Dental Biochem. 2006-Exam.

Dental Biochemistry Exam. I-2006

Fig. 1
Use figure 1 above for eukaryotic cell to answer questions 1-2
1.
Identify the letter, which represents the structure of mitochondria-----------E
2.

Identify the letter, which represents the structure of the nucleus-------------C

3.
Which one of the following components is present in the largest percentage in a
human being?
A.
B.
C.
D.
E.

Proteins
Carbohydrates
Lipids
DNA
RNA

4.

Phospholipids are

A.
B.
C.
D.
E.

extremely hydrophobic.
contain fatty acids linked to glycerol by ester bonds.
contain fatty acids linked to glycerol by amide bonds.
Only statements A and B are correct.
Only Statements A and C are correct.

Dental Biochem. 2006-Exam. I

5.

Which one of the following structures is a primary alcohol?

A.
B.
C.
D.

R-CH2-CHOH-CH2-CH3
R-CH2-CH2-CHO
R-CH2-CH2-CONH-CH3
R-CH2-CH2-OH

For questions 6-7 select one of the following. Any answer may be used once or more than
once or not at all.
A.
B
C.
D.
E.

Oxidation- Reduction reaction

Hydrolysis
Transamination
Lyase
Ligase

6.

CH3-CH2-OH + NAD+ CH3CHO + NADH + H+

7.

ATP + CoA + Acetate Acetyl-CoA + ADP + H+

-------------------A
---------------------------E

8.
Peptidases are enzymes that are important in a number of physiological processes
like blood coagulation. Their function is to hydrolyze
A.
B.
C.
D.
E.

Proteins.
Triglycerides.
Fatty acids
Carbohydrates.
Amino acids.
The [H+] concentration of saliva in a patient with oral cancer is

9.

3.2 x 10-7 M. The pH value of saliva would approximately be

A.
B.
C.
D.
10.

4.5.
6.5.
2.5
3.5
A system with good buffering capacity is made up of

A.
B.
C.
D.
E.

a strong acid and its conjugate base

a strong base and its conjugate acid
a weak base and a strong acid
a weak acid and its conjugate base
two weak bases

Dental Biochem. 2006-Exam. I

11.
Lactic acid is produced in the oral cavity from anaerobic oxidation of glucose.
What would be the pH of saliva if salivary concentrations of lactic acid and sodium
lactate were 0.02 and 0.08 moles/liter respectively. The pKa of lactic acid is given as 5.2.
Answers are given to one decimal place.
A.
B.
C.
D.
E.

4.6
5.8
4.8
3.8
6.6

12.
Which pair of side chains of amino acid are likely to show significant
hydrophobic interactions in proteins?
A.
B.
C.
D.
E.
13.

Leu and Lys

Ala and Ser
Trp and Gln
Val and Ile
Gln and Asn
Which is (are) the characteristic feature(s) of peptide bond(s) in proteins?

A.
B.
C.
D.
E.
14.

Peptide bond is formed between an alpha-amino group of one amino acid and
the carboxyl group of another amino acid
The peptide bond is planar and has a partial double bond character.
The hydrogen of the peptide bond has partial positive charge and is able to
hydrogen bonds with other partially negatively charged groups.
Only statements A and B are correct.
Statements A, B and C are all correct.
Lys-Gly-Lys-Glu-Arg-Asp

The above peptide was isolated from the secretions of the parotid gland. The charge on
this peptide at neutral pH is expected to be
A.
B.
C.
D.
E.

+3
+2
+1
1
2

15.
Most amino acids rotate the plane of polarized light and are thereby designated as
optically active. An amino acid that is not optically active is
A.
B.
C.
D.
E.

Glu
Asp
His
Gly
Ala

Dental Biochem. 2006-Exam. I

16.
Which of the following is LEAST likely to affect the Vmax of an enzyme
catalyzed reaction?
A.
B.
C.
D.

change in pH.
change in temperature.
Addition of a noncompetitive inhibitor.
Addition of a competitive inhibitor.

17.
The kinetics of most enzymatic reactions can be described in terms of Km and
Vmax. Which of the following best describes Km? Km is
A.
B.
C.
D.

equal to the concentration of a substrate, which gives a rate equal to Vmax.

equal to one-half of Vmax
the concentration of an inhibitor required to produce 50% inhibition.
nearly equal to the dissociation constant for ES complex.

18.

The free energy change (G) for a reaction at equilibrium is

A.
equal to 1.
B.
zero.
C.
greater than 1.
D.
equal to -RT In Keq.

19.

A competitive inhibitor of an enzymatic reaction

A.
B.
C.
D.

lowers the apparent Km but does not change Vmax..

does not change apparent Km and does not change Vmax.
increases apparent Km and lowers Vmax.
increases apparent Km, but does not change Vmax.

20.

The alpha-helix protein structure

A.
B.
C.
D
E.

can exist in parallel and anti-parallel forms.

is stabilized by hydrogen bonds.
is stabilized by the presence of proline residues.
is characterized by both A and B.
is characterized by A, B and C.

21.
An attempt is made to separate proteins A, B, and C of molecular weights 15000
(A), 50000 (B) and 80000 (C) Daltons respectively, by chromatography using G-50
Sephadex. The order of elution of these proteins sequentially from this column is
expected to be
A.
B.
C.
D.
E.

A, B, C
C, B, A
B, C, A
A, C, B
B, A, A

Dental Biochem. 2006-Exam. I

22.
SDS-PAGE gel electrophoresis is used to estimate the size of a protein. The
success of this method depends on the knowledge that after SDS treatment
A.
B.

all proteins are negatively charged and move towards the positively charged
electrode
all proteins are positively charged and move towards the negatively charged
electrode.
proteins carry no charge and are separated on the basis of their size.
peptide bonds are cleaved and the method is not very successful.

C.
D.
.
23.
An enzyme is reacted with an irreversible inhibitor until the enzyme activity is
reduced to of the original value. Which of the following statements will be correct
concerning the kinetics of this system?
A. Vmax is decreased to one-half of its original activity but Km remains
unchanged.
B. Vmax is doubled and Km is decreased.
C. Both the Km and Vmax values are decreased to of original values.
D. Both the Km and Vmax values are increased.
24.
A sigmoid curve is obtained for an enzyme when the initial rate of reaction (v) is
plotted against the concentration of the substrate (S). This means that
A. the enzyme follows Michaelis-Menten Kinetics.
B. the binding of substrate to the active site will not be affected by activators or
inhibitors of the enzyme
C. binding of the substrate to the first subunit alters the conformation of other associated
subunits.
D. Answers A, B and C are all incorrect.
25.
You are asked to determine the specific activity of lysozyme in the saliva of
patients having periodontal disease. Under what conditions should the activity be
measured so the values of specific activities can be correlated with the amount of enzyme
in the saliva?
A. Activities should be measured at a substrate concentration equal to the Km value.
B. Enzyme activity should preferably be measured when the active site of the enzyme is
nearly saturated with the substrate.
C. The activity should be measured when enzyme concentration is greater the substrate
concentration.
D. Activities should be measured when substrate and enzyme are in equal
concentrations.

Dental Biochem. 2006-Exam. I

26.
Specific activity of an enzyme in saliva may be defined as micromoles of
substrate converted to product
A.
B.
C.
D.
27.

per unit time per unit volume of saliva.

per second per mole of the active site of the enzyme.
per hour.
per year.
An enzyme affects the rate of a chemical reaction by

A.
B.
C.
D.
E.
28.

lowering the free energy of a reaction.

increasing the free energy of a reaction.
lowering the activation energy of a reaction.
increasing the activation energy of the reaction.
increasing the equilibrium constant for the reaction.
An allosteric enzyme is expected to modulate

A.
B.
C.
D.
E.
29.

the first reaction of the sequence.

the last reaction of the sequence.
the committed step of the sequence.
any reaction of the sequence.
the first and last reactions of the sequence.
An allosteric activator affects the activity of an allosteric enzyme by

A.
B.
C.
D.
E.
30.

binding at the substrate binding site.

increasing the K0.5 for the substrate.
decreasing K0.5 for the substrate.
lowering the Vmax for the reaction.
binding to the Taut (T) conformational state of the enzyme.
Standard free energy changes (G0) for two reactions are additive when

A.
B.
C.
D.
E.

one G0 is a negative number and the other G0 is a positive number.

both G0 are negative numbers.
both G0 are positive numbers.
product of first reaction is a substrate for the second reaction.
product of first reaction is also a product of the second reaction.

31.
In an enzyme catalyzed reaction, if the substrate concentration is three times the
value of Km, the initial rate of reaction will be
A.
B.
C.
D.
E.

0.25 Vmax.
0.5 Vmax.
0.33 Vmax.
0.67 Vmax.
0.75 Vmax.

Dental Biochem. 2006-Exam. I

32.
Doxycycline and minocycline inhibit collagenase and are being used to control
periodontal disease. Assume that the Ki values for these inhibitors are 10-6 M and
0.5x10-6 M respectively. If the drugs were used at the same molar dose and their rates of
clearance were identical, which drug would be a preferred choice?
A.
B.
C.

Doxycycline.
Minocycline.
Both drugs will be equally effective.

33.
Methotrexate is a drug that is used for cancer chemotherapy. It inhibits the
enzyme, dihydrofolate reductase. This inhibition has been characterized as
A.
B.
C.
D.
E.

competitive inhibition.
non-competitive inhibition.
irreversible inhibition.
allosteric inhibition.
end-product inhibition.

34.
The equilibrium constant for the conversion of sucrose to glucose and fructose is
1,000. What can you conclude about the reaction?
Sucrose + H2O
A.
B.
C.
D.

It is a closed system.
It never reaches equilibrium.
It is spontaneous, starting with sucrose.
The equilibrium constant increases when the starting
concentration of sucrose is increased.
At equilibrium, the concentration of sucrose is much higher than
the concentrations of glucose and fructose.

E.
35.

glucose + fructose

Penicillin is an antibiotic and inhibits bacterial growth. It

A.
B.
C.
D.
E.

competes with dihydrofolate for the active site of glycopeptide

transpeptidase.
promotes the synthesis of bacterial cell walls.
is a competitive inhibitor of bacterial glycopeptide transpeptidase.
is an irreversible of inhibitor of bacterial glycopeptide transpeptidase.
All of the above statements are correct.

Dental Biochem. 2006-Exam. I

36.
Calculate the isoelectric point (pI) of amino acid histidine if the three pKa values
are given as pKa1 (2.2), pKa2 (6.8) and pKa3 (9.6).
A.
B.
C.
D.
E.
37.

4.5.
5.9.
8.2.
6.8.
2.2

A.
B.
C.
D.
E.

The only oxidative reaction in the conversion of glucose to pyruvate is catalyzed by

lactate dehydrogenase.
succinate dehydrogenase.
alpha glycerophosphate dehydrogenase.
glyceraldehyde-3-phosphate dehydrogenase.
fructose oxidase.

A.
B.
C.
D.
E.

Hypoglycemia would be anticipated as a consequence of a deficiency of the enzyme

glucose-6-phosphatase.
glucose-6-phosphate dehydrogenase.
pyruvate dehydrogenase.
glucose oxidase.
glucose isomerase.

A.
B.
C.
D.
E.

ATP is generated directly in glycolysis as result of the action of

hexokinase.
aldolase.
glyceraldehyde-3-phosphate dehydrogenase.
phosphofructokinase.
pyruvate kinase.

38.

39.

40.
Conversion of dihydroxyacetone phosphate to pyruvate in glycolysis requires the
action of
A. lactate dehydrogenase.
B. glycerokinase.
C. alpha glycerophosphate dehydrogenase.
D. triose phosphate isomerase.
E. aldolase.
41.
A.
B.
C.
D.
E.

Inorganic phosphate is liberated in gluconeogenesis in the reaction catalyzed by

hexokinase.
aldolase.
phosphoglycerate mutase.
fructose 1,6-bisphosphatase.
phosphoglucomutase

Dental Biochem. 2006-Exam. I

42.
A.
B.
C.
D.
E.

High levels of ATP regulate glycolysis by inhibition of

aldolase.
phosphofructokinase.
glyceraldehyde-3-phosphate dehydrogenase.
enolase.
phosphoglycerate mutase.

A.
B.
C.
D.
E.

The first reaction in the conversion of pyruvate to glucose occurs in

nuclei.
mitochondria.
lysosomes.
cytosol.
microsomes.

A.
B.
C.
D.
E.

Pyruvate generated by glycolysis must enter the mitochondria to be oxidized

because the mitochondria are impermeable to lactate.
so that the cytosol remains electrically neutral.
because pyruvate dehydrogenase is a mitochondrial enzyme.
by exchange with malate.
to generate malate in the malic enzyme reaction.

A.
B.
C.
D.
E.

Formation of carbon dioxide occurs in the conversion of

glucose to 6-phosphogluconate.
6-phosphogluconate to glyceraldehyde-3-phosphate .
ribulose 5-phosphate to ribose 5-phosphate.
glucose to UDP-glucose.
xylulose 5-phosphate to sedoheptulose 7-phosphate.

43.

44.

45.

46.
In the conversion of one mole of glucose 6-phosphate to ribose 5-phosphate the
number of moles of NADP which are reduced is
A. 1.
B. 2.
C. 3.
D. 4.
E. 5.
47.
A.
B.
C.
D.
E.

Glycogen synthase
is inhibited by glucose 6-phosphate.
requires 3,5-cyclic AMP as a coenzyme .
forms alpha 1,4 glycosidic links.
requires orthophosphate as a substrate.
generates UTP as a reaction product.

Dental Biochem. 2006-Exam. I

48.

All the following statements about glycogen metabolism are true EXCEPT
A. Cyclic AMP-activated protein kinase stimulates glycogen synthase.
B. Phosphorylase kinase is activated by phosphorylation.
C. Phosphorylase b is activated by phosphorylation.
D. Cyclic AMP levels are raised by epinephrine and glucagon stimulation of adenylate
cyclase.
E. A futile cycle of glycogenesis and glycogenolysis is prevented by second-messenger
regulation.

49.
A.
B.
C.
D.
E.
50.

Glycogen
occurs in highest concentration in the brain
is secreted by the liver during exercise
is the major energy reserve in the body
synthesis is increased during starvation
is a branched chain polymer of glucose
Which of the following does not serve as a precursor for gluconeogenesis?

A.
B.
C.
D.
E.

leucine
glycerol
pyruvate
alanine
lactate

A.
B.
C.
D.
E.

Accumulation of mucopolysaccharide occurs with an inherited deficiency of

glycogen phosphorylase.
galactokinase.
alpha-L-iduronidase
acid maltase.
galactose-1-phosphate uridyl transferase.

A.
B.
C.
D.
E.

Which of the following polysaccharides is most notable for its anticoagulant action ?
Hyaluronic acid
Chondroitin sulfate
Keratan sulfate
Heparin
Glycogen

A.
B.
C.
D.
E.

Glycosaminoglycans
are synthesized by amidation of glycogen.
always have alpha 1-4 glycosidic links.
are polyanionic.
usually contain sialic acid.
are only found in cartilage.

51.

52.

53.

10

Dental Biochem. 2006-Exam. I

54.

Which of the following is produced in one turn of the citric acid (TCA) cycle?

A.
B.
C.
D.
E.

three molecules of carbon dioxide.

three molecules of NADH
one molecule of CTP
one molecule of NADPH.
two molecules of pyruvate.

55.

The citric acid (TCA) cycle

A.
B.
C.
D.
E.

occurs in the cytosol.

is inhibited by high concentrations of ADP.
includes two oxidative decarboxylation reactions.
differs from glycolysis in requiring NAD as a coenzyme.
is activated by high concentrations of ATP.

56.

The activity of pyruvate dehydrogenase

A.
B.
C.
D.
E.

yields lactate under anaerobic conditions.

is the first step in gluconeogenesis.
is stimulated by an associated protein kinase.
requires the reduction and oxidation of a lipoyl residue.
is inhibited by thiamine pyrophosphate.

11