BIOC1011 Module 1 Week 4 Tutorial Sheet 2024 The University of Queensland

BIOC1011 Module 1: Tutorial questions Week-4

Q1: Which statement about enzymes is INCORRECT?

a) There are enzymes that interact with one enantiomer, but not the other.
b) Enzymes are capable of reducing the activation energy.
c) Enzymes can be proteins or RNA
d) Enzymes are not used up during the reaction in which they are involved.
e) Enzymes can either speed up or slow down a chemical reaction.

Q2: Synthetic activated-complex analogues do which of the following?

a) They assist in the synthesis of specialized enzymes
b) They enhance enzyme activity
c) They reduce enzyme activity
d) They assist in transporting the substrate to the active site

Q3: Which of the following accurately describes how an enzyme functions?

a) Shifts the equilibrium for the reaction.
b) Reduces the enthalpy difference for the reactants and products.
c) Allows for the exothermic reaction of materials that are usually endothermic.
d) Changes the reaction mechanism, effectively reducing the activation energy.
e) Removes the requirement for water in reaction mechanisms.

Q4: When enzyme activity is graphed versus the following, which graph is a straight line?
a) Substrate concentration
b) Enzyme concentration
c) pH
d) Temperature

Q5: Substrate concentration has what effect on the rate of an enzyme-catalyzed reaction?
a) Increases until reaching a maximum
b) Decreases until reaching a minimum
c) Increases
d) Decreases
e) No effect
BIOC1011 Module 1 Week 4 Tutorial Sheet 2024 The University of Queensland

Q6: Which statement describes the currently accepted theory of how an enzyme and its
substrate fit together?

a) As the product is released, the enzyme breaks down.

b) The enzyme is like a key that fits into the substrate, which is like a lock.
c) The active site is permanently changed by its interaction with the substrate.
d) As the substrate binds to the enzyme, there is a conformational change in the enzyme
that result in stronger binding of the substrate or the activated complex.

Q7: Which of the following statements about the effects of various conditions on the activity
of an enzyme is INCORRECT?

a) Higher temperatures generally increase the activity of an enzyme up to a point.

b) Above a certain range of temperatures, the protein of an enzyme is denatured.
c) A change in pH can cause an enzyme to be inactivated.
d) An enzyme’s activity is generally reduced by an increase in substrate concentration.
e) A denatured enzyme has no catalytic activity.

Q8: Which one of the following statements is INCORRECT about the active site of an
enzyme?

a) it is similar to that of any other enzyme;

b) it is the part of the enzyme where its substrate can bind;
c) it can be used over and over again;
d) it contains specific amino acid side chains that can form non-covalent bonds with the
substrate. This is the explanation for an enzyme’s specificity.

Q9. Which of the following statements about inhibitors is INCORRECT?

a) An inhibitor is a compound that decreases the rate of an enzyme-catalysed reaction.

b) All enzyme inhibitors bind to the active site of enzymes they inhibit.
c) Inhibitors are frequently used as therapeutic drugs.
d) Knowledge of the 3-dimensional structures of enzymes and enzyme-inhibitor
complexes is invaluable in designing drugs as it aids design of better inhibitors.

Q10: Which of the following statements about competitive inhibitors is INCORRECT?

a) Mimic the structure of part of the enzyme.

b) Form a reversible complex with the enzyme.
c) Bind to the active site of an enzyme.
d) May be displaced by an excess of substrate
BIOC1011 Module 1 Week 4 Tutorial Sheet 2024 The University of Queensland

Q11: Shown below are data from urea-induced protein unfolding experiments on a wild-type (WT)
protein and bioengineered form of the same protein (R42W). Evaluate which of the two forms of
the protein is most stable.

Q12: A bioengineered thermostable Catalase displayed the following pH dependence on its

enzyme activity.

120

100

80

60
% activity

40

20

0
4 6 8 10 12
pH

a) What does the shape of the pH profile indicate in terms of the number of acidic and/or basic
groups involved in the catalysis?

b) Based on the data above, roughly estimate the pKa value(s).

c) It was found that cysteine and lysine were present in the active site. State which form
(protonated or deprotonated) each of these amino acids should be for optimum catalytic
activity.
BIOC1011 Module 1 Week 4 Tutorial Sheet 2024 The University of Queensland

Q13: The LWB plot for a reaction with no inhibition present is shown below and the equation
for the fit to the data is included.

0.45
0.4 y = 303x + 0.1
0.35
0.3
1/v (µM-1 s)

0.25
0.2
0.15
0.1
0.05
0
0 0.0005 0.001 0.0015
1/[S] (µM-1)

Two different inhibitors for this enzyme were evaluated, Inhibitor A and Inhibitor B. The
LWB plots obtained in the presence of each of these inhibitors are shown below. Use this
information to evaluate the type of inhibitor in each case.
Inhibitor A Inhibitor B

1 1.4
y = 753x + 0.1 y = 1000x + 0.3
1.2
0.8
1
1/v (µM-1 s)

1/v (µM-1 s)

0.6 0.8
0.4 0.6
0.4
0.2
0.2
0 0
0 0.0005 0.001 0.0015 0 0.0005 0.001 0.0015
1/[S] (µM-1) 1/[S] (µM-1)