KENYATTA UNIVERSITY

UNIVERSITY EXAMINATIONS 2017/2018

SECOND SEMESTER EXAMINATIONS FOR THE DEGREE OF BACHELOR OF
MEDICINE AND BACHELOR OF SURGERY

HMB 103 ENZYMOLOGY

DATE: ______________________________TIME: __________________________

INSTRUCTIONS

Section A: Answer ALL the questions (1 mark each)

1. Which one of the following is not among the six internationally accepted classes of enzymes?
A) Hydrolases
B) Ligases
C) Oxidoreductases
D) Polymerases

2. The concept of “induced fit” refers to the fact that:

A) Enzyme specificity is induced by enzyme-substrate binding.
B) Enzyme-substrate binding induces an increase in the reaction entropy, thereby catalyzing the
reaction.
C) Enzyme-substrate binding induces movement along the reaction coordinate to the transition
state.
D) Substrate binding may induce a conformational change in the enzyme, which then brings
catalytic groups into proper orientation.

3. Which of the following statements about a plot of V 0 versus [S] for an enzyme that follows
Michaelis-Menten kinetics is false?
A) As [S] increases, the initial velocity of reaction V 0 also increases.
B) At very high [S], the velocity curve becomes a horizontal line that intersects the y-axis at K M.
C) KM is the [S] at which V0 = 1/2 Vmax.
D) The shape of the curve is a hyperbola.

4. The following data were obtained in a study of an enzyme known to follow Michaelis-Menten
kinetics:
V0 (µmol/min) Substrate added (mmol/L)
217 0.8
325 2
 433 4
488 6
647 1,000

The KM for this enzyme is approximately:

A) 1 mM.
B) 1,000 mM.
C) 2 mM.
D) 4 mM.

5. The Lineweaver-Burk plot is used to:

A) Determine the equilibrium constant for an enzymatic reaction.
B) Extrapolate for the value of reaction rate at infinite enzyme concentration.
C) Illustrate the effect of temperature on an enzymatic reaction.
D) Solve, graphically, for the rate of an enzymatic reaction at infinite substrate concentration.

6. To calculate the turnover number of an enzyme, you need to know:

A) The enzyme concentration.
B) The initial velocity of the catalyzed reaction at [S] >> KM.
C) The initial velocity of the catalyzed reaction at low [S].
D) Both A and B.

7. In competitive inhibition, an inhibitor:

A) Binds at several different sites on an enzyme.
B) Binds covalently to the enzyme.
C) Binds only to the ES complex.
D) Binds reversibly at the active site.

8. Enzyme X exhibits maximum activity at pH = 6.9. X shows a fairly sharp decrease in its activity
when the pH goes much lower than 6.4. One likely interpretation of this pH activity is that:
A) A Glu residue on the enzyme is involved in the reaction.
B) A His residue on the enzyme is involved in the reaction.
C) The enzyme has a metallic cofactor.
D) The enzyme is found in gastric secretions.

9. A small molecule that decreases the activity of an enzyme by binding to a site other than the
catalytic site is termed a(n):
A) Allosteric inhibitor.
B) Alternative inhibitor.
C) Competitive inhibitor.
D) Stereospecific agent.

10. A metabolic pathway proceeds according to the scheme, R → S → T → U → V → W. A

regulatory enzyme, X, catalyzes the first reaction in the pathway. Which of the following is most
likely correct for this pathway?
A) Either metabolite U or V is likely to be a positive modulator, increasing the activity of X.
B) The first product S, is probably the primary negative modulator of X, leading to feedback
inhibition.
C) The last product, W, is likely to be a negative modulator of X, leading to feedback inhibition.
D) The last product, W, is likely to be a positive modulator, increasing the activity of X.

11. How is trypsinogen converted to trypsin?

A) A protein kinase-catalyzed phosphorylation converts trypsinogen to trypsin.
B) An increase in Ca2+ concentration promotes the conversion.
C) Proteolysis of trypsinogen forms trypsin.
D) Trypsinogen dimers bind an allosteric modulator, cAMP, causing dissociation into active
trypsin monomers.

12. In the binding of oxygen to myoglobin, the relationship between the concentration of oxygen
and the fraction of binding sites occupied can best be described as:
A) Hyperbolic.
B) Linear with a negative slope.
C) Linear with a positive slope.
D) Random.

13. When oxygen binds to a heme-containing protein, the two open coordination bonds of Fe2+ are
occupied by:
A) One O atom and one amino acid atom.
B) One O2 molecule and one amino acid atom.
C) One O2 molecule and one heme atom.
D) Two O atoms.

14. Which of the following is not correct concerning 2,3-bisphosphoglycerate (BPG)?

A) It binds at a distance from the heme groups of hemoglobin.
B) It binds with lower affinity to fetal hemoglobin than to adult hemoglobin.
C) It increases the affinity of hemoglobin for oxygen.
D) It is an allosteric modulator.

15. The fundamental cause of sickle-cell disease is a change in the structure of:
A) Blood.
B) Capillaries.
C) Hemoglobin.
D) Red cells.

16. An example of group transferring coenzyme is:

A) NAD+
B) NADP+
C) FAD
D) CoASH

17. Kinetics of an allosteric enzyme are explained by:

A) Michaelis-Menten equation
B) Lineweaver-Burk plot
C) Hill plot
D) All of these

18. Covalent modification of an enzyme usually involves phosphorylation/dephosphorylation of:

A) Serine residue
B) Proline residue
C) Hydroxylysine residue
D) Hydroxyproline residue

19. Dehydrogenases utilize, as coenzymes, all of the following except:

(A) NAD+
(B) NADP+
(C) FAD
(D) FH4

20. The steady state assumption, as applied to enzyme kinetics, implies:

A) KM = KS.
B) The enzyme is regulated.
C) The ES complex is formed and broken down at equivalent rates.
D) The KM is equivalent to the cellular substrate concentration.

Section B: Answer ALL the questions (5 marks each)

1. Explain the two assumptions used in the derivation of the simple Michaelis-Menten equation.
V [S ] V V V
2. Show ALL the steps involved in the transformation of V0 = max to 0 = max − 0
K M + [S ] [S ] K M K M
indicating the meaning of each symbol used in the equation(s).
3. Give five examples illustrating the use of enzymes as suicide inhibitors.
4. Explain the detoxification role of hemoglobin and myoglobin.
5. Explain how the activity of an enzyme of your choice is regulated via phosphorylation and
dephosphorylation.
6. Draw a well-labeled reaction scheme to represent the bell-shaped curve obtained by plotting the
effects of pH on the initial reaction velocity
7. Explain the two problems associated with enzyme therapy and the approaches used to overcome
them.

Section C: Answer ANY TWO questions (10 marks each)

1. Derive the Adair equation for a tetrameric protein.

2. Given the following data, determine, (a) the order of the reaction, (b) the rate law, and the value
of the rate constant, k.
A (aq) + B (aq) → Products
Trial [A] [B] Rate (M/s)
1 0.10 M 0.10 M 2.45 x 10-3
2 0.10 M 0.20 M 9.80 x 10-3
3 0.20 M 0.10 M 4.90 x 10-3
3. Derive the kinetics equation that explains the behaviour of a competitive inhibitor indicating
how the kinetic parameters of the equation are determined.
4. Give a well-labeled reaction scheme to explain sequential bisubstrate enzymatic reactions.

KENYATTA UNIVERSITY
UNIVERSITY EXAMINATIONS 2017/2018
SECOND SEMESTER EXAMINATIONS FOR THE DEGREE OF BACHELOR OF
MEDICINE AND BACHELOR OF SURGERY

HMB 103 ENZYMOLOGY

DATE: ______________________________TIME: __________________________

INSTRUCTIONS

Section A: Answer ALL the Questions (1 mark each)

1. From the Lineweaver-Burk plot of Michaelis-Menten equation, KM and Vmax can be determined
when Vo is the reaction velocity at substrate concentration S, the X-axis experimental data are
expressed as:
(A) 1/Vo
(B) Vo
(C) 1/[S]
(D) [S]

2. A sigmoidal plot of substrate concentration ([S]) verses reaction velocity (V o) may indicate:
(A) Michaelis-Menten kinetics
(B) Co-operative binding
(C) Competitive inhibition
(D) Non-competitive inhibition

3. The kinetic effect of purely competitive inhibitor of an enzyme

(A) Increases KM without affecting Vmax
(B) Decreases KM without affecting Vmax
(C) Increases Vmax without affecting KM
(D) Decreases Vmax without affecting KM
4. Activation or inactivation of certain key regulatory enzymes is accomplished by covalent
modification of the amino acid:
(A) Tyrosine
(B) Phenylalanine
(C) Lysine
(D) Serine

5. In enzyme kinetics KM implies:

(A) The substrate concentration that gives one half Vmax
(B) The dissociation constant for the enzyme substrate complexes
(C) Concentration of enzyme
(D) Half of the substrate concentration required to achieve V max

6. The pH optimum of most of the enzymes is:

(A) Between 2 and 4
(B) Between 5 and 9
(C) Between 8 and 12
(D) Above 12

7. An example of group transferring coenzyme is:

(A) NAD+
(B) NADP+
(C) FAD
(D) CoA

8. 2, 3-Biphosphoglycerate in high concentrations, combines with hemoglobin, causes:

(A) Displacement of the oxyhemoglobin dissociation curve to the left
(B) Displacement of the oxyhemoglobin dissociation curve to the right
(C) No change in oxy hemoglobin dissociation curve
(D) Increased affinity for oxygen

9. Lineweaver-Burk or double reciprocal plot is related to:

(A) Substrate concentration
(B) Enzyme activity
(C) Temperature
(D) Both (A) and (B)

10. Malonate is an inhibitor of:

(A) Malate dehydrogenase
(B) α-Ketoglutarate dehydrogenase
(C) Succinate dehydrogenase
(D) Isocitrate dehydrogenase

11. An example of enzyme inhibition:

(A) Reversible inhibition
(B) Irreversible inhibition
(C) Allosteric inhibition
(D) All of these

12. Competitive inhibition can be relieved by raising the:

(A) Enzyme concentration
(B) Substrate concentration
(C) Inhibitor concentration
(D) None of these

13. Regulation of some enzymes by covalent modification involves addition or removal of:
(A) Acetate
(B) Sulphate
(C) Phosphate
(D) Coenzyme

14. Kinetics of an allosteric enzyme are explained by:

(A) Michaelis-Menten equation
(B) Lineweaver-Burk plot
(C) Hill plot
(D) All of these

15. If the substrate concentration is much below the km of the enzyme, the velocity of the reaction
is:
(A) Directly proportional to substrate concentration
(B) Not affected by enzyme concentration
(C) Nearly equal to Vmax
(D) Inversely proportional to substrate concentration

16. Enzymes requiring NAD as co-substrate can be assayed by measuring change in absorbance
at:
(A) 210 nm
(B) 290 nm
(C) 340 nm
(D) 365 nm

17. In non-competitive enzyme action:

(A) Vmax is increased
(B) Apparent km is increased
(C) Apparent km is decreased
(D) Concentration of active enzyme molecule is reduced

18. ‘Lock’ and ‘Key’ model of enzyme action proposed by Fisher implies that:
(A) The active site is flexible and adjusts to substrate
(B) The active site requires removal of PO4 group
(C) The active site is complementary in shape to that of the substrate
(D) Substrates change conformation prior to active site interaction
19. Enzymes activity is controlled by:
(A) pH of the solution
(B) Temperature
(C) Concentration of the enzyme
(D) Concentration of the substrate
(E) All of these
20. Allosteric enzymes contain
(A) Multiple subunits
(B) Single chain
(C) Two chains
(D) Three chains

Section B: Answer ALL the Questions (5 marks each)

1. Briefly describe the steps involved in the conversion of the simple Michaelis-Menten kinetics
equation to Eadie-Hofstee equation.
2. Draw a well-labeled reaction scheme to explain non-competitive inhibition.
3. By the aid of a reaction scheme, explain the effects of pH on enzyme activity.
4. Explain the detoxification of nitric oxide (NO) in blood and muscle
5. Identify the various types of enzyme regulation mechanisms
6. Explain mathematically two situations which convert the symmetry/Monod-Wyman-Changeux
(MWC) model equation to that of a rectangular hyperbola.
7. Explain the use of asparaginase in managing some cancers.

Section C: Answer TWO Questions (10 marks each)

1. Describe briefly one mathematical model that explains cooperative binding of ligands to
proteins with multiple binding sites.
2. (a) Describe the use of an enzyme as a meat tenderizing agent
(b) Draw a reaction scheme to represent the conversion of pyruvate to lactate by lactate
dehydrogenase.
3. Describe the use of dehydrogenases in metabolite assays.
4. Write briefly on the Ping-Pong reaction mechanism.