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Republic of the Philippines

University of Eastern Philippines


University Town, Northern Samar

COLLEGE OF SCIENCE

Final Examination in Chemistry 2/Major 15


BIOCHEMISTRY
2nd Semester 2015 – 2016

INSTRUCTION:
1. Use the answer sheet provided for your answer. Shade properly the box that corresponds to
the letter of your answer.
2. Use only blue or black ball pen. Pencil is not allowed.
3. Do not write or put any marks on the questionnaire.
4. Examinees are not allowed to leave the examination room during examination proper
5. Borrowing of any material (ball pen, calculator, periodic table, etc) is not allowed.
6. Cellphones are not allowed to be used as calculator.
7. Do not detached any of the pages of your questioner
8. Complete all information on your answer sheet.

GOOD LUCK!!

1. Biochemical pathway is;


a. The sum of all the chemical reaction that takes in living organism.
b. The actual reaction by means of which energy stored in the food is converted to an
energy used in every minute of our life.
c. The reaction by which large complex food substances are broken down into its simple
building blocks
d. The reaction by which a simple molecule are linked together to form a complex one
2. The enzyme that catalyzed the cleavage or hydrolysis of the peptide bond only on the carboxylic
side of lysine and arginine residue;
a. Trypsin c. Pepsin
b. Carboxypeptidase d. Pepsinogen

CH 3
3. Amino acid with a side chain of - CH is;
CH 3
a. Leucine c. Valine
b. Glycine d. Alanine
4. The RNA molecule that carries genetic information from the DNA in the nucleus directly to the
ribosomes in the cytoplasm;
a. tRNA c. mRNA
b. rRNA d. snRNA
5. Zwitterion are compounds;
a. That can act both as an acid and a base
b. That are capable of resisting pH change
c. Having a positive charge on one atom and a negative charge on another.
d. Where four different groups are attached to the same carbon atom
6. The phosphorylation of glucose to glucose-6-phosphate during the initial step of
glycolytic pathway is catalyzed by an enzyme called;
a. Dehydrogenase c. Hexokinase
b. Enolase d. Aldolase
7. Group of enzymes that catalyzes the joining of two molecules together are collectively called as;
a. Isomerase c. Hydrolase
b. Ligases d. Lyases
8. The process in which information encoded in a mRNA molecule is used to assemble an specific
protein;
a. Transcription c. Transduction
b. Translation d. Transition
9. Hemoglobin based on their function are;
a. Transport protein c. Storage protein
b. Protective protein d. Structural protein
c.
10. In certain bacteria and yeast, pyruvate formed from glycolysis undergoes reductive
decarboxylation to form;
a. Acetic acid c. Lactic acid
b. Ethyl alcohol d. CO2 and H2O
11. An uncommon amino acid formed as an intermediate product of synthesis of serotonin from
tryptophan;
a. 5-hydroxytryptophan c. 5-aminotryptophan
b. 5-nitrotryptophan d. 5-oxytryptophan
12. The mRNA has a codon of UAC that codes for amino acid tyrosine. Which anticodon must be
found in tRNA for it to carry tyrosine to the site of protein synthesis;
a. UAC c. GUA
b. AUC d. AUG
13. The enzyme that catalyze the hydrolysis of simple fats and lipids to fatty acids and glycerol in the
small intestine;
a. Ptyalin c. Gastrin
b. Amylopsin d. Steapsin
14. Biochemical reaction involving cleavage or splitting of a single molecule to two distinct molecule
in the presence of water;
a. Decomposition c. Hydrolysis
b. Synthesis d. Oxidation-reduction
15. Dehydration of 2-phosphoglycerate to give phosphoenolpyruvate during glycolytic reaction is
catalyzed by an enzyme;
a. Enolase c. Aldolase
b. Isomerase d. Hydratase
16. The specific pathway by which energy is extracted from glucose where a molecule of glucose is
converted into two molecules of pyruvate;
a. Gluconeogenesis c. Glycolysis
b. Glycogenesis d. Glycogenolysis
17. The isomerization of dihydroxyacetone to D-glyceraldehyde-3-phosphate is catalyzed by and
enzyme called;
a. Triosemutase c. Triosephosphate isomerase
b. Trioseisomerase d. Triose enolase

18. Glutathione is a tripeptide protein containing which of the following?


a. L-glutamic acid – L-cysteiene – glycine
b. L-glutamic acid – L- aspartic acid – leucine
c. L-glutamic acid – L- proline – valine
d. L-glutamic acid – L- asparagines – alanine
19. Albinism is a genetic disorder caused by the lack of which of the following enzymes;
a. Transaminase c. Thyroxinase
b. Tyrosinase d. Amino transferase
20. Human insulin differ from the hogs insulin in that the amino acid residue – threonine – in
sequence no. 30 in the β – chain of human insulin is replaced with _____ in hogs insulin;
a. Phenylalanine c. Alanine
b. Serine d. Valine
21. Which of the following is absorbed through the wall of gastrointestinal tract to the blood via a
lymph vessel called lacteals;
a. Fatty acid c. Nucleotides
b. Amino acids d. Glucose
22. A plasma protein responsible for the formation of blood clot;
a. Albumin c. Fibrinogen
b. Histone d. Protamine
23. The covalent bond most often involved in stabilizing tertiary structure of protein is the;
a. Peptide bond c. Electrostatic bond
b. Disulfide bond d. Hydrophilic bond
24. The combination of pentose sugar and a nitrogen base form a compound known as;
a. Nucleosome c. Nucleoside
b. Nucleoloid d. Nucleotide
25. How many ATP molecules is produced during glycolysis of one glucose molecule?
a. 2 c. 6
b. 4 d. 8
26. The protein portion of an enzyme;
a. Proenzyme c. Apoenzyme
b. Holoenzyme d. Co-enzyme
27. Which of the following secondary protein molecules exists in α – helix form?
a. Fibroin c. Keratin
b. Collagen d. Elastin

28. The process of protein denaturation in which colloidal particle come together to form a larger
mass;
a. Precipitation c. Suspension
b. Colloid formation d. Coagulation
29. A green pigment formed from oxidation of the heme part of hemoglobin molecule;
a. Cytochrome c. Biliverdin
b. Bilirubin d. Urobilin
30. If the anticodon in tRNA that transport amino acid serine is UCA; the codon in mRNA in the
ribosome where protein synthesis takes place must be;
a. AGU c. UGA
b. GUA d. GAU
31. Biochemical combination reaction is catalyzed by group of enzyme called;
a. Ligase c. Lyases
b. Isomerase d. oxido-reductase
32. They pioneered in the kinetic study of enzyme catalyzed reaction as well as the development of
explanation as to how enzyme participate in the reaction;
a. Koshland and Fischer c. Michaeles and Menten
b. Watson and Crick d. Beadle and Tatum
33. β – oxidation of fatty acids occurs only in the;
a. Mitochondria c. Cytoplasm of the cell
b. Ribosomes d. Endoplasmic reticulum
34. In the nucleus the acidic nucleic acid DNA and the basic histone attract each other by electrostatic
forces combining to form a unit called;
a. Nucleotide c. Nucleoloid
b. Nucleoside d. Nucleosome
35. The uncoiling of the protein molecule which causes loss of its biological function is termed as;
a. Denaturation c. Conjugation
b. Mutation d. Modification
36. The spatial relationship and interaction between subunit in a protein that has more than one
polypeptide chain form the;
a. Primary Protein Structure c. Tertiary Protein Structure
b. Secondary Protein structure d. Quaternary Protein Structure
37. Organic co-factor are called;
a. Proenzyme c. Holoenzyme
b. Co-enzyme d. Allosteric enzyme
38. Which is the correct sequence of the three stage nitrogen metabolism?
a. Urea cycle – oxidative deamination – transamination
b. Transamination – urea cycle – oxidative deamination
c. Oxidative deamination – transamination – urea cycle
d. Transamination – oxidative deamination – urea cycle
39. A heterocyclic nitrogen base of high energy phosphate compound GTP;
a. Adenine c. Cytosine
b. Guanine d. Uracil
40. Saliva based on their chemical composition is a;
a. Glycoprotein c. Chromoprotein
b. Lipoprotein d. Phosphoprotein
41. Aromatic amino acid include the following, EXCEPT;
a. Tryptophan c. Phenylalanine
b. Proline d. Tyrosine
42. Oxidation of hydroacyl-CoA to ketoacyl-CoA during the 4th step of β – oxidation is catalyzed by
an enzyme;
a. Hydroxyacyl dehydrogenase c. Hydroxyacyl isomerase
b. Hydroxyacyl hydratase d. Hydroxyacyl decarboxylase
43. The following are factors affecting enzyme activity, EXCEPT;
a. Enzyme concentration d. Ion concentration
b. Substrate concentration e. pH
c. Temperature
44. The triplets of bases in mRNA that codes for a particular amino acid is called;
a. Codon c. Anticodon
b. Genetic sequence d. Genetic code

45. The following are fibrous protein, EXCEPT;


a. Keratin c. Elastin
b. Collagen d. Myosin
46. The compound on which the enzyme act or work on are called;
a. Apoenzyme c. Substrate
b. Inhibitor d. Activator
47. Uncommon amino acid formed from modification of tyrosine residue in the protein
thyroglobulin;
a. Thyronine c. Thyroxine
b. Hydroxythyronine d. Thyroglobin
48. In the absence of oxygen pyruvate formed from glycolysis in some bacteria and in mammals is
reduced to;
a. Acetyl-CoA c. Lactic acid
b. Ethyl acetate d. Acetic acid
49. T he backbone of the two strands of DNA molecule is formed by;
a. Pentose sugar and pyrimidine bases c. Phosphate group and purine bases
b. Pentose sugar and phosphate group d. Purine and pyrimidine bases
50. Which region of protein molecule is affected by strong acid and base as chemical denaturant?
a. Hydrogen bond & hydrophobic interaction c. Disulfide bond & salt bridges
b. Salt bridges & disulfide bond d. Salt bridges and hydrogen bond.
51. The American biochemist who introduced the induced-fit model of enzyme action;
a. Gerardus Mulder c. Emil Fischer
b. Linus Pauling d. Daniel Koshland
52. Myoglobin, casein, and ferritin according to function are;
a. Protective protein c. Storage protein
b. Transport protein d. Catalytic protein
53. They demonstrated that each gene control the manufacture of one specific protein and the
external and internal characteristics are expressed through this gene;
a. James Watson and Francis Crick c. Oswald Avery and George Beadle
b. George Beadle and Edward Tatum d. Rosalind Franklin and Maurice Wilkins
54. A type of enzyme regulation in which formation of product inhibit an earlier reaction in the
sequence;
a. Allosterism c. Feedback control
b. Isoenzyme d. Protein modification
55. The following are polar, aliphatic amino acids; EXCEPT;
a. Serine c. Threonine
b. Isoleucine d. Glutamine
56. The type of RNA molecule that help in the processing of the initial mRNA transcribed from DNA
into a mature form;
a. miRNA c. snRNA
b. siRNA d. tRNA
57. During glycolysis, the isomerization of dihydroxyacetone phosphate to glyceraldehyde-3-
phosphate is catalyzed by an enzyme;
a. Triosphosphate dehydrogenase c. Triosphosphate mutase
b. Triosphosphate isomerase d. Triosphosphate decarboxylase
58. An event that occurs at a site other than the active site of an enzyme but that eventually affect the
active site;
a. Feedback control c. Proenzyme activation
b. Allosterism d. Protein modification
59. The shape of α – helix secondary protein structure is maintained by;
a. Disulfide bond c. Intramolecular hydrogen bond
b. Intermolecular hydrogen bond d. Salt bridges
60. Enzyme protein according to function is a;
a. Catalytic protein c. Protective protein
b. Regulatory protein d. Hormone protein
61. 2-amino-6-oxypurine is;
a. Adenine c. Cytosine
b. Uracil d. Guanine
62. The cleavage of ketoacyl-CoA to acyl-CoA and acetyl-CoA during the final step of β – oxidation
is catalyzed by an enzyme;
a. Thiolase c.Enolase
b. Hydratase d.Aldolase
63. Non-hydrolytic cleavage is also known as;
a. Biochemical combination reaction c. Decomposition reaction
b. Oxidation reaction d. Isomerization reaction
64. The enzyme that catalyze the hydrolysis of dextrin and maltose to simple sugar in the small
intestine;
a. Amylopsin c. Ptyalin
b. Steapsin d. Gastrin
65. Methyl benzene is the side chain of;
a. Serine c. Phenylalanine
b. Threonine d. Asparagine

66. The stage of nitrogen metabolism involving the conversion of glutamate to α – ketoglutarate;
a. Nitrogen fixation c. Urea cycle
b. Oxidative deamination d. Transamination
67. Which region of protein molecule is affected by salts of heavy metals during denaturation;
a. Salt bridges & hydrogen bond c. Hydration layer & hydrogen bond
b. Salt bridges and disulfide bone d. Hydrophobic interaction
68. During RNA synthesis if the exposed nitrogen base of the unwinded strand is adenine; the free
nucleotide transported to the site to build a new strand must _______ as nitrogen base;
a. Guanine c. Uracil
b. Thymine d. Cytosine
69. The mechanism of enzyme action that states that the surface of an enzyme contain an active site
having a restricted opening in which only one kind of substrate can fit;
a. Induced-fit model c. Lock-and-key model
b. Competitive enzyme model d. Non-competitive enzyme model
70. An enzyme that belong to a subclass of isomerase that catalyzes intramolecular rearrangement;
a. Aldolase c. Enolase
b. Mutase d. Synthetase
71. The cleavage/breakdown of fructose-1,6-biphosphate to dihydroxyacetone phosphate and D-
glyceraldehyde-3-phosphate is catalyzed by an enzyme;
a. Enolase c. Aldolase
b. Phosphatase d. Dehydrogenase
72. Methyl-indole is the side chain of which amino acid?
a. Tryptophan c. Tyrosine
b. Methionine d. Phenylalanine
73. The following are the genetic code to stop protein synthesis, EXCEPT;
a. AAU c. UAA
b. UAG d. UGA
74. A nona-peptide protein also known as antidiuretic hormone;
a. Oxytocin c. Estrone
b. Prolactin d. Vasopressin
75. Which the following is the side chain of amino acid serine?
a. – CHOH – CH3 c. – CH2 – CO – NH2
b. – CH3- OH d. – CH2 – CH2 – CO – NH2
76. 2-oxy-5-aminopyrimidine is;
a. Thymine c. Uracil
b. Guanine d. Cytosine
77. An apoenzyme together with co-factor and co-enzyme form a complete enzyme called;
a. Allosteric enzyme c. Zymogen
b. Proenzyme d. Holoenzyme
78. Chemical bond that help stabilize tertiary structure of protein formed between polar groups of the
side chain or between side chain and peptide backbone;
a. Disulfide bonding c. Salt bridges
b. Hydrogen bonding d. Electrostatic attraction
79. Each enzyme operate best within narrow pH range usually between;
a. 3 – 5.4 c. 5.4 – 8
b. 5.4 – 7.5 d. 7.5 – 8.5
80. In the genes of eukaryotic organism, the stretch of nucleotide sequence that codes for protein are
called;
a. Exons c. Introns
b. Axons d. None of these
81. An enzyme that catalyze the hydrolysis of starch to a shorter polysaccharide fragments called
dextrin and maltose in the mouth during salivary digestion;
a. Amylopsin c. Steapsin
b. Gastrin d. Ptyalin
82. Amino acid where there side chain are attracted to a magnesium ion forming a bridge called metal
ion coordination;
a. Aspartic acid c. Asparagine
b. Serine d. Glutamic acid

83. Inactive form of enzymes are called;


a. Co-enzyme c. Apoenzyme
b. Holoenzyme d. Proenzyme
84. A genetic disorder resulting from the body’s lack of ceruplasmin;
a. Wilson’s disease c. Duchenne’s muscular dystrophy
b. Albinism d. Phenylketonuria
85. The following protein molecule exist in a quaternary protein structure; EXCEPT;
a. Hemoglobin c. Collagen
b. Tropocollagen d. Integral membrane protein
86. The following are proteinases enzyme, EXCEPT;
a. Pepsin c. Trypsin
b. Aminopeptidase d. Chymotrypsin
87. The following are chemical denaturant, EXCEPT;
a. UV rays c. Strong alkaloidal reagent
b. Salt of heavy metal d. Strong mineral acid
88. Substances that render active enzyme inactive or less active are called;
a. Activator c. Inhibitor
b. Regulator d. Operator
89. The type of RNA molecule that attaches to individual amino acids and transport them to the
ribosomes where they are linked together to form protein;
a. rRNA c. siRNA
b. snRNA d. tRNA
90. Which amino acid has a side chain of - CH2 - SH ;
a. Methionine c. Cystiene
b. Proline d. Tyrosine
91. The temperature range where enzyme is active is between;
a. 15 – 220C c. 32 – 520C
0
b. 22 – 52 C d. 52 – 620C
92. The enzyme that catalyzed the conversion of Lactate ion to pyruvate ion during oxidation reaction
belongs to a group known as;
a. Dehydrogenase c. Decarboxylase
b. Deoxygenase d. Kinase
93. The following are basic amino acids, EXCEPT;
a. Proline c. Lysine
b. Arginine d. Histidine
94. The group of enzyme that catalyzes non-hydrolytic cleavage;
a. Ligase c. Mutase
b. Synthetase d. Lyases
95. In sickle cell hemoglobin the glutamic acid in the sixth position in normal hemoglobin is replaced
with;
a. Serine c. Glutamine
b. Leucine d. Valine
96. He envisioned the Lock-and-Key model of enzyme action;
a. Daniel Koshland c. Gerardus Mulder
b. Emil Fischer d. Linus Pauling
97. Proteases are;
a. Group of enzyme that catalyze hydrolysis of carbohydrates
b. Group of enzyme that catalyze hydrolysis of protein
c. Group of enzyme that catalyze hydrolysis of nucleic acid
d. Group of enzyme that catalyze hydrolysis of simple & complex lipid
98. The orderly alignment of β – pleated secondary protein structure if maintained by;
a. Intermolecular hydrogen bond c. Intramolecular hydrogen bond
b. Disulfide bond d. Electrostatic attraction
99. The Dutch chemist who first used the term protein to name a specific group of substance
abundant in plants and animals;
a. Linus Pauling c. Daniel Koshland
b. Gerardus Mulder d. Emil Fischer
100. In nucleosome eight histone molecules are surrounded by DNA double helix consisting of
_____ base pair;
a. 127 c. 147
b. 137 d. 157
Prepared by:

Dr. Allan A. Sales, DMD, MAT-MRS


Department of Biological Sciences
UEP, College of Science

College of Science
Department of Physical Sciences
Removal Examination in Chemistry 2
BIOCHEMISTRY
2nd Semester 2015 – 2016

Name: _______________________________________ Date of Exam: ______________


Course & Section: ______________________________ Rating: ___________________

ANSWER SHEET

MULTIPLE CHOICE

1. [ A ] [ B ] [ C ] [ D ] 36. [ A ] [ B ] [ C ] [ D ] 71. [ A ] [ B ] [ C ] [ D ]

2. [ A ] [ B ] [ C ] [ D ] 37. [ A ] [ B ] [ C ] [ D ] 72. [ A ] [ B ] [ C ] [ D ]
3. [ A ] [ B ] [ C ] [ D ] 38. [ A ] [ B ] [ C ] [ D ] 73. [ A ] [ B ] [ C ] [ D ]
4. [ A ] [ B ] [ C ] [ D ] 39. [ A ] [ B ] [ C ] [ D ] 74. [ A ] [ B ] [ C ] [ D ]
5. [ A ] [ B ] [ C ] [ D ] 40. [ A ] [ B ] [ C ] [ D ] 75. [ A ] [ B ] [ C ] [ D ]
6. [ A ] [ B ] [ C ] [ D ] 41. [ A ] [ B ] [ C ] [ D ] 76. [ A ] [ B ] [ C ] [ D ]
7. [ A ] [ B ] [ C ] [ D ] 42. [ A ] [ B ] [ C ] [ D ] 77. [ A ] [ B ] [ C ] [ D ]
8. [ A ] [ B ] [ C ] [ D ] 43. [ A ] [ B ] [ C ] [ D ] 78. [ A ] [ B ] [ C ] [ D ]
9. [ A ] [ B ] [ C ] [ D ] 44. [ A ] [ B ] [ C ] [ D ] 79. [ A ] [ B ] [ C ] [ D ]
10. [ A ] [ B ] [ C ] [ D ] 45. [ A ] [ B ] [ C ] [ D ] 80. [ A ] [ B ] [ C ] [ D ]
11. [ A ] [ B ] [ C ] [ D ] 46. [ A ] [ B ] [ C ] [ D ] 81. [ A ] [ B ] [ C ] [ D ]
12. [ A ] [ B ] [ C ] [ D ] 47. [ A ] [ B ] [ C ] [ D ] 82. [ A ] [ B ] [ C ] [ D ]
13. [ A ] [ B ] [ C ] [ D ] 48. [ A ] [ B ] [ C ] [ D ] 83. [ A ] [ B ] [ C ] [ D ]
14. [ A ] [ B ] [ C ] [ D ] 49. [ A ] [ B ] [ C ] [ D ] 84. [ A ] [ B ] [ C ] [ D ]
15. [ A ] [ B ] [ C ] [ D ] 50. [ A ] [ B ] [ C ] [ D ] 85. [ A ] [ B ] [ C ] [ D ]
16. [ A ] [ B ] [ C ] [ D ] 51. [ A ] [ B ] [ C ] [ D ] 86. [ A ] [ B ] [ C ] [ D ]
17. [ A ] [ B ] [ C ] [ D ] 52. [ A ] [ B ] [ C ] [ D ] 87. [ A ] [ B ] [ C ] [ D ]
18. [ A ] [ B ] [ C ] [ D ] 53. [ A ] [ B ] [ C ] [ D ] 88. [ A ] [ B ] [ C ] [ D ]
19. [ A ] [ B ] [ C ] [ D ] 54. [ A ] [ B ] [ C ] [ D ] 89. [ A ] [ B ] [ C ] [ D ]
20. [ A ] [ B ] [ C ] [ D ] 55. [ A ] [ B ] [ C ] [ D ] 90. [ A ] [ B ] [ C ] [ D ]
21. [ A ] [ B ] [ C ] [ D ] 56. [ A ] [ B ] [ C ] [ D ] 91. [ A ] [ B ] [ C ] [ D ]
22. [ A ] [ B ] [ C ] [ D ] 57. [ A ] [ B ] [ C ] [ D ] 92. [ A ] [ B ] [ C ] [ D ]
23. [ A ] [ B ] [ C ] [ D ] 58. [ A ] [ B ] [ C ] [ D ] 93. [ A ] [ B ] [ C ] [ D ]
24. [ A ] [ B ] [ C ] [ D ] 59. [ A ] [ B ] [ C ] [ D ] 94. [ A ] [ B ] [ C ] [ D ]
25. [ A ] [ B ] [ C ] [ D ] 60. [ A ] [ B ] [ C ] [ D ] 95. [ A ] [ B ] [ C ] [ D ]
26. [ A ] [ B ] [ C ] [ D ] 61. [ A ] [ B ] [ C ] [ D ] 96. [ A ] [ B ] [ C ] [ D ]
27. [ A ] [ B ] [ C ] [ D ] 62. [ A ] [ B ] [ C ] [ D ] 97. [ A ] [ B ] [ C ] [ D ]
28. [ A ] [ B ] [ C ] [ D ] 63. [ A ] [ B ] [ C ] [ D ] 98. [ A ] [ B ] [ C ] [ D ]
29. [ A ] [ B ] [ C ] [ D ] 64. [ A ] [ B ] [ C ] [ D ] 99. [ A ] [ B ] [ C ] [ D ]
30. [ A ] [ B ] [ C ] [ D ] 65. [ A ] [ B ] [ C ] [ D ] 100. [ A ] [ B ] [ C ] [ D ]
31. [ A ] [ B ] [ C ] [ D ] 66. [ A ] [ B ] [ C ] [ D ] 101. [ A ] [ B ] [ C ] [ D ]
32. [ A ] [ B ] [ C ] [ D ] 67. [ A ] [ B ] [ C ] [ D ] 102. [ A ] [ B ] [ C ] [ D ]
33. [ A ] [ B ] [ C ] [ D ] 68. [ A ] [ B ] [ C ] [ D ] 103. [ A ] [ B ] [ C ] [ D ]
34. [ A ] [ B ] [ C ] [ D ] 69. [ A ] [ B ] [ C ] [ D ] 104. [ A ] [ B ] [ C ] [ D ]
35. [ A ] [ B ] [ C ] [ D ] 70. [ A ] [ B ] [ C ] [ D ] 105. [ A ] [ B ] [ C ] [ D ]

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