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BOCE2626 - Sem - Test1 - 2023 For BB

This document contains a semester test for a microbiology and biochemistry course. The test has 6 questions assessing students' knowledge of enzyme kinetics, allosteric regulation, coenzymes, and glycolysis. It provides context for the test such as the date, assessor, time limit, and instructions for students to answer all questions in their book and show calculations. The questions cover topics like transition states, turnover numbers, Michaelis-Menten kinetics, types of inhibition, kinetic profiles of allosteric enzymes, reactions in glycolysis, and fates of pyruvate. Students are directed to define terms, draw graphs, identify reaction types, discuss models, and give metabolic reactions and pathway intermediates.

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52 views4 pages

BOCE2626 - Sem - Test1 - 2023 For BB

This document contains a semester test for a microbiology and biochemistry course. The test has 6 questions assessing students' knowledge of enzyme kinetics, allosteric regulation, coenzymes, and glycolysis. It provides context for the test such as the date, assessor, time limit, and instructions for students to answer all questions in their book and show calculations. The questions cover topics like transition states, turnover numbers, Michaelis-Menten kinetics, types of inhibition, kinetic profiles of allosteric enzymes, reactions in glycolysis, and fates of pyruvate. Students are directed to define terms, draw graphs, identify reaction types, discuss models, and give metabolic reactions and pathway intermediates.

Uploaded by

ntsakopreciousko
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd
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UNIVERSITY OF THE FREE STATE

MAIN CAMPUS

BOCE2626

DEPARTMENT OF MICROBIOLOGY AND BIOCHEMISTRY


CONTACT NUMBER: 051 401 2532

SEMESTER TEST 1

26 October 2023

ASSESSOR : Dr. C. Tolmie


MODERATOR : Prof. G. Osthoff

TIME: 90 minutes MARKS: 50

Please answer all questions in your answer book. Please read all questions carefully.

Question 2 (6 marks)
Define the following terms:

2.1 Transition state (1)

2.2 Turnover number (1)

2.3 Electrophile (1)

2.4 K system (1)

2.5 Anabolism. (1)

2.6 Steady state (1)

Question 3 (11 marks)

3.1.1 Draw a Michaelis-Menten kinetic curve and indicate the kinetic parameters. (3)
(Please note that absence of or incorrect axis labels will lead to no marks being
awarded).

3.1.2 Give the mathematical equation that defines the graph you drew for 3.1.1. (1)

1
3.2 An enzyme that follows Michaelis-Menten kinetics is characterised in the
presence and absence of a reversible inhibitor. At very high substrate
concentrations, a decrease in the initial velocity is observed between the
reactions in the presence and absence of the inhibitor; however, the substrate
concentration that gives half of these respective initial velocities is the same for
the reactions with and without the inhibitor.

3.2.1 Identify the type of reversible inhibition. (1)

3.2.2 By referring to the mode of action of the inhibitor, explain why the respective
kinetic parameters change or do not change in the presence of the inhibitor.
(8 x ½)

3.3 An enzyme that follows Michaelis-Menten kinetics has been characterised, and
the following parameters were determined:
KM: 2 mM
vmax: 15 μmol.min-1
(0.5 μmol enzyme was used in the experiments)

Calculate the catalytic efficiency of the enzyme. Show all calculations and
include all units. (2)

Question 4 (11 marks)


4.1 Draw the kinetic profile of the enzyme ATCase in the presence and absence of its
effectors (on one graph). Write the identities of the effectors next to their respective

2
curves (abbreviations may be used). (Please note that absence of or incorrect axis
labels will lead to no marks being awarded). (4)

4.2 Discuss the T:R concerted model for allosteric enzymes. Your answer must
include the type of model, the principle of the model, the role of effectors and
the parameters of the model. (10 x ½)

4.3 Give the full name and draw the deprotonated side chain of an amino acid that
commonly adopts a negative charge. (2)

Question 5 (3 marks)

Show how NAD is oxidized and reduced by drawing the appropriate nitrogen
base (only the base, not the full molecule). Indicate which structure is oxidized
and which is reduced. (3)

Question 6 (14 marks)


Please note

When a complete reaction is asked, the following must be included in the answer:

→ Enzyme name

→ Names of metabolites & all molecules involved in the reaction

→ Structures of the pathway intermediates must be drawn

→ The abbreviated names of coenzymes and/or nucleotides must be given, but their
structures do not have to be drawn

When a linear reaction is asked, the following must be included in the answer:

3
→ Enzyme name

→ Names of metabolites & all molecules involved in the reaction

→ The abbreviated names of coenzymes and/or nucleotides

NB: When a reaction is asked, your answer must only contain the specific reaction and
not the whole pathway. Answering the entire pathway will lead to 0 marks being
awarded.

6.1 Give the complete reaction that is catalysed by phosphofructokinase. (4)

6.2 Give the linear reaction in which the second ATP molecule is produced in
glycolysis. (3)

6.3 Give the complete, overall reaction of glycolysis that is catalysed by


glyceraldehyde-3-phosphate dehydrogenase. (5)

6.4 Name the two possible fates of pyruvate in the absence of oxygen. (2)

END OF TEST

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