Term End Examination - November 2011

Course :
Time

BIY207 - Enzymology

Slot: F2

: Three Hours

Max.Marks:100
PART A (25 X 1 = 25 Marks)
Answer ALL the Questions

Fill in the blanks

1.

Transition state stabilization hypothesis of enzymes was proposed by------------

2.

A coenzyme required for one carbon transfer reactions is -----------------

3.

The metal ion present in the nitrogenase enzyme is -------------------

4.

The amino acids present in the active site of lysozyme is------------------

5.

Allopurinol is a competitive inhibitor for the enzyme -------------------Choose the best answer

6.

Which of the following properties is not characteristic of enzymes?

(a) Stabilize transition states
(b) Alter the equibrium distribution of substrate and product.
(c) Reduce the activation energy

7.

(d) Often use acid-base catalysis

In general, an enzyme increases the reaction rate over an uncatalyzed reaction by:
(a) 106 to 1012 times (b) 1012 to 1018 times (c) 1020 to 1026 times (d) 1021 to 1036 times

8.

The class of enzyme that catalyzes the following reaction is:

COOH 3+N

(a) Lyase
9.

CH

COO-

COO-

(CH2)2

CH2

COO-

COO-

COO

(b) Ligase

(c) Transferase

CH2

COOH3+N

CH
(CH2) 2

COO-

(d) Oxidoreductase

Among the following which is the wrong pair

(a) Transferase - kinase
(b) Lyase - decarboxylase
(c) Hydrolase - pepsin
(d) Oxidoreductase - epimerase
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10.

11.

The low value of Km indicates

(a) High enzyme activity
(c) No effect on reaction

Which of the following is defined as the "turnover number for an enzyme?"

(a) kcat

12.

(b) High substrate affinity of enzyme

(d) Low affinity of enzyme with substrate

(b) kcat/Km

(c) Km/kcat

(d) kcat x Km

You have obtained the following data for enzyme activity measured in the presence of
an inhibitor, I. Identify the type of inhibition.
(a) Competitive
(b) Noncompetitive
(c) Uncompetitive
(d) Cannot be determined from the information given

13.

Which type of reversible enzyme inhibitor binds to both the free enzyme and the ES
complex?
(a) Noncompetitive (b) uncompetitive (c) competitive (d) Two of the above

14.

Which of the following amino acids is most ideally suited to participate in acid-base
catalysis near neutral pH?
(a) Aspartate
(b) Glutamate
(c) Lysine
(d) Histidine

15.

In enzyme catalysis, the proximity effect refers to:

(a) The effective increase in concentration of reacting species by binding to the active
site
(b) The approach of a substrate to an enzyme
(c) Close contacts made by neighboring enzyme monomers
(d) The increase in energy produced by bringing two atoms closer than their van der
waals distance

16.

A common feature of all serine proteases is:

(a) Cleavage of proteins on the carboxyl side of serine residues
(b) Tight binding of p-toluenesulfonyl phenylalanine chloromethyl ketone (TPCK)
(c) Autocatalytic activation of zymogen precursors
(d) The presence of a ser-his-asp catalytic triad at the active site

17.

A kidney homogenate enzyme preparation catalyzes a reaction at a velocity of 10.55

moles x litre -1 min -1. When the reaction is inhibited by a non-competeitive inhibitor
the velocity is reduced to 6.22 moles x litre -1 min -1. What is the degree of inhibition
caused by the non-competeitive inhibitor?
(a) 41.5%

(b) 58.9%

(c) 69.6%

(d) 20.7%

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18.

19.

In chymotrypsin, the tetrahedral substrate intermediate is stabilized by:

(a) His-57

(b) Ser-195

(c) Neighboring backbone amine hydrogens

(d) All of the above

Phosphorylation is a common means of regulating protein activity. Which of the

following amino acids are typically phosphorylated in proteins regulated by kinases?
(a) Serine

20.

(b) Tyrosine

(c) Threonine

(d) All of the above

Allosteric effectors:
(a) Convert the enzyme either to the R or the T state
(b) Typically bind to sites distant from the active site of an enzyme
(c) Can be very different in structure than the substrates of the enzyme
(d) Induce a conformational change in the protein to alter its activity
(e) All of the above

21.

In a mixture of the five proteins listed below, which should elute second in sizeexclusion (Gel filtration) chromatography?
(a) Cytochrome c

MW = 13 kDa

(c) Ribonuclease A MW = 13.7 kDa

(e) Serum albumin
22.

(d) RNA polymerase MW = 450 kDa

MW = 68.5 kDa

1 Katal is equal to
(a) 6 x 107 IU

23.

(b) Immunoglobulin G MW =145 kDa

(b) 9 x 107 IU

(c) 8 x 107 IU

(d) 7.5 x 107 IU

The specific activity of an enzyme is

(a) The amount of enzyme that produces one mole of product per second under
standard conditions
(b)The activity of an enzyme in relation to a standard preparation of the enzyme
(c)The number of enzyme units per milligram of enzyme protein
(d) The activity of an enzyme in the presence of its preferred substrate

24.

Liver and skeletal muscle disorders are characterized by a disproportionate 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-3 and LDH-5

25.

The purity of an enzyme at various stages of purification is best measured by:

(a) Total protein (b) Total enzyme activity (c) Specific activity of the enzyme
(d) Percent recovery of protein

(e) Percent recovery of the enzyme

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PART B (5 X 5 = 25 Marks)
Answer any FIVE Questions
26.

Enzymes act as catalysts by lowering the activation energy. Explain this statement
using reaction coordinate diagram.

27.

Explain the lock and key model and induced fit model for enzyme substrate interaction.

28.

How will you prove that Km is the substrate concentration at half-maximal velocity?

29.

When comparing the activity of an enzyme toward several structurally-related

substrates why is the value kcat/Km used to determine the "best" substrate, rather than
kcat or Km alone?

30.

A cancer patient is treated with methotrexate. Which enzyme is probable target for this
drug? What will be the action of the drug on that enzyme? Explain with suitable
chemical reaction.

31.

Explain the regulation of glycogen phosphorylase activity by the covalent modification

of the functional group.

32.

What is compartmentalization? Give some examples.

33.

Tabulate therapeutic enzymes and the corresponding diseases cured.

PART C (5 X 10 = 50 Marks)
Answer any FIVE Questions

34.

Give an account of six major classes of enzymes and explain reaction catalyzed by
each class with suitable examples.

35.

Explain different types of reversible enzyme inhibition and show the Km and Vmax
change using Lineweaver Burk plot.

36.

What are serine proteases? Explain the mechanism of action of serine protease using
chymotrypsin as an example.

37.

What are the advantages of immobilized enzymes over free enzymes? Discuss the
applications of immobilized enzymes?

38.

Describe the role of ion exchange chromatography and two dimensional gel
electrophoresis in enzyme purification.

39.

What are isoenzymes? Give four important examples of isoenzymes? Explain the
clinical significance (usage) of LDH isoenzymes.

40.

Describe the various industrial uses of enzymes.

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