synthesis
(C) Absence of
Apo-E
(D) Absence of
Apo-D
270. Enzyme
deficient in Hyperammonemia type II is
(A) Glutamine
synthetase
(B) Glutaminase
(C) Ornithine transcarbamoylase
(D)
Carbamoylphosphate synthetase
271. An
important finding in Hyperammonemia type II is
(A) Increased
serum gluatmine level
(B) Enlarged
liver
(C) Mental retardation
(D) Increased
carbamoyl phosphate synthetase level
272. Absence
of the enzyme argininosuccinate synthetase causes
(A) Argininosuccinic aciduria
(B)
Hyperargininemia
(C) Tricorrhexis
nodosa
(D)
Citrullinemia
273. Tricorrhexis
nodosa is a characteristic finding of
(A)
Argininosuccinic aciduria
(B)
Citrullinemia
(C)
Phenylketonuria
(D) Hyperargininemia
274. Elevated
blood argininosuccinate level is found in
(A) Hyperargininemia
(B)
Argininosuccinic aciduria
(C)
Citrullinemia
(D) Tyrosinosis
275. Hyperargininemia,
a defect in urea synthesis develops due to deficiency of the enzyme:
(A) Ornithine
transcarbamoylase
(B) Argininosuccinase
(C) Arginase
(D)
Argininosuccinate synthetase
276. Albinism
is due to deficiency of the enzyme:
(A)
Phenylalanine hydroxylase
(B) Tyrosinase
(C) p-Hydroxyphenylpyruvic acid oxidase
(D) Tyrosine
dehydrogenase
277. Neonatal
tyrosinemia is due to deficiency of the enzyme:
(A) p-Hydroxyphenylpyruvate
hydroxylase
(B) Fumarylacetoacetate hydrolase
(C)
Phenylalanine hydroxylase
(D) Tyrosine
dehydrogenase
278. Which of
the following is a substrate specific enzyme?
(A) Hexokinase
(B) Thiokinase
(C) Lactase
(D)
Aminopeptidase
279. Coenzymes
combine with
(A) Proenzymes
(B) Apoenzymes
(C) Holoenzymes
(D) Antienzymes
280. Coenzymes
are required in which of the following reactions?
(A)
Oxidation-reduction
(B)
Transamination
(C)
Phosphorylation
(D) All of these
281. Which of
the following coenzyme takes part in hydrogen transfer reactions?
(A)
Tetrahydrofolate
(B) Coenzyme A
(C) Coenzyme Q
(D) Biotin
282. Which of
the following coenzyme takes part in oxidation-reduction reactions?
(A) Pyridoxal
phosphate
(B) Lipoic acid
(C) Thiamin
diphosphate
(D) None of
these
283. In
conversion of glucose to glucose-6-phsophate, the coenzyme is
(A) Mg++
(B) ATP
(C) Both (A)
and (B)
(D) None of
these
284. A
coenzyme required in transamination reactions is
(A) Coenzyme A
(B) Coenzyme Q
(C) Biotin
(D) Pyridoxal phosphate
285. Coenzyme
A contains a vitamin which is
(A) Thiamin
(B) Ascorbic
acid
(C) Pantothenic acid
(D) Niacinamide
286. Cobamides
contain a vitamin which is
(A) Folic acid
(B) Ascorbic acid
(C) Pantothenic
acid
(D) Vitamin B12
287. A
coenzyme required in carboxylation reactions is
(A) Lipoic acid
(B) Coenzyme A
(C) Biotin
(D) All of
these
288. Which of
the following coenzyme takes part in tissue respiration?
(A) Coenzyme Q
(B) Coenzyme A
(C) NADP
(D) Cobamide
289. The
enzyme hexokinase is a
(A) Hydrolase
(B)
Oxidoreductase
(C) Transferase
(D) Ligase
290. Which of
the following is a proteolytic enzyme?
(A) Pepsin
(B) Trypsin
(C)
Chymotrypsin
(D) All of these
291. Enzymes
which catalyse binding of two substrates by covalent bonds are known as
(A) Lyases
(B) Hydrolases
(C) Ligases
(D)
Oxidoreductases
292. The
induced fit model of enzyme action was proposed by
(A) Fischer
(B) Koshland
(C) Mitchell
(D) Markert
293. Allosteric
inhibition is also known as
(A) Competitive
inhibition
(B)
Non-competitive inhibition
(C) Feedback inhibition
(D) None of
these
294. An
allosteric enzyme is generally inhibited by
(A) Initial
substrate of the pathway
(B) Substrate
analogues
(C) Product of
the reaction catalysed by allosteric enzyme
(D) Product of the pathway
295. When the
velocity of an enzymatic reaction equals Vmax, substrate
concentration is
(A) Half of Km
(B) Equal to Km
(C) Twice the Km
(D) Far above the Km
296. In
Lineweaver-Burk plot, the y-intercept represents
(A) Vmax
(B) Km
(C) Km
(D) 1/Km
297. In
competitive inhibition, the inhibitor
(A) Competes
with the enzyme
(B) Irreversibly binds with the enzyme
(C) Binds with
the substrate
(D) Competes with the substrate
298 Competitive
inhibitors
(A) Decrease
the Km
(B) Decrease
the Vmax
(C) Increase the Km
(D) Increase
the Vmax
299. Competitive
inhibition can be relieved by raising the
(A) Enzyme
concentration
(B) Substrate concentration
(C) Inhibitor
concentration
(D) None of
these
300. Physostigmine
is a competitive inhibitor of
(A) Xanthine
oxidase
(B) Cholinesterase
(C) Carbonic
anhydrase
(D) Monoamine
oxidase
301. Carbonic
anhydrase is competitively inhibited by
(A) Allopurinol
(B) Acetazolamide
(C) Aminopterin
(D) Neostigmine
302. Serum
lactate dehydrogenase rises in
(A) Viral
hepatitis
(B) Myocardial
infarction
(C)
Carcinomatosis
(D) All of these
303. Which of
the following serum enzyme rises in myocardial infarction:
(A) Creatine
kinase
(B) GOT
(C) LDH
(D) All of these
304. From the
following myocardial infarction, the earliest serum enzyme to rise is
(A) Creatine Kinase
(B) GOT
(C) GPT
(D) LDH
305. Proenzymes:
(A)
Chymotrysinogen
(B) Pepsinogen
(C) Both (A)
and (B)
(D) None of
these
306. Alkaline
phosphatase is present in
(A) Liver
(B) Bones
(C) Placenta
(D) All of these
307. Which of
the following isoenzyme of lactate dehydrogenase is raised in serum in
myocardial infarction:
(A) LD1
(B) LD2
(C) LD1 and LD2
(D) LD5
308. Enzymes
which are always present in an organism are known as
(A) Inducible
enzymes
(B) Constitutive enzymes
(C) Functional
enzymes
(D) Apoenzymes
309. Inactive
precursors of enzymes are known as
(A) Apoenzymes
(B) Coenzymes
(C) Proenzymes
(D) Holoenzymes
310. Whcih of
the following is a proenzyme?
(A)
Carboxypeptidase
(B)
Aminopeptidase
(C)
Chymotrypsin
(D) Pepsinogen
311. Allosteric
enzymes regulate the formation of products by
(A) Feedback inhibition
(B)
Non-competitive inhibition
(C) Competitive
inhibition
(D)
Repression-derepression
312 Regulation
of some enzymes by covalentmodification involves addition or removal of
(A) Acetate
(B) Sulphate
(C) Phosphate
(D) Coenzyme
313. Covalent
modification of an enzyme generally requires a
(A) Hormone
(B) cAMP
(C) Protein
kinase
(D) All of these
314. An
inorganic ion required for the activity of an enzyme is known as
(A) Activator
(B) Cofactor
(C) Coenzyme
(D) None of
these
315. The
first enzyme found to have isoenzymes was
(A) Alkaline
Phosphatase
(B) Lactate dehydrogenase
(C) Acid
Phosphatase
(D) Creatine
kinase
316. Lactate
dehydrogenase is located in
(A) Lysosomes
(B) Mitochondria
(C) Cytosol
(D) Microsomes
317. Lactate
dehydrogenase is a
(A) Monomer
(B) Dimer
(C) Tetramer
(D) Hexamer
318. Ceruloplasmin
is absent in
(A) Cirrhosis
of liver
(B) Wilson’s disease
(C) Menke’s
disease
(D) Copper
deficiency
319. Ceruloplasmin
oxidizes
(A) Copper
(B) Iron
(C) Both (A)
and (B)
(D) None of
these
320. Creatine
kinase is present in all of the following except
(A) Liver
(B) Myocardium
(C) Muscles
(D) Brain
321. Alkaline
phosphatase is present in
(A) Liver
(B) Bones
(C) Intestinal
mucosa
(D) All of these
322. All of
the following are zinc-containing enzymes except
(A) Acid Phosphatase
(B) Alkaline
Phosphatase
(C) Carbonic
anhydrase
(D) RNA
polymerase
323. All of
the following are iron-containing enzymes except
(A) Carbonic anhydrase
(B) Catalase
(C) Peroxidase
(D) Cytochrome
oxidase
324. Biotin
is a coenzyme for
(A) Pyruvate
dehydrogenase
(B) Pyruvate carboxylase
(C) PEP
carboxykinase
(D) Glutamate
pyruvate transminase
325. Enzymes
accelerate the rate of reactions by
(A) Increasing
the equilibrium constant of reactions
(B) Increasing
the energy of activation
(C) Decreasing the energy of activation
(D) Decreasing
the free energy change of the reaction
326. Kinetics
of an allosteric enzyme are explained by
(A)
Michaelis-Menten equation
(B)
Lineweaver-Burk plot
(C) Hill plot
(D) All of
these
327. Covalent
modification of an enzyme usually involves phosphorylation /dephosphorylation
of
(A) Serine residue
(B) Proline residue
(C)
Hydroxylysine residue
(D)
Hydroxyproline residue
328. Vmax
of an enzyme may be affected by
(A) pH
(B) Temperature
(C)
Non-competitive inhibitors
(D) All of these
329. In
enzyme assays, all the following are kept constant except
(A) Substrate
concentration
(B) Enzyme concentration
(C) pH
(D) Temperature
330. If the
substrate concentration is much below the km of the enzyme, the velocity of the
reaction is
(A) Directly proportional to substrate
concentration
(B) Not
affected by enzyme concentration
(C) Nearly
equal to Vmax
(D) Inversely
proportional to substrate concentration
331. Enzymes
requiring NAD as co-substrate can be assayed by measuring change in absorbance
at
(A) 210 nm
(B) 290 nm
(C) 340 nm
(D) 365 nm
332. Different
isoenzymes of an enzyme have the same
(A) Amino acid
sequence
(B) Michaelis
constant
(C) Catalytic activity
(D) All of
these
333. From the
pentapeptide, phe-ala-leu-lys-arg, phenylalanine residue is split off by
(A) Trypsin
(B) Chymotrypsin
(C) Aminopeptidase
(D)
Carboxypeptidase
334. A
high-energy phosphate among the following is
(A)
Glucose-6-phosphate
(B) Glucose-1-phosphate
(C) 1, 3-Biphoglycerate
(D) All of
these
335. The
highest energy level is present amongst the following in
(A) 1, 3-Biphosphoglycerate
(B) Creatine phosphate
(C) Carbamoyl
phosphate
(D) Phosphoenol pyruvate
336. Daily
urinary urobilinogen excretion in adult men is
(A) 0-4 mg
(B) 5-8 mg
(C) 9-12 mg
(D) 13-20
mg
337. In obstructive jaundice, faecal urobilinogen is
(A) Absent
(B) Decreased
(C) Increased
(D) Normal
338. Acetyl-CoA
can be formed from
(A) Pyruvate
(B) Fatty acids
(C) ketone
bodies
(D) All of these
339. Pyruvate
is converted into acetyl-CoA by
(A)
Decarboxylation
(B) Dehydrogenation
(C) Oxidative decarboxylation
(D) Oxidative
deamination
340. Conversion
of pyruvate into acetyl CoA
is catalysed by
(A) Pyruvate
dehydrogenase
(B) Didrolipoyl acetyl transferase
(C)
Dihydrolipoyl dehydrogenase
(D) All the 3 acting in concert
341. Pyruvate
dehydrogenase complex is located in
(A) Cytosol
(B) Lysosomes
(C) Mitochondria
(D) Endoplasmic
reticulum
342. A
flavoprotein in pyruvate dehydrogenase complex is
(A) Pyruvate
dehydrogenase
(B) Didrolipoyl acetyl transferase
(C) Dihydrolipoyl dehydrogenase
(D) None of
these
343. Pyruvate
dehydrogenase complex is regulated by
(A) Covalent
modification
(B) Allosteric
regulation
(C) Both (A) and (B)
(D) None of
these
344. An
allosteric inhibitor of pyruvate dehydrogenase is
(A) Acetyl CoA
(B) ATP
(C) NADH
(D) Pyruvate
345. Ribozymes:
(A) RNA enzyme
(B) Non-protein
enzymes
(C) Catalyst
function
(D) All of these
346. In
citric acid cycle, NAD is reduced in
(A) One
reactions
(B) Two
reactions
(C) Three reactions
(D) Four
reactions
347. Among
citric acid cycle enzymes, a flavo-
protein is
(A) Malate
(B) Fumarase
(C) Succinate dehrogenase
(D) Isocitrate
dehrogenase
348. In
citric acid cycle, GDP is phosphorylated
by
(A) Succinate
dehydrogenase
(B) Aconitase
(C) Succinate thiokinase
(D) Fumarse
349. Malonate
is an inhibitor of
(A) Malate
dehydrogenase
(B) α-Ketoglutarate dehydrogenase
(C) Succinate dehydrogenase
(D) Isocitrate
dehydrogenase
350. Isocitrate
dehydrogenase is allosterically inhibited by
(A)
Oxalosuccinate
(B)
α-Ketoglutarate
(C) ATP
(D) NADH
351. All of
the following are allosteric enzymes
except
(A) Citrate
synthetase
(B)
a-Ketoglutarate dehdrogenase
(C) Succinate thiokinase
(D) Succinate
dehydrogenase
352. All of
the following are intermediates of citric acid cycle except
(A)
Oxalosuccinate
(B)
Oxaloacetate
(C) Pyruvate
(D) Fumarate
353. All of
the following intermediates of citric acid cycle can be formed from amino acids
except
(A)
α-Ketoglutarate
(B) Fumarate
(C) Malate
(D)
Oxaloacetate
354. Glycolytic
pathway is located in
(A)
Mitochondria
(B) Cytosol
(C) Microsomes
(D) Nucleus
355. End
product of aerobic glycolysis is
(A) Acetyl CoA
(B) Lactate
(C) Pyruvate
(D) CO2
and H2O
356. During
fasting, glucose is phosphorylated mainly by
(A) Hexokinase
(B) Glucokinase
(C) Both (A)
and (B)
(D) None of
these
357. Glucokinase
is found in
(A) Muscles
(B) Brain
(C) Liver
(D) All of
these
358. In anaerobic
glycolysis, energy yield from each molecule of glucose is
(A) 2 ATP equivalents
(B) 8 ATP equivalents
(C) 30 ATP
equivalents
(D) 38 ATP equivalents
359. Which of
the following is an allosteric
enzyme?
(A)
Phosphohexose isomerase
(B) Phosphotriose isomerase
(C) Lactate
dehydrogenase
(D) Phosphofructokinase
360. Glycolysis
is anaerobic in
(A) Liver
(B) Brain
(C) Kidneys
(D) Erythrocytes
361. Phosphofructokinase
is allosterically inhibited by
(A) Fructose-1,
6-biphosphate
(B) Lactate
(C) Pyruvate
(D) Citrate
362. Glucose-6-phosphate
is an allosteric inhibitor of
(A) Glucokinase
(B) Hexokinase
(C)
Phosphohexose isomerase
(D) None of
these
363. ATP is a
co-substrate as well as an allosteric inhibitor of
(A) Phosphofructokinase
(B) Hexokinase
(C) Glucokinase
(D) None of
these
364. Complete
oxidation of one molecule of glucose into CO2 and H2O
yields
(A) 8 ATP
equivalents
(B) 15 ATP
equivalents
(C) 30 ATP
equivalents
(D) 38 ATP equivalents
365. A unique
by-product of glycolysis in
erythrocytes is
(A) Lactate
(B) 1,
3-Biphosphoglycerate
(C) 2, 3-Biphosphoglycerate
(D) All of
these
366. Which of
the following enzymes incorporates inorganic phosphate into the substrate?
(A) Phosphoglycerate kinase
(B) Glyceraldehyde-3-phosphate
dehydrogenase
(C) Pyruvate
kinase
(D) Enolase
367. Rapoport-Luebering
cycle is located in
(A) Liver
(B) Muscles
(C) Brain
(D) Erythrocytes
368. Glycerol
can enter glycolytic pathway via
(A) Dihydroxyacetone phosphate
(B) 1, 3-Biphospoglycerate
(C) 3-Phosphoglycerate
(D) 2-Phosphoglycerate
369. HMP
shunt is present in
(A)
Erythrocytes
(B) Liver
(C) Testes
(D) All of these
370. Glucose-6-phosphate
dehydrogenase is
induced by
(A) 6-Phosphogluconolactone
(B) Glucose-6-phosphate
(C) Ribose-5-phosphate
(D) Insulin
371. The
decarboxylation reaction in HMP shunt is catalysed by
(A)
Gluconolactone hydrolase
(B) 6-Phosphogluconate
dehydrogenase
(C) 6-Phosphogluconate decarboxylase
(D)
Transaldolase
372. The
first pentose formed in HMP shunt is
(A)
Ribose-5-phosphate
(B)
Ribulose-5-phosphate
(C)
Xylose-5-phosphate
(D) Xylulose-5-phosphate
373. The
regulatory enzyme in HMP shunt is
(A)
Glucose-6-phosphate dehydrogenase
(B) 6-Phosphogluconate dehydrogenase
(C) Both (A) and (B)
(D) None of
these
374. The rate
of HMP shunt reactions is
(A) Increased by Insulin
(B) Increased
in diabetes mellitus
(C) Increased
by glucagons
(D) Increased
in starvation
375. Glycogenesis
requires
(A) GTP
(B) CTP
(C) UTP
(D) None of
these
376. Glycogen
synthetase catalyses the
formation of
(A) α−1, 4-Glycosidic bonds
(B) α−1, 6-Glycosidic bonds
(C) Both (A)
and (B)
(D) None of
these
377. Glycogenoloysis
is increased by
(A) Glucagon
(B) Insulin
(C) Epinephrine
(D) cAMP
378. Hepatic
glycogenoloysis is increased by
(A) Insulin
(B) Glucagon
(C) Epinephrine
(D)
Glucocorticoids
379. Glycogen
phosphorylase liberates the
following from glycogen
(A) Glucose
(B)
Glucose-6-phosphate
(C) Glucose-1-phosphate
(D) Maltose
380. After
the action of phosphorylase, glycogen is converted into
(A) Amylopectin
(B) dextrin
(C) Amylose
(D) Maltose
381. Glucose-1-phosphate
liberated from glycogen cannot be converted into free
glucose in
(A) Liver
(B) Kidneys
(C) Muscles
(D) Brain
382. A
coenzyme present in phosphorylase is
(A) NAD
(B) Pyridoxal phosphate
(C) Thiamin
pyrophosphate
(D) Coenzyme A
383. If
glucose-1-phosphate formed by glycogenoloysis in muscles is oxidized to
CO2 and H2O, the energy yield
will be
(A) 2 ATP
equivalents
(B) 3 ATP
equivalents
(C) 4 ATP equivalents
(D) 8 ATP equivalents
384. A
molecule of phosphorylase kinase is made up of
(A) 4
subunits
(B) 8
subunits
(C) 12
subunits
(D) 16 subunits
385. Cyclic
AMP binds to
(A) Catalytic
subunits of protein kinase
(B) Regulatory subunits of protein kinase
(C) Catalytic
subunits of phosphorylase kinase
(D) Regulatory
subunits of phosphorylase kinase
386. Glucose
is the only source of energy for
(A) Myocardium
(B) Kidneys
(C) Erythrocytes
(D)
Thrombocytes
387. Glycerol-3-phosphate
for the synthesis of triglycerides in adipose tissue is derived from
(A)
Phosphatidic acid
(B)
Diacylglycerol
(C) Glycerol
(D) Glucose
388. Gluconeogenesis
does not occur in
(A) Brain
(B) Kidneys
(C) Muscles
(D) Liver
389. Glucose
cannot be synthesized from
(A) Glycerol
(B) Lactate
(C) Alanine
(D) Leucine
390. Coenzyme
for phosphoenolpyruvate
carboxykinase is
(A) ATP
(B) ADP
(C) GTP
(D) GDP
391. Therapeutic
enzymes:
(A) Streptokinase
(B)
Asparaginase
(C) Riboflavinase
(D) Both (A) and (B)
392. A
gluconeogenic enzyme among the following is
(A) Phosphofructokinase
(B) Pyruvate kinase
(C) Phosphoenol pyruvate carboxykinase
(D) Glucokinase
393. Glucose-6-phosphatase
and PEP carboxy
kinase are regulated by
(A) Covalent modification
(B) Allosteric regulation
(C) Induction and repression
(D) All of
these
394. The
maximum possible chain length of fatty acids formed in the pathway of de
novo synthesis is
(A) 16 Carbon atoms
(B) 18 Carbon atoms
(C) 20
Carbon atoms
(D) 24 Carbon atoms
395. Acetyl
CoA required for de novo synthesis of fatty acids is obtained from
(A) Breakdown
of existing fatty acids
(B) Ketone
bodies
(C) Acetate
(D) Pyruvate
396. Formation
of acetyl CoA from pyruvate for de novo synthesis of fatty acids requires
(A) Pyruvate
dehydrogenase complex
(B) Citrate
synthetase
(C) ATP citrate
lyase
(D) All of these
397. The
major site for elongation of medium chain fatty acids is
(A)
Mitochondria
(B) Cytosol
(C) Microsomes
(D) All of
these
398.
β-oxidation of fatty acids is inhibited by
(A) NADPH
(B) Acetyl CoA
(C) Malonyl CoA
(D) None of
these
399. The
enzyme regulating extramitochondrial fatty acid synthesis is
(A)
Thioesterase
(B) Acetyl CoA carboxylase
(C) Acyl
transferase
(D)
Multi-enzyme complex
400. Acetyl
CoA carboxylase is activated by
(A) Citrate
(B) Insulin
(C) Both (A) and (B)
(D) None of
these
401. All the
following statements about acetyl CoA carboxylase are true except:
(A) It is
activated by citrate
(B) It is
inhibited by palmitoyl CoA
(C) It can
undergo covalent modification
(D) Its dephosphorylated form is inactive
402. All the
following statements about acetyl
CoA carboxylase are true except
(A) It is
required for de novo synthesis of fatty acids
(B) It is required for mitochondrial elongation
of fatty acids
(C) It is
required for microsomal elongation of fatty acids
(D) Insulin
converts its inactive form into its active form
403. Both
Acyl carrier protein (ACP) of fatty
acid synthetase and coenzyme (CoA) are
(A) Contain
reactive phosphorylated
(B) Contain
thymidine
(C) Contain phosphopantetheine reactive groups
(D) Contain
cystine reactive groups
404. Which
one of the following transfers acyl groups?
(A) Thiamine
pyrophosphate
(B) Lipomide
(C) ATP
(D) NADH
405. Which
one of the following cofactors must be utilized during the conversion of acetyl
CoA to malonyl CoA?
(A) TPP
(B) ACP
(C) NAD+
(D) Biotin
406. Which
one of the following enzymes requires a coenzyme derived from the
vitamin whose structure is shown below?
(A) Enoyl CoA
hydratase
(B)
Phosphofructokinase
(C)
Glucose-6-phosphatase
(D) Glucose-6-phosphate dehydrogenase
407. Coenzymes
derived from the vitamin shown below are required by enzymes
involved in the synthesis of which of the following?
(A) ATP
(B) UTP
(C) CTP
(D) NADH
408. Coenzymes
derived from the vitamin shown below are required by which of
the following enzymes?
(A) Lactate
dehydrogenase
(B) Glutamate dehydrogenase
(C) Pyruvate dehydrogenase
(D) Malate
dehydrogenase
409. All the
following are coenzymes except
(A) Ubiquinone
(B) CoA
(C) Pyruvate dehydrogenase
(D) Lipoic acid
410. Which of
the following is not a cofactor?
(A) Mg
(B) Iron
(C) Cu
(D) Methylcobalamine
411. All the
following compounds are members of the electron transport chain except
(A) Ubiquinone
(B) Carnitine
(C) NAD
(D) FAD
412. Thiamine
is essential for
(A) Pyruvate
dehydrogenase
(B) Isocitrate dehydrogenase
(C) Succinate
dehydrogenase
(D) Acetyl CoA
synthetase
413. Adenylate
cyclase is activated by
(A) Insulin
(B) Glucagon
(C)
Prostaglandin E1
(D) Ca2+
ions
414. Maximum
enzyme activity is observed at
(A) Acidic pH
(B) Neutral pH
(C) Basic pH
(D) Optimum pH
415. Which of
the following is known as bone forming enzyme?
(A) Alkaline phosphatase
(B) Acid
phosphatase
(C) Leucine
aminopeptidase
(D) γ-glutamyl
transpeptidase
416. Conversion
of pepsinogen to pepsin is
(A) Intra
molecular rearrangement
(B) Breaking of hydrogen bonds
(C) Covalent modification
(D)
Polymerisation
417. Which of
the following is not having an
apoenzyme and coenzyme?
(A) Lactate
dehydrogenase
(B) Succinate dehydrogenase
(C) Malate
dehydrogenase
(D) Pepsin
418. Pyruvate
dehydrogenase is a/an
(A) Isomerase
(B) Lyase
(C) Ligase
(D) Oxido reductase
419. Homogentisic
oxidase is an
(A) Oxidase
(B)
Monooxygenase
(C) Dioxygenase
(D) Anaerotic
dehydrogenase
420. Isocitrate
dehydrogenase can use__________ as a cofactor.
(A) NAD+
only
(B) NADP+
only
(C) NAD+ or NADP+
(D) FMN and FAD
421. The rate
of most enzyme catalysed reactions changes with pH. As the pH
increases, this rate
(A) reaches a
minimum, then increases
(B) reaches a maximum, then decreases
(C) increases
(D) decreases
422. A
substrate for the enzyme aldolase is
(A)
galactose-6-phosphate
(B) isocitric
acid
(C)
Glucose-1-phosphate
(D) Fructose 1, 6 diphosphate
423. Decarboxylation
of α-keto acids requires+
(A) Thiamine pyrophosphate, FAD, NAD
(B) Flavin mononucleotide+
(C) NADP
(D) NAD+
only
424. Coenzyme
A contains the vitamin:
(A) Riboflavin
(B) Pantothenic acid
(C) Pyridoxine
(D) Thiamine
425. Which of
the following is not a component
of coenzyme A?
(A) Adenylic
acid
(B) Pantothenic acid
(C) β
-mercaptoethylamine
(D) Deoxyadenylic acid
426. Malic
enzyme convers malic acid, in the presence of NADP+ to Pyruvic acid.
This
reaction is a/an
(A)
Decarboxylation
(B) Decarboxylation and Dehydrogenation
(C)
Dehydrogenation
(D) Oxidation
427. The
following reaction is characteristic of
what type of enzymes? 2H2O2 → 2H2O
+ O2
(A) Peroxides
(B) Catalase
(C)
Dehydrogenase
(D) Copper
containing oxidases
428. Of Which
warburg’s yellow enzyme
contains as a prosthetic group?
(A) Thiamine
pyrophosphate
(B) Biotin
(C) NAD+
(D) Riboflavin-5-phosphate
429. Dehydrogenases
utilize, as coenzymes, all
of the following except
(A) NAD+
(B) NADP+
(C) FAD
(D) FH4
430. Urea is
produced physiologically by the
action of the enzyme:
(A) Urease
(B) Glutaminase
(C) Arginase
(D) None of
these
431. Urease
is a
(A) Lyase
(B) Ligase
(C) Isomerase
(D) Hydrolase
432. Velocity
maximum for an enzyme at half
the substrate concentration gives
(A) The
molecular weight of the enzyme
(B) Km value
(C) Isoelectric
pH
(D) Pk value
433. Which of
the following amino acid has been shown as one of the active site of
phosphoglucomutase?
(A) Lysine
(B) Tyrosine
(C) Serine
(D) Histidine
434. The
inhibition of succinate dehydrogenase by malonate by
(A) Competitive inhibition
(B) Non-competitive inhibition
(C)
Uncompetitive inhibition
(D) Feedback
inhibition
435. Cobamide
coenzymes are
(A) Vitamin B1
(B) Riboflavin
(C) Pyridoxine
(D) Vitamin B12
436. The
isozyme CK-MB is specifically increased in the blood of patients who
had
(A) Skeletal
muscle disease
(B) Recent myocardial infarction
(C) Infective
hepatitis
(D) Myxoedema
437. FAD
containing enzyme, catalyzing
formation of α, β unsaturated fatty acyl CoA
derivative.
(A) Acyl CoA dehydrogenase
(B) Enoyl
hydrase
(C) β-OH acyl
CoA dehydrogenase
(D) Thiolase
438. Immobilized
enzymes:
(A)
Potentiation of activity
(B) Presentation of activity
(C) Preparation
of activity
(D) All of
these
439. This
catalyzes formation of CoA derivatives from fatty acid, CoA and ATP:
(A) Acyl CoA
dehydrogenase
(B) Enoyl
hydrase
(C) β-OH acyl
CoA dehydrogenase
(D) Thio kinase
440. Fructose
2, 3 bi phosphate is a powerful allosteric activator of
(A) Fructose 1,
6 diphosphatase
(B) Phosphofructokinase
(C) Hexokinase
(D)
Fructokinase
441. ‘Clearing
factor’ is
(A) Lipoprotein lipase
(B) Crotonase
(C) 7-dehydro
cholesterol
(D) β-sitosterol
442. Maltase
attacks only
(A) α-glucosides
(B)
β-glucosides
(C) Starch
(D) Dextrins
443. Pepsin
is
(A)
Exo-peptidase
(B) Endo-peptidase
(C) Carboxy
peptidase
(D) Amino
peptidase
444. An
enzyme in saliva which hydrolyzes
starch is
(A) Pepsinogen
(B) Chymotrysin
(C) α-Amylase
(D) Malate
445. If a
coenzyme is required in an enzyme reaction, the former usually has the
function of
(A) Acting as an acceptor for one of the cleavage products of the substrate
(B) Enhancing
the specificity of the apo enzyme
(C) Increasing
the number of receptor sites of the apo enzyme
(D) Activating
the substrate
446. The
Michaehis-Menten hypothesis:
(A) Postulates the formation of an enzyme substrate
complex
(B) Enables us
to calculate the isoelectric point of an enzyme
(C) States that
the rate of a chemical reaction may be independent of substrate concentration
(D) States that
the reaction rate is proportional to substrate concentration
447. Schardinger’s
enzyme is
(A) Lactate
dehydrogenase
(B) Xanthine dehydrogenase
(C) Uric
oxidase
(D) L amino
acid dehydrogenase
448. Tryptophan
pyrolase is currently known
as
(A) Tryptophan
deaminase
(B) Tryptophan dioxygenase
(C) Tryptophan
mono oxygenase
(D) Tryptophan
decarboxylase
449. An
enzyme which brings about lysis of
bacterial cell wall is
(A) Amylase
(B) Lysozyme
(C) Trypsin
(D) Lipase
450. Trypsin
has no action on
(A) Hemoglobin
(B) Albumin
(C) Histone
(D) DNA
451. Multiple
forms of the same enzymes are
known as
(A) Zymogens
(B) Isoenzymes
(C) Proenzymes
(D) Pre-enzymes
452. 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
453. An
allosteric enzyme influences the
enzyme activity by
(A) Competiting
for the catalytic site with the substrate
(B) Changing
the specificity of the enzyme for the substrate
(C) Changing the conformation of the enzyme by
binding to a site other than catalytic site
(D) Changing
the nature of the products formed
454. Which of
the following regulatory reactions involves a reversible covalent
modification of an enzyme?
(A) Phosphorylation of serine OH on the enzyme
(B) Allosteric
modulation
(C) Competitive
inhibition
(D)
Non-competitive inhibition
455. 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
456. 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
457. Which of
the following statements about an enzyme exhibiting allosteric kinetics
with cooperative interaction is false?
(A) A plot of
V-Vk [s] has a sigmaidal shape
(B) An
inhibitor may increase the apparent Km
(C) Line weaver
Bnrk plot is useful for determining Km and Vmax
(D) Removal of allosteric inhibitor may result in
hyperbolic V-S [s] plot
458. Pantothenic
acid acts on
(A) NADP
(B) NADPH
(C) FAD
(D) CoA
459. Vitamin
deficiency that causes fatty liver includes all except
(A) Vitamin E
(B) Pyridoxine
(C) Retionic acid
(D) Pantothenic
acid
460. 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
461. 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
462. ‘Lock’
and ‘Key’ model of enzyme action proposed by Fisher implies that
(A) The active
site is flexible and adjusts 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
463. In
competitive inhibition of enzyme action
(A) The
apparent Km is decreased
(B) The apparent Km is increased
(C) Vmax
is decreased
(D) Apparent
concentration of enzyme molecules decreased
464. 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
465. Enzymes
increase the rates of reactions
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
466. The most
useful test for the diagnosis of acute hemorrhagic pancreatitis during the
first few days is
(A) Urinary
lipase test
(B) Serum
calcium
(C) Urinary
amylase
(D) Serum amylase
467. The best
test for acute pancreatitis in the
presence of mumps is
(A) A
serological test for mumps
(B) Serum
amylase
(C) Urinary
amylase
(D) Serum lipase
468. The slow
moving fraction of LDH is typically increased in pancreas with
(A)
Cerebrovascular accidents
(B) Acute myocardial infarction
(C) Acute
pancreatitis
(D) Acute viral hepatits
469. Which of
the following enzyme typically elevated in alcoholism?
(A) Serum ALP
(B) Serum GOT
(C) Serum γ-GT
(D) Serum acid
phosphatase
470. Patients
with hepatocellular jaundice, as compared to those with purely obstruc-
tive jaundice tend to have
(A) Lower serum
ALP, LDH and AST activity
(B) Lower serum ALP, Higher LDH and AST activity
(C) Higher
serum ALP, LDH and AST activity
(D) Higher
serum ALP, Lower LDH and AST activity
471. If
results of the serum bilirubin, serum ALP, LDH and AST determinations suggest obstructive
jaundice, the best confirmatory test would be the estimation of
(A) Serum ALT
(B) Serum 5’ nucleotidase
(C) Serum
Pseudo cholinesterase
(D) None of
these
472. Which
enzyme estimation will be helpful in differentiating the elevated serum ALP
found in obstructive jaundice as well as bone
disorders?
(A) Serum AST
(B) Serum ALT
(C) Serum LDH
(D) Serum γ-GT
473. Cardiac
muscle contains which of the
following CK osoenzyme?
(A) BB only
(B) MM and BB
only
(C) MM, BB and
MB
(D) MM and MB only
474. Liver
and skeletol measle disorders are characterized by on disk proportionate
increase in which of the LDH isoenzyme fraction?
(A) LDH-1
(B) LDH-1 and
LDH-2
(C) LDH-3 and LDH-4
(D) LDH-2 and
LDH-3
(E) LDH-5
475. On the
third day following onset of acute myocardial infarction, which enzyme
estimation will have the best predictive value?
(A) Serum AST
(B) Serum CK
(C) Serum ALT
(D) Serum LDH
476. Serum
AST activity is not characteristically elevated as the result of
(A) Myocardial
infarction
(B) Passive congestion of liver
(C) Muscular
dystrophies
(D) Peptic ulcer
477. On which
day following acute myocardial infarction the estimation of serum AST will be
of greatest significance?
(A) First day
(B) Second day
(C) Third day
(D) Fourth day
478. In which
diseases of the following organs, isoenzymes LDH-1 and LDH-2 will be
released in plasma?
(A) Kidney,
R.B.C and Liver
(B) Heart, Kidney and R.B.C
(C) Heart,
Kidney and Liver
(D) Heart,
Lungs and Brain
479. Plasma
non-functional enzymes are
(A) totally
absent
(B) low
concentration in plastic
(C) important
for diagnosis of several disease
(D) All of these
480. Pyruvate
dehydrogenase contains all
except
(A) Biotin
(B) NAD
(C) FAD
(D) CoA
481. An
increase in LDH-5 enzyme is seen in
the following except
(A) Acute
hepatitis
(B) Muscular distrophies
(C) Breast
carcinoma
(D) Pulmonary embolism
482. Diastase
can be used for the hydrolysis can be used for the hydrolysis of
(A) Sucrose
(B) Starch
(C) Cellulose
(D) Maltose
483. Which of
the following statements is true?
(A) Enzymes
have names ending ase
(B) Enzymes are highly specific in their action
(C) Enzymes are
living organisms
(D) Enzymes get
activated on heating
484. Enzymes
activity is controlled by
(A) pH of the
solution
(B) Temperature
(C) Concentration of the enzyme
(D)
Concentration of the substrate (E)
All of these
485. Which of
the following is not true regarding enzymes?
(A) They
catalyze only a particular type of reaction
(B) They remain active even after
separation from the source
(C) They are destroyed after the completion of the
reaction they catalyse
(D) They are
irreversibly destroyed at high temperature
(E) Their
activity depends on the pH of the solution
486 The
number of enzymes known is about
(A) 10,000
(B) 100
(C) 50
(D) 26
487. Nicotine
present in tobacco is a/an
(A) Alkaloid
(B) Terpene
(C) Steroid
(D) Protein
488. The
poisonous alkaloid present in the oil
of hemlock is
(A) Cocaine
(B) Nicotine
(C) Quinine
(D) Morphine
489. Alkaloids
are usually purified by extraction with
(A) Ether
(B) Dil HCl
(C) NaOH
(D) Chloroform
490. The
number of N-MC groups in alkaloids
is best estimate with the help of
(A) HI
(B) H2SO4
(C) (CH3CO)2
CO
(D) CH3
Mg I
491. A
competitive inhibitor of an enzyme
(A) Increases Km without affecting Vmax
(B) Decreases Km
without affecting Vmax
(C) Increases Vmax
without affecting Km
(D) Decreases
both Vmax and Km
492. The Michaelis constant, Km is
(A) Numerically
equal to ½ Vmax
(B) Dependent
on the enzyme concentration
(C) Independent
of pH
(D) Numerically equal to the substrate concentration
that gives half maximal velocity
493. The rate
of an enzyme catalyzed reaction was measured using several substrate
concentrations that were much lower than Km,
the dependence of reaction velocity on substrate concentration can best be
described as
(A) Independent
of enzyme concentration
(B) A constant
fraction of Vmax
(C) Equal to Km
(D)
Proportional to the substrate concentration
494. The
presence of a non competitive inhibitor
(A) Leads to
both an increase in the Vmax of a reaction and an increase in Km
(B) Leads to a decrease in the observed Vmax
(C) Leads to a
decrease in Km and Vmax
(D) Leads to an
increase in Km without affecting Vmax
495. Which
one of the following statements is not characteristic of allosteric enzymes?
(A) They
frequently catalyze a committed step early in a metabolic pathway
(B) They are
often composed of subunits
(C) They follow Michaelis-Menten kinetics
(D) They
frequently show cooperativity for substrate binding
496. The
abnormal isoenzyme need not
(A) Be an oxidoreductase
(B) Have any coenzyme
(C) Require ATP
(D) Be
localized intracellularly
(E) Be a
catalyst
497. LDH
assays are most useful in diagnosing
diseases of the
(A) Heart
(B) Pancreas
(C) Brain
(D) Kidney
498. The
chemical forces that bind most coenzymes and substrates to enzymes
such as LDH are
(A) Hydrogen
bonds
(B) Peptide
bonds
(C) Coordinate
bonds
(D) Covalent bonds
499. How many
different proteins may be present in normal LDH?
(A) One
(B) Two
(C) Three
(D) Four
500. All the
isoenzymes function with the
coenzyme:
(A) NADP+
(B) FAD
(C) Lipoate
(D) NAD+
501. ‘Lock’
and ‘Key’ theory was proposed by
(A) Sorenson
(B) Fischer
(C) Mehler
(D) Sanger
502. Which of
the following forms part of a
coenzyme?
(A) Zn2+
(B) Lipase
(C) Vitamin B2
(D) Lysine
503. The
shape of an enzyme and consequently its activity can be reversibly altered from
moment to moment by
(A) Heat
(B) Amino acid
substrate
(C) Allosteric subunits
(D) Sulfur
substitutions
504. Which
one of the following regulatory actions involves a reversible covalent
modification of the enzyme?
(A) Phosphorylation of ser-OH on the enzyme
(B) Allosteric
modulation
(C) Competitive
inhibition
(D)
Non-competitive inhibition
505. An
enzyme is a
(A)
Carbohydrate
(B) Lipid
(C) Protein
(D) Nucleic
acid
506. An
enzyme promotes a chemical reaction
by
(A) Lowering the energy of activation
(B) Causing the release of heat which
acts as a primer
(C) Increasing
molecular motion
(D) Changing
the free energy difference between substrate and product
507. In most
metabolic pathways, all needed enzymes are arranged together in a
multienzyme complex within a
(A) Solution of
ATP
(B) Membrane
(C) Quanternary
protein
(D) Coenzyme
508. An
enzyme catalyzes the conversion of an aldose sugar to a ketose sugar would be
classified as one of the
(A)
Transferases
(B) Isomerases
(C) Oxido
reductases
(D) Hydrolases
509. The function
of an enzyme is to
(A) Cause chemical
reactions that would not otherwise take place
(B) Change the rates of chemical reactions
(C) Control the
equilibrium points of reactions
(D) Change the
directions of reactions
510. In which
of the following types of enzymes, water may be added to a C —C
double bond without breaking the bond?
(A) Hydrolase
(B) Hydratase
(C) Hydroxylase
(D) Oxygenase
511. Enzymes
increases the rate of reactions
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
512. The
active site of an enzyme is formed by
a few of the enzymes:
(A) R groups of
the amino acids
(B) Amino groups of the amino acids
(C) Carboxyl group of the amino acids
(D) Exposed
sulfur bonds
513. Allosteric
enzymes contain
(A) Multiple subunits
(B) Single
chain
(C) Two chains
(D) Three
chains
514. Isoenzymes
of lactate dehydrogenase are
useful for the diagnosis of
(A) Heart
disease
(B) Kidney
disease
(C) Liver
disease
(D) Both (A) and (C)
515. IUB had
divided enzymes into how many
classes?
(A) 6
(B) 5
(C) 8
(D) 4
516. The
first enzyme isolated, purified and crystallied from Jack bean (Canavalia) by
summer in 1926 was
(A) Urease
(B) Insulin
(C)
Ribonuclease
(D) Zymase
517. Who
suggested that enzymes are proteinaceous?
(A) Buchner
(B) Kuhne
(C) Sumner
(D) Pasteur
518. Feedback
inhibition of enzyme action is affected by
(A) Enzyme
(B) Substrate
(C) End products
(D) None of
these
519. The
enzyme that converts glucose to glucose-6-phosphate is
(A) Phosphatase
(B) Hexokinase
(C)
Phosphorylase
(D) Glucose
synthetase
520. Enzymes
are required in traces because they
(A) Have high
turnover number
(B) Remain
unused at the end of reaction and are re used
(C) Show
cascade effect
(D) All correct
521. An
organic substance bound to an enzyme and essential for the activity of
enzyme is called
(A) Holoenzyme
(B) Apoenzyme
(C) Coenzyme
(D) Isoenzyme
522. Enzyme
catalysed reactions occur in
(A) Pico
seconds
(B) Micro
seconds
(C) Milli seconds
(D) None of
these
523. An
enzyme can accelerate a reaction up to
(A) 1010 times
(B) 101
times
(C) 10100
times
(D) 10
times
524. In
plants, enzymes occur in
(A) Flowers
only
(B) Leaves only
(C) All living cells
(D) Storage
organs only
525. Zymogen
is a
(A) Vitamin
(B) Enzyme precursor
(C) Modulator
(D) Hormone
526. Cofactor
(Prosthetic group) is a part of holoenzyme, it is
(A) Inorganic
part loosely attached
(B) Accessory non-protein substance attached firmly
(C) Organic
part attached loosely
(D) None of
these
527. A
protein having both structural and
enzymatic traits is
(A) Myosin
(B) Collagen
(C) Trypsin
(D) Actin
528. Enzymes
are different from catalysts in
(A) Being proteinaceous
(B) Not used up in reaction
(C) Functional
at high temperature
(D) Having high
rate of diffusion
529. Enzymes,
vitamins and hormones are
common in
(A) Being
proteinaceous
(B) Being
synthesized in the body of organisms
(C) Enhancing
oxidative metabolism
(D) Regulating metabolism
530. Dry
seeds endure higher temperature
than germinating seeds as
(A) Hydration is essential for making enzymes sensitive
to temperature
(B) Dry seeds
have a hard covering
(C) Dry seeds
have more reserve food
(D) Seedlings
are tender
531. Coenzymes
FMN and FAD are derived
from vitamin
(A) C
(B) B6
(C) B1
(D) B2
532. Template/lock
and key theory of enzyme
action is supported by
(A) Enzymes
speed up reaction
(B) Enzymes occur
in living beings and speed up certain reactions
(C) Enzymes
determine the direction of reaction
(D) Compounds similar to substrate inhibit enzyme
activity
533. Combination of apoenzyme
and
coenzyme produces
(A) Prosthetic
group
(B) Holoenzyme
(C) Enzyme
substrate complex
(D) Enzyme
product complex
534. Enzyme
inhibition caused by a substance resembling substrate molecule is
(A) Competitive inhibition
(B) Non-competitive inhibition
(C) Feedback
inhibition
(D) Allosteric
inhibition
535. An
enzyme brings about
(A) Decrease in
reaction time
(B) Increase in reaction time
(C) Increase in
activation energy
(D) Reduction in activation energy
536. Feedback
inhibition of enzyme is influenced by
(A) Enzyme
(B) External
factors
(C) End product
(D) Substrate
537. Coenzyme
is
(A) Often a vitamin
(B) Always an
inorganic compound
(C) Always a
protein
(D) Often a
metal
538. Genetic
engineering requires enzyme:
(A) DNA ase
(B) Amylase
(C) Lipase
(D) Restriction endonuclease
539. Which is
not true about inorganic catalysts and enzymes?
(A) They are
specific
(B) Inorganic catalysts require specific not needed
by enzymes
(C) They are
sensitive to pH
(D) They speed
up the rate of chemical reaction
540. Key and
lock hypothesis of enzyme action
was given by
(A) Fischer
(B) Koshland
(C) Buchner
(D) Kuhne
541. An
example of feedback inhibition is
(A) Allosteric inhibition of hexokinase by
glucose-6-phosphate
(B) Cyanide
action on cytochrome
(C) Sulpha drug
on folic acid synthesizer bacteria
(D) Reaction between
succinic dehydrogenase and succinic acid
542. Feedback
term refers to
(A) Effect of
substrate on rate of enzymatic reaction
(B) Effect of end product on rate reaction
(C) Effect of
enzyme concentration on rate of reaction
(D) Effect of
external compound on rate of reaction
543. Allosteric
inhibition
(A) Makes
active site unifit for substrate
(B) Controls
excess formation and end product
(C) Both (A) and (B)
(D) None of
these
544. The
ratio of enzyme to substrate mole-
cules can be as low as
(A) 1 : 100,000
(B) 1 :
500,000
(C) 1 :
10,000
(D) 1 :
1,000
545. Vitamin
B2 is component of coenzyme:
(A) Pyridoxal
phosphate
(B) TPP
(C) NAD
(D) FMN/FAD
546. Km
value of enzyme is substrate concentration at
(A) ½ Vmax
(B) 2 Vmax
(C) ½ Vmax
(D) 4 Vmax
547. Part of
enzyme which combines with non-protein part to form functional enzyme is
(A) Apoenzyme
(B) Coenzyme
(C) Prosthetic group
(D) None of
these
548. Who got
Nobel Prize in 1978 for working on enzymes?
(A) Koshland
(B) Arber and
Nathans
(C) Nass and
Nass
(D) H.G.
Khorana
549. Site of
enzyme synthesis in a cell is
(A) Ribosomes
(B) RER
(C) Golgi
bodies
(D) All of
these
550. The
fruit when kept is open, tastes bitter after 2 hours because of
(A) Loss of
water from juice
(B) Decreased
concentration of fructose in juice
(C)
Fermentation by yeast
(D) Contamination by bacterial enzymes
551. Hexokinase
(Glucose + ATP → Glucose-6-P + ADP) belongs to the category:
(A)
Transferases
(B) Lysases
(C) Oxidoreductases
(D) Isomerases
552. Which
enzyme is concerned with transfer of electrons?
(A) Desmolase
(B) Hydrolase
(C)
Dehydrogenase
(D)
Transaminase
553. The best
example of extracellular enzymes (exoenzyme) is
(A) Nucleases
(B) Digestive
enzymes
(C) Succinic dehydrogenase
(D) None of
these
554. Which
mineral element controls the activity of Nitrate reductase ?
(A) Fe
(B) Mo
(C) Zn
(D) Ca
555. Name the
enzyme that acts both as carboxylase at one time and oxygenase
at another time.
(A) PEP
carboxylase
(B) RuBP carboxylase
(C) Carbonic
anyhdrase
(D) None of
these
556. A
metabolic pathways is a
(A) Route taken
by chemicals
(B) Sequence of enzyme facilitated chemical reactions
(C) Route taken
by an enzyme from one reaction to another
(D) Sequence of
origin of organic molecules
557. The
energy required to start an enzymatic reaction is called
(A) Chemical
energy
(B) Metabolic
energy
(C) Activation energy
(D) Potential
energy
558. Out of
the total enzymes present in a cell, a mitochondrion alone has
(A) 4%
(B) 70%
(C) 95%
(D) 50%
559. Creatine
phosphokinase isoenzyme is a marker for
(A) Kidney
disease
(B) Liver
disease
(C) Myocardial infarction
(D) None of
these
560. Which
inactivates an enzyme by occupying its active site?
(A) Competitive inhibitor
(B) Allosteric
inhibitor
(C)
Non-competitive inhibitor
(D) All of
these
561. Which
one is coenzyme?
(A) ATP
(B) Vitamin B
and C
(C) CoQ and CoA
(D) All of these
562. The
active site of an enzyme is formed by
(A) R group of amino acids
(B) NH2
group of amino acids
(C) CO group of
amino acids
(D) Sulphur
bonds which are exposed
563. Carbonic
anhydrase enzyme has maximum turn over number (36 million). Min-
imum turn over number for an enzyme:
(A) DNA
polymerase
(B) Lysozyme
(C) Penicillase
(D) Lactase
dehydrogenase
564. In cell,
digestive enzymes are found mainly in
(A) Vacuoles
(B) Lysosomes
(C) Ribosomes
(D) Lomasomes
565. Substrate
concentration at which an enzyme attains half its maximum velocity
is
(A) Threshold
value
(B) Michaelis-Menton constant
(C)
Concentration level
(D) None of
these
566. Which
enzyme hydrolyses starch?
(A) Invertase
(B) Maltase
(C) Sucrase
(D) Diastase
567. Enzymes
functional in cell or mitochondria
are
(A) Endoenzymes
(B) Exoenzymes
(C) Apoenzymes
(D) Holoenzymes
568. The
enzymes present in the membrane of
mitochondria are
(A) Flavoproteins and cytochromes
(B) Fumarase
and lipase
(C) Enolase and
catalase
(D) Hexokinase
and zymase
569. A
mitochondrial marker enzyme is
(A) Aldolase
(B) Amylase
(C) Succinic dehydrogenase
(D) Pyruvate
dehydrogenase
570. The
enzyme used in polymerase chain
reaction (PCR) is
(A) Taq
polymerase
(B) RNA
polymerase
(C)
Ribonuclease
(D) Endonuclease
571. Which of
the following is a microsomal enzyme inducer?
(A)
Indomethacin
(B) Clofibrate
(C) Tolbutamide
(D) Glutethamide
572. Identify
the correct molecule which controls the biosynthesis of proteins in
living organisms.
(A) DNA
(B) RNA
(C) Purines
(D) Pyrimidines
573. The tear
secretion contains an antibacterial enzyme known as
(A) Zymase
(B) Diastase
(C) Lysozyme
(D) Lipase
574. Identify
one of the canbonic anhydrase inhibitor that inhibit only luminal
carbonic anhydrase enzyme.
(A)
Methazolamide
(B) Acetazolamide
(C)
Dichlorphenamide
(D) Benzolamide
575. Group
transferring Co-enzyme is
(A) CoA
(B) NAD+
(C) NADP+
(D) FAD+
576. The
co-enzyme containing an automatic hetero ring in the structure is
(A) Biotin
(B) TPP
(C) Sugar Phosphate
(D) Co-enzyme
577. The
example of hydrogen transferring Co-enzyme is:
(A) B6-PO4
(B) NADP+
(C) TPP
(D) ATP
578. Enzyme
catalyzed hydrolysis of proteins produces amino acid of the form
(A) D
(B) DL
(C) L
(D) Racemic
579. Transaminase
activity needs the Co-
enzyme:
(A) ATP
(B) B6-PO4
(C) FADT
(D) NAD+
580. The
biosynthesis of urea occurs mainly in
the liver:
(A) Cytosol
(B) Mitochondria
(C) Microsomes
(D) Nuclei
581. Bile
salts make emulsification with fat for the action of
(A) Amylose
(B) Lipase
(C) Pepsin
(D) Trypsin
582. All of
the following compounds are intermediates of TCA cycle except
(A) Maleate
(B) Pyruvate
(C)
Oxaloacetate
(D) Fumarate
583. In
conversion of lactic acid to glucose, three reactions of glycolytic pathway are
circumvented, which of the following enzymes do not
participate?
(A) Pyruvate
carboxylase
(B) Phosphoenol pyruvate carboxy kinase
(C) Pyruvate
kinase
(D)
Glucose-6-phosphatase
584. In the
normal resting state of human most of the blood glucose burnt as fuel is
consumed by
(A) Liver
(B) Brain
(C) Adipose
tissue
(D) Muscles
585. A
regulator of the enzyme glucogen synthase is
(A) Citric Acid
(B) Pyruvate
(C) Glucose-6-PO4
(D) GTP
586. A
specific inhibitor for succinate dehydro-
genase is
(A) Arsenite
(B) Malonate
(C) Citrate
(D) Fluoride
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