Exam Details
Subject | bioenergetics and enzymology | |
Paper | ||
Exam / Course | b.sc. (biotechnology) | |
Department | ||
Organization | solapur university | |
Position | ||
Exam Date | October, 2018 | |
City, State | maharashtra, solapur |
Question Paper
B.Sc. II (Biotechnology) (Semester III) (CBCS) Examination, 2018
bioenergetics and enzymology
Day and Date Wednesday, 5-12-2018 Max. Marks 70
Time 2.30 p.m. to 5.00 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
The term enzymes are coined by
Pasteur Buchner Urey Miller Kuhne
Number of substrate molecules converted into product by one molecule of enzyme active site per unit time is called
Turnover number Substrate number
Reaction None of these
In uncompetitive inhibition inhibitors binds only to
Enzyme Substrate
ES-complex Active site
Succinate thiokinase is an example of class of enzyme.
ligase lyase isomerase oxidoreductase
Ribozymes are the catalytic molecules.
RNA DNA Antibody Vitamin
The inhibitor molecule does not bind with the active site of enzyme to lower its catalytic.
catalytic allosteric reversible irreversible
Entropy of a system is measure of its
hardness softness
randomness spontaneity
The carbon carbon bond forming reaction among esters in presence of a strong base is
Isomerization Claisen condensation
Elimination Aldol condensation
The nonprotein part cavalently bound to the enzyme is the
Holoenzyme Apoenzyme
Prosthetic group Ribozyme
10) At optimum temperature or pH, the rate or velocity of an enzymatic reaction is
Maximum Minimum Moderate Constant
11) Km of an enzymatic reaction is the concentration of at which enzyme shows half of its maximum velocity.
Enzyme Substrate ES complex Product
12) The free energy of ATP hydrolysis under standard conditions is KJ/mol.
-2.303 -51.8 -8.314 none of these
13) The reaction's ratio is the ratio of product concentrations to reactant concentrations at one given time which may be at equilibrium or not.
Velocity Mass action Kinetic Catalytic
14) Reduction potential is the tendency of a chemical species to acquire
Electrons Protons Ions Neutrons
2. Answer any four of the following 8
Give significance of Vmax and Km.
State features of active site of an enzyme.
What is redox potential State its unit.
Define enzyme activity.
What is the effect of temperature on enzyme activity
Write a note on any two of the following 6
Lock and key model.
Thermodynamic systems.
Biological standard state.
3. Answer any two of the following 8
Explain induced fit mechanism.
Write a note on abzymes.
Describe biological role of enzymes.
Answer any one of the following 6
Describe types of enzyme inhibition.
Illustrate free energy of hydrolysis of ATP and its role as an universal currency of free energy in biological systems.
4. Answer any two of the following 10
Describe types of enzyme specificity.
Describe redox reactions. Add a note on redox potential.
Describe modes of enzyme regulation in living system.
Answer any one of the following 4
Describe clinical significance LDH isoenzymes.
Explain the concept of activation energy of enzyme.
5. Write a detailed account on any two of the following 14
Write in detail classification of enzyme with two examples of each.
Derive Michalis Menten equation. Give significance of Vmax and Km.
Describe in detail the factors affecting enzyme activity.
bioenergetics and enzymology
Day and Date Wednesday, 5-12-2018 Max. Marks 70
Time 2.30 p.m. to 5.00 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
The term enzymes are coined by
Pasteur Buchner Urey Miller Kuhne
Number of substrate molecules converted into product by one molecule of enzyme active site per unit time is called
Turnover number Substrate number
Reaction None of these
In uncompetitive inhibition inhibitors binds only to
Enzyme Substrate
ES-complex Active site
Succinate thiokinase is an example of class of enzyme.
ligase lyase isomerase oxidoreductase
Ribozymes are the catalytic molecules.
RNA DNA Antibody Vitamin
The inhibitor molecule does not bind with the active site of enzyme to lower its catalytic.
catalytic allosteric reversible irreversible
Entropy of a system is measure of its
hardness softness
randomness spontaneity
The carbon carbon bond forming reaction among esters in presence of a strong base is
Isomerization Claisen condensation
Elimination Aldol condensation
The nonprotein part cavalently bound to the enzyme is the
Holoenzyme Apoenzyme
Prosthetic group Ribozyme
10) At optimum temperature or pH, the rate or velocity of an enzymatic reaction is
Maximum Minimum Moderate Constant
11) Km of an enzymatic reaction is the concentration of at which enzyme shows half of its maximum velocity.
Enzyme Substrate ES complex Product
12) The free energy of ATP hydrolysis under standard conditions is KJ/mol.
-2.303 -51.8 -8.314 none of these
13) The reaction's ratio is the ratio of product concentrations to reactant concentrations at one given time which may be at equilibrium or not.
Velocity Mass action Kinetic Catalytic
14) Reduction potential is the tendency of a chemical species to acquire
Electrons Protons Ions Neutrons
2. Answer any four of the following 8
Give significance of Vmax and Km.
State features of active site of an enzyme.
What is redox potential State its unit.
Define enzyme activity.
What is the effect of temperature on enzyme activity
Write a note on any two of the following 6
Lock and key model.
Thermodynamic systems.
Biological standard state.
3. Answer any two of the following 8
Explain induced fit mechanism.
Write a note on abzymes.
Describe biological role of enzymes.
Answer any one of the following 6
Describe types of enzyme inhibition.
Illustrate free energy of hydrolysis of ATP and its role as an universal currency of free energy in biological systems.
4. Answer any two of the following 10
Describe types of enzyme specificity.
Describe redox reactions. Add a note on redox potential.
Describe modes of enzyme regulation in living system.
Answer any one of the following 4
Describe clinical significance LDH isoenzymes.
Explain the concept of activation energy of enzyme.
5. Write a detailed account on any two of the following 14
Write in detail classification of enzyme with two examples of each.
Derive Michalis Menten equation. Give significance of Vmax and Km.
Describe in detail the factors affecting enzyme activity.
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