Concepts in Biochemistry, 2e, Chapter 4

1. Amino acids are the building blocks of proteins. There are 20 amino
acids used in proteins. Fill in the blanks to describe the side-chain
properties of various amino acids. __________ is the only amino acid
that does not have a carbon atom in its side chain. The only cyclic
amino acid is called __________. __________ has a hydrophobic
side chain characterized by four carbons that are branched in the
middle. The amino acid that has a pKa around 6 is called
__________. The only amino acid with a two-ringed side chain is
__________.

Answer:

2. At physiological pH, amino acids are zwitterions. Which of the

following is a zwitterion?

1
 A. A
B. B
C. C
D. D

3. Some amino acids have ionizable side chains. Which amino acid
would have this titration curve?

A. Tyrosine
B. Aspartate
C. Cysteine

2
 D. Glycine
E. Lysine

4. Amino acids are linked together in proteins by __________ bonds.

This peptide bond formation reaction results in the loss of a
__________ molecule, which makes this a condensation reaction.
The amino acids that make up a protein are numbered from the ___
terminus to the ___ terminus. The protein size in Daltons can be
determined by multiplying the number of amino acids by ___, the
average size of an amino acid.

Answer:

5. Which of the following definitions are not properly matched with the
respective proteins?
A. Amylase: Transport/storage protein
B. Collagen: Structural protein
C. Antibody: Immune system molecule
D. Hemoglobin: Transport protein
E. Actin: Required for muscle contraction

6. Additional chemical groups such as small organics or metals attached

to proteins are called:
A. Subunit
B. -chain

3
 C. Residue
D. Prosthetic groups
E. Heme

7. The primary structure of a protein is its:

A. Shape
B. Sequence
C. Size
D. Charge

8. The secondary structure is a regularly repeating structure such as:

A. Collagen helix
B. Disulfide bond
C. -helix
D. All of the above

9. The tertiary structure of a protein refers to the:

A. Three connected residues of a protein
B. Volume of protein
C. Protein elasticity
D. Interaction of secondary structures to form a compact unit

10. A protein's quaternary structure refers to:

4
 A. Allosterism
B. Two or more polypeptide chains forming a multisubunit
structure
C. Disulfide bond
D. Extended chain

11. To determine the sequence of a protein, several methods may be

used. The preferred method, which labels and releases the N-
terminal residue, is called:
A. Sanger method
B. Ninhydrin reaction
C. Edman degradation
D. CNBr cleavage

12. In order to study the characteristics of a protein, it is first necessary

to isolate and purify the protein. Most of the methods employed
involve isolating a protein based on its charge (as in __________
chromatography), its size, (as in __________ chromatography), or
by selecting specific binding properties ( __________
chromatography). To visualize the purity of a protein solution
__________ is used, wherein a protein is applied to a gel that is
then subjected to an electric field.

Answer:

5
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the test.

Grade the Test

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correct) The questions marked with symbol have not

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 been graded.
Responses to questions are indicated by the
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1. Amino acids are the building blocks of proteins. There are 20

amino acids used in proteins. Fill in the blanks to describe the
side-chain properties of various amino acids. __________ is the
only amino acid that does not have a carbon atom in its side
chain. The only cyclic amino acid is called __________.
__________ has a hydrophobic side chain characterized by four
carbons that are branched in the middle. The amino acid that has a
pKa around 6 is called __________. The only amino acid with a
two-ringed side chain is __________.

YOUR ANSWER:

The suggested answer is glycine, proline, isoleucine, histidine,

tryptophan

2 At physiological pH, amino acids are zwitterions. Which of the

. following is a zwitterion?

A. A
B. B
7
 C. C
D. D

3. Some amino acids have ionizable side chains. Which amino

acid would have this titration curve?

A. Tyrosine
B. Aspartate
C. Cysteine
D. Glycine
E. Lysine

4. Amino acids are linked together in proteins by __________

bonds. This peptide bond formation reaction results in the loss of
a __________ molecule, which makes this a condensation
reaction. The amino acids that make up a protein are numbered
from the ___ terminus to the ___ terminus. The protein size in

8
 Daltons can be determined by multiplying the number of amino
acids by ___, the average size of an amino acid.

YOUR ANSWER:

The suggested answer is peptide, water, N, C, 110

5. Which of the following definitions are not properly matched

with the respective proteins?
A. Amylase: Transport/storage protein
B. Collagen: Structural protein
C. Antibody: Immune system molecule
D. Hemoglobin: Transport protein
E. Actin: Required for muscle contraction

6. Additional chemical groups such as small organics or metals

attached to proteins are called:
A. Subunit
B. -chain
C. Residue
D. Prosthetic groups
E. Heme

7. The primary structure of a protein is its:

A. Shape

9
 B. Sequence
C. Size
D. Charge

8. The secondary structure is a regularly repeating structure such

as:
A. Collagen helix
B. Disulfide bond
C. -helix
D. All of the above

9. The tertiary structure of a protein refers to the:

A. Three connected residues of a protein
B. Volume of protein
C. Protein elasticity
D. Interaction of secondary structures to form a compact unit

10. A protein's quaternary structure refers to:

A. Allosterism
B. Two or more polypeptide chains forming a multisubunit
structure
C. Disulfide bond
D. Extended chain

10
 11. To determine the sequence of a protein, several methods may
be used. The preferred method, which labels and releases the
N-terminal residue, is called:
A. Sanger method
B. Ninhydrin reaction
C. Edman degradation
D. CNBr cleavage

12. In order to study the characteristics of a protein, it is first

necessary to isolate and purify the protein. Most of the methods
employed involve isolating a protein based on its charge (as in
__________ chromatography), its size, (as in __________
chromatography), or by selecting specific binding properties (
__________ chromatography). To visualize the purity of a
protein solution __________ is used, wherein a protein is
applied to a gel that is then subjected to an electric field.

YOUR ANSWER:

The suggested answer is ion-exchange, gel, affinity,

electrophoresis

Retake Test

Concepts in Biochemistry, 2e, Chapter 5

1. What determines the tertiary structure of a protein?

11
 A. -helices
B. -sheets
C. Primary structure
D. Hydrophobic interactions

2. Amino acids are held together in proteins by peptide bonds. Which of

the following is true of a peptide bond?
A. Planar
B. Partial double-bond character
C. Rigid
D. trans configuration
E. All of the above

3. Proteins have regularly repeating structures called secondary

structures. One of these is an -helix. Which of the following are true
of an -helix?
th th
A. H bonds between C=O of the n amino acid and N-H of n+4
amino acid.
B. L-amino acids favor a right-handed -helix.
C. Proline disrupts an -helix
D. An -helix contains3.6 amino acid residues per turn.
E. All of the above

4. Another secondary structure is a -sheet. Which statements are true

of - sheets?
12
 A. -sheets exist in either parallel (both N  C) directions; not in
antiparallel (one C  N and one N  C) directions.
B. -sheets contain almost no alanine or glycine residues.
C. H bonds are formed between intrachain and interchain amino
acid side chains.
D. The size and charge of R group side chains is unimportant.

5. Bends or loops are considered to be non-regular secondary structures

because they do not repeat. Which of the following is true of bends?
A. Bends do not reverse the direction of a polypeptide chain.
B. Bends connect regions of -helixes and -sheets.
C. Glycine and proline are absent from bends.
D. Bends are usually found at the C terminus.

6. Fill in each blank with the letter that matches the described secondary
structure.

 ___




13
 Answer:

7. Collagen, a major component of skin and bone, is a fibrous protein

with repeating units of Pro-Gly-X or Hyp-Gly-X. Collagen has
strength because the structure is:
A. Web like
B. Three interlaced helices forming a rope
C. An -helix
D. A -sheet
E. A -barrel

8. Proteins must fold into their final structures to be functional. Which

of the following statements are not true?
A. Protein tertiary structure is determined by the primary
sequence.
B. Hydrophobic amino acids are buried in the interior.
C. Structural motifs such as  or  act as seeds around which
the rest of the protein folds.
D. Helper proteins called chaperones may assist protein folding.
E. Folding begins with disulfide bond formation.

9. Hemoglobin is the O2 carrier in the blood. It is made up of 4

polypeptide chains. Each chain contains the heme, which is a
prosthetic group containing Fe held in place by 4 Nitrogen atoms.
Which of the following is a true statement:
14
 A. O2 binding is achieved by the heme groups of hemoglobin.
B. A sigmoidal curve is characteristic of uncooperative binding.
C. Allosteric interactions are driven by a difference in charge of
nearby molecules.
D. Increased O2 binding to hemoglobin at low pH describes the
Bohr effect.
E. Sickle cell anemia has no effect on a patient's hemoglobin.

10. Hair contains the fibrous protein  keratin. How does a permanent
wave (perm) change the shape of hair?
A. Hair fibers are stacked.
B. -keratin is converted from the "soft" to "hard" form.
C. Disulfide bonds are broken and reformed.
D. Hair is made water-soluble.

11. The salt-tolerant bacteria Halobacterium halobium contains the

protein bacteriorhodopsin in its cell membrane. Bacteriorhodopsin
consists of a bundle of -helical rods. How does this protein allow
H. halobium to live in water with a high salt concentration?
A. Bacteriorhodopsin turns the cell purple.
B. Bacteriorhodopsin acts as a proton channel in the membrane.
C. Bacteriorhodopsin forms salt crystals.
D. Bacteriorhodopsin acts as an O2 carrier.
E. All of the above

15
 This is the end of the test. When you have completed all the
questions and reviewed your answers, press the button below to grade
the test.

Grade the Test

The questions marked with symbol have not

0% (0 out of 10 been graded.
correct) Responses to questions are indicated by the
symbol.

1. What determines the tertiary structure of a protein?

A. -helices
B. -sheets
C. Primary structure
D. Hydrophobic interactions

2. Amino acids are held together in proteins by peptide bonds.

Which of the following is true of a peptide bond?
A. Planar
B. Partial double-bond character
C. Rigid
D. trans configuration
E. All of the above

16
3. Proteins have regularly repeating structures called secondary
structures. One of these is an -helix. Which of the following
are true of an -helix?
A. H bonds between C=O of the nth amino acid and N-H of
n+4th amino acid.
B. L-amino acids favor a right-handed -helix.
C. Proline disrupts an -helix
D. An -helix contains3.6 amino acid residues per turn.
E. All of the above

4. Another secondary structure is a -sheet. Which statements are

true of - sheets?
A. -sheets exist in either parallel (both N  C) directions;
not in antiparallel (one C  N and one N  C) directions.
B. -sheets contain almost no alanine or glycine residues.
C. H bonds are formed between intrachain and interchain
amino acid side chains.
D. The size and charge of R group side chains is unimportant.

5. Bends or loops are considered to be non-regular secondary

structures because they do not repeat. Which of the following is
true of bends?
A. Bends do not reverse the direction of a polypeptide chain.
B. Bends connect regions of -helixes and -sheets.
C. Glycine and proline are absent from bends.
D. Bends are usually found at the C terminus.

17
6 Fill in each blank with the letter that matches the described
. secondary structure.

 ___




YOUR ANSWER:

The suggested answer is D, A, C, B

7. Collagen, a major component of skin and bone, is a fibrous

protein with repeating units of Pro-Gly-X or Hyp-Gly-X.
Collagen has strength because the structure is:
A. Web like
B. Three interlaced helices forming a rope
C. An -helix
D. A -sheet

18
 E. A -barrel

8. Proteins must fold into their final structures to be functional.

Which of the following statements are not true?
A. Protein tertiary structure is determined by the primary
sequence.
B. Hydrophobic amino acids are buried in the interior.
C. Structural motifs such as  or  act as seeds around
which the rest of the protein folds.
D. Helper proteins called chaperones may assist protein
folding.
E. Folding begins with disulfide bond formation.

9. Hemoglobin is the O2 carrier in the blood. It is made up of 4

polypeptide chains. Each chain contains the heme, which is a
prosthetic group containing Fe held in place by 4 Nitrogen
atoms. Which of the following is a true statement:
A. O2 binding is achieved by the heme groups of hemoglobin.
B. A sigmoidal curve is characteristic of uncooperative
binding.
C. Allosteric interactions are driven by a difference in charge
of nearby molecules.
D. Increased O2 binding to hemoglobin at low pH describes
the Bohr effect.
E. Sickle cell anemia has no effect on a patient's hemoglobin.

19
 10. Hair contains the fibrous protein  keratin. How does a
permanent wave (perm) change the shape of hair?
A. Hair fibers are stacked.
B. -keratin is converted from the "soft" to "hard" form.
C. Disulfide bonds are broken and reformed.
D. Hair is made water-soluble.

11. The salt-tolerant bacteria Halobacterium halobium contains

the protein bacteriorhodopsin in its cell membrane.
Bacteriorhodopsin consists of a bundle of -helical rods. How
does this protein allow H. halobium to live in water with a
high salt concentration?
A. Bacteriorhodopsin turns the cell purple.
B. Bacteriorhodopsin acts as a proton channel in the
membrane.
C. Bacteriorhodopsin forms salt crystals.
D. Bacteriorhodopsin acts as an O2 carrier.
E. All of the above

Retake Test

20
ENZYMES

21
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

4. A Holoenzyme is
(A) Functional unit (B) Apo enzyme
(C) Coenzyme (D) All of these

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

22
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
23
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

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

23. An inducer is absent in the type of enzyme:

(A) Allosteric enzyme
(B) Constitutive enzyme
(C) Co-operative enzyme
(D) Isoenzymic enzyme

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
24
(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
(E) 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
25
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

26
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
27
(C) Biotin
(D) CoA

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

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

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
28
59. LDH1 and LDH2 are elevated in
(A) Myocardial infarction
(B) Liver disease
(C) Kidney disease
(D) Brain disease

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

29
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

70. The substrate for amylase is

(A) Cane sugar (B) Starch
(C) Lactose (D) Ribose

89. Lineweaver – Burk double reciprocal plot

is related to
(A) Substrate concentration
(B) Enzyme activity
(C) Temperature
(D) Both (A) and (B)

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

130. Allosteric activator of glycogen synthase

is
(A) Glucose (B) Glucose-6-Phosphate
(C) UTP (D) Glucose-1-phosphate

133. Characteristic features of active site are

(A) Flexible in nature (B) Site of binding
(C) Acidic (D) Both (A) and (B)
30
278. Which of the following is a substratespecific
enzyme?
(A) Hexokinase (B) Thiokinase
(C) Lactase (D) Aminopeptidase

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

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
31
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
32
(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
33
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

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

34
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 covalent

modification 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

317. Lactate dehydrogenase is a

(A) Monomer (B) Dimer
(C) Tetramer (D) Hexamer

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320. Creatine kinase is present in all of the
following except
(A) Liver (B) Myocardium
(C) Muscles (D) Brain

3
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

36
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

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332. Different isoenzymes of an enzyme have
the same
(A) Amino acid sequence
(B) Michaelis constant
(C) Catalytic activity
(D) All of these

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

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