B.Sc. II Biotechnology (Semester IV) (CGPA) Examination, 2018
BIOENERGETICS AND ENZYMOLOGY
Day and Date Tuesday, 8-5-2018 Max. Marks 70
Time 10.30 a.m. to 1.00 p.m.
Instructions All questions carry equal marks.
Figures to right indicate full marks.
Draw neat and labeled diagrams.
1. Rewrite the following sentences by using correct alternative. 14
Entropy of a system is measure of its
hardness softness
randomness spontaneity
According to second law of thermodynamics, the of a
system always increases.
free energy velocity
enthalpy entropy
The system can exchange both energy and matter with its
surroundings.
open closed
isolated thermodynamic
is the carbon carbon bond forming reaction among esters in
presence of a strong base.
Isomerization Claisen condensation
Elimination Aldol condensation
The tendency of a chemical species to acquire electrons is its
potential.
electron reduction oxidation action
The more is the reduction potential, greater is the species
affinity for electrons and tendency to be reduced.
negative positive equilibrium steady
The nonprotein part covalently bound to the enzyme is the
holoenzyme apoenzyme
prosthetic group ribozyme
In inhibition of enzymes, the inhibitor binds to the site other
than active site of an enzyme.
competitive noncompetitive
uncompetitive irreversible
Abzymes are the antibodies with catalytic activity and also known as

immunocatalysts globular enzymes
catmabs interferons
10) Ribozymes are the molecules capable of catalyzing specific
biochemical reactions.
DNA RNA protein ribosome
11) Lactate dehydrogenase is observed in isomeric forms in
mammals.
2 3 4 5
12) At optimum temperature or pH, the rate or velocity of an enzymatic
reaction is
maximum minimum moderate constant
13) The rigidity of active site upon binding with substrate can be explained on
the basis of mechanism.
Induced-fit Ping pong
Michaelis Menten Lock and Key
14) Km of an enzymatic reaction is the concentration of at which
enzyme shows half of its maximum velocity.
enzyme substrate ES complex product
2. Answer the following (any 14
What is biological standard state
ii) State the relation between standard redox potential and standard free energy
change.
iii) State induced fit hypothesis of enzyme catalysis.
iv) What is significance of Km
State role of an allosteric modulator.
vi) Differentiate between competitive and noncompetitive inhibition.
vii) What are features of active site of an enzyme
viii) Define the terms coenzyme and prosthetic group.
ix) What is mass action ratio of a reaction
3. Answer the following (any 10
Explain ATP as an universal currency of free energy in biological system.
ii) Describe classification of enzyme with an example of each class.
iii) Write a note on specificity of enzymes.
Solve the following 4
Calculate the standard free-energy change of the reaction catalyzed by the
enzyme phosphoglucomutase.
Glucose 1-phosphate glucose 6-phosphate
Given R 8.315 J/mol, T 298 K.
Initial concentration Glucose 1 phosphate 20 mM, glucose 6 phosphate
0 mM concentration at equilibrium Glucose 1 phosphate 1 mM, glucose 6
phosphate 19 mM.
4. Answer any two of the following 14
Add an account on 'Common Biochemical Reactions'.
ii) Discuss in detail 'regulation of enzymes' in biological system.
iii) Describe in detail factors affecting enzyme activity.
5. Answer any two of the following 14
Describe in detail types of enzyme inhibition.
ii) Discuss biological oxidation reduction reactions. Add a note on measurement
of redox potential.
iii) Describe in detail isoenzymes of lactate dehydrogenase and their clinical
importance.