CH405

BIOCHEMISTRY

FSTE
School of Biological and Chemical Sciences

Final Examination
Semester 2, 2015

Face to Face Mode

Duration of Exam: 3 hours + 10 minutes

Reading Time: 10 minutes
Writing Time: 3 hours

INSTRUCTIONS

1. This exam has FIVE questions.

2. Candidates are to answer any FOUR in the answer book provided.
3. Each question is worth 20 marks.
4. Answer each question on a NEW page.
5. This exam is worth 40% of your overall mark.

Materials
You may use a non-programmable calculator.
You will be provided with a graph paper.
Question 1

The kinetic data in the following table were obtained for a reaction between β-methylaspartase
and its substrate β-methylaspartate. The rate of the reaction was determined by monitoring the
absorbance of the product at 240 nm (A240).

β-methylaspartate Mesaconate absorbs at 240nm

The above reaction was also monitored in the presence of an inhibitor

hydroxymethylaspartate. The rate of the reaction was again determined by monitoring the
absorbance of the product at 240 nm.

Substrate (µM) Velocity with No Velocity with 25 nM Velocity with 50

inhibitor inhibitor nM inhibitor
(µmol/min) (µmol/min) (µmol/min)
0.40 0.22 0.21 0.20
0.67 0.29 0.26 0.24
1.00 0.32 0.30 0.28
2.00 0.40 0.36 0.32

i. Use this data to sketch a Lineweaver Burk Plot.

(10 marks)

ii. Determine the maximum velocity (Vmax) with inhibitor and without inhibitor.
(2 marks)

iii. Determine the Km values with inhibitor and without inhibitor.

(2 marks)

iv. Using the values from ii and iii above, determine if the inhibitor is competitive or
non-competitive.
(2 marks)

v. Explain the difference between competitive and non-competitive inhibition.

(4 marks)

2
Question 2

A. Describe FOUR transport mechanisms of biomolecules across the cell membrane with
suitable example(s).
(10 marks)

B. List TWO co-factors or vitamins and explain the importance in biochemical reactions.
(10 marks)

Question 3

A. Explain the models used for the binding of a substrate to the enzyme. (You may use
diagrams)
(8 marks)

B. Using an energy diagram, show why the lock-and-key model could lead to an inefficient
enzyme mechanism. Relate the inefficiency to the distance between transition state and
the enzyme. (5 marks)

C. Explain TWO factors that affect any catalytic reaction.

(4 marks)

D. There is a disadvantage of an enzyme having a very high affinity for its substrate. Discuss
this statement. (3 marks)

Question 4

Describe the main biochemical features of glycolysis, Krebs cycle and electron transport chain
(whole cycle and structures are not required).
(20 marks)

3
Question 5
Answer Either

A. Describe the main biochemical processes involved in fatty acid biosynthesis. You may want
to use the following:
 Synthesis of malonyl acyl carrier protein and acetyl acyl carrier protein
 Initiation of fatty acid synthesis
 Elongation reactions
 Fatty acid activation
 Fatty acid extension and desaturation

(20 marks)

OR

B. Describe the main biochemical processes involved in fatty acid oxidation. You may want to
use the following:
 Activation of fatty acids
 β-oxidation
 Fatty acid synthesis
 Transport of fatty acylCoA into mitochondria
 ATP generation
(20 marks)

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