Questions for preparation. Final test “Proteins. Vitamins. Enzymes”
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Question and answer variants
The primary structure in ALL proteins is stabilized with…
1. Disulfide bonds; 2. Electrostatic interactions; 3. Hydrogen bonds; 4. Peptide bonds
The secondary structure of proteins is stabilized ONLY with…
1. Disulfide bonds; 2. Electrostatic interactions; 3. Hydrogen bonds; 4. Peptide bonds
The tertiary structure of proteins is stabilized with…
1. Covalent or/and noncovalent bonds;
2. Only disulfide bridges without noncovalent bonds;
3. Only hydrogen bonds;
4. Only hydrophobic interactions;
The quaternary structure of proteins is stabilized mainly with…
1. Only hydrophobic interactions;
2. Only disulfide bridges without noncovalent bonds;
3. Only hydrogen bonds;
4. Noncovalent bonds and hydrophobic interactions;
Choose apprpriate definition for proteins:
1. Low molecular weight nitrogen containing substances;
2. Biopolymers which consist of monomeric units linked together by –O-C< covalent bonds;
3. High molecular weight substances which consist of aminoacids linked by –CO-NH- bonds;
4. Branched polymers, composed by aminoacids.
The primary structure in ALL proteins is stabilized with…
1. Disulfide bonds; 2. Electrostatic interactions; 3. Peptide bonds;
4. Hydrogen bonds
The secondary structure of proteins is stabilized ONLY with…
1. Hydrogen bonds; 2. Electrostatic interactions; 3. Disulfide bonds; 4. Peptide bonds
The tertiary structure of proteins is stabilized with…
1. Only hydrogen bonds;
2. Only disulfide bridges without noncovalent bonds;
3. Covalent or/and noncovalent bonds; 4. Only hydrophobic interactions;
The quaternary structure of proteins is stabilized mainly with…
1. Only hydrophobic interactions;
2. Noncovalent bonds and hydrophobic interactions;
3. Only hydrogen bonds;
4. Only disulfide bridges without noncovalent bonds;
Choose apprpriate definition for proteins:
1. Branched polymers, composed by aminoacids;
2. Low molecular weight nitrogen containing substances;
3. Biopolymers which consist of monomeric units linked together by –O-C< covalent bonds;
4. High molecular weight substances which consist of aminoacids linked by –CO-NH- bonds;
At neutral pH peptide Val-Gly-His-Pro-Arg…
1. carries positive charge and is moving towards anode.
2. carries positive charge and is moving towards cathode.
3. carries negative charge and is moving towards cathode.
4. carries negative charge and is moving towards anode.
At pH=3 peptide Val-Glu-Phe-Pro-Arg…
1. carries positive charge and is moving towards anode.
2. carries positive charge and is moving towards cathode.
3. carries negative charge and is moving towards cathode.
4. carries negative charge and is moving towards anode.
At pH=10 peptide Gln-Glu-His-Met-Arg…
1. carries positive charge and is moving towards anode.
2. carries positive charge and is moving towards cathode.
3. carries negative charge and is moving towards cathode.
4. carries negative charge and is moving towards anode.
Isoelectric point for peptide Phe-Ser-Asn-Lys-Pro is…
1. near pH 7,0;
2. in acidic zone of pH values;
3. in basic zone of pH values;
Isoelectric point for peptide Glu-Trp-Asn-Phe-Pro is…
1. near pH 7,0;
2. in acidic zone of pH values;
3. in basic zone of pH values;
At neutral pH peptide Val-Gly-Glu-Pro-Glu…
1. carries positive charge and is moving towards anode.
2. carries positive charge and is moving towards cathode.
3. carries negative charge and is moving towards cathode.
4. carries negative charge and is moving towards anode.
At pH=3 peptide Val-Glu-Phe-Pro-Ser…
1. carries positive charge and is moving towards anode.
2. carries positive charge and is moving towards cathode.
3. carries negative charge and is moving towards cathode.
4. carries negative charge and is moving towards anode.
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At pH=10 peptide Glu-Arg-His-Trp-Ala…
1. carries positive charge and is moving towards anode.
2. carries positive charge and is moving towards cathode.
3. carries negative charge and is moving towards cathode.
4. carries negative charge and is moving towards anode.
Isoelectric point for peptide Phe-Ser-Asn-Asp-Ile is…
1. near pH 7,0;
2. in acidic zone of pH values;
3. in basic zone of pH values;
Isoelectric point for peptide Gln-Thr-His-Phe-Pro is…
1. near pH 7,0;
2. in acidic zone of pH values;
3. in basic zone of pH values;
Choose protein which performs transport function:
1. Hemoglobin
2. Insulin
3. Pepsin
4. Myosin
Choose protein which performs regulatory function:
1. Hemoglobin
2. Insulin
3. Pepsin
4. Myosin
Choose protein which performs movement (contraction) function:
1. Transferrin
2. Calmodulin
3. Pepsin
4. Myosin
Choose protein which performs catalytical function:
1. Hemoglobin
2. Insulin
3. Pepsin
4. Myosin
Choose protein which performs structural function:
1. Albumin
2. Insulin
3. Collagen
4. Myosin
Choose protein which performs defensive (protective) function:
1. Immunoglobulin
2. Insulin
3. Collagen
4. Myosin
Choose protein which performs regulatory function:
1. Transferrin
2. Pepsin
3. Calmodulin
4. Myosin
Choose protein which performs catalytical function:
1. Hemoglobin
2. Insulin
3. Myosin
4. Trypsin
Choose protein which performs transport function:
1. Myosin
2. Insulin
3. Pepsin
4. Albumin
Choose protein which performs movement (contraction) function:
1. Transferrin
2. Actin
3. Pepsin
4. Calmodulin
Functional activity of protein may be changed by …
1. precipitation (salting out);
2. biuret reaction;
3. phosphorylation reaction;
4. hydration (hydratation) reaction;
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Quantitative determination of total protein concentration in blood serum may be provided using …
1. precipitation (salting out);
2. biuret reaction;
3. phosphorylation reaction;
4. hydration (hydratation) reaction;
Serum protein fractionation may be provided by…
1. precipitation (salting out);
2. biuret reaction;
3. phosphorylation reaction;
4. hydration (hydratation) reaction;
Solubility of protein in water is a result of …
1. precipitation (salting out);
2. biuret reaction;
3. phosphorylation reaction;
4. hydration (hydratation) reaction;
Breakdown of proteins in the body is a result of …
1. acid hydrolysis;
2. alkaline hydrolysis;
3. enzymatic hydrolysis;
Functional activity of protein may be changed by …
1. precipitation (salting out);
2. biuret reaction;
3. hydration (hydratation) reaction;
4. phosphorylation reaction;
Quantitative determination of total protein concentration in blood serum may be provided using …
1. precipitation (salting out);
2. phosphorylation reaction;
3. biuret reaction;
4. hydration (hydratation) reaction;
Serum protein fractionation may be provided by…
1. hydration (hydratation) reaction;
2. biuret reaction;
3. phosphorylation reaction;
4. precipitation (salting out);
Solubility of protein in water is a result of …
1. hydration (hydratation) reaction;
2. precipitation (salting out);
3. phosphorylation reaction;
4. biuret reaction;
Breakdown of proteins in the body is a result of …
1. enzymatic hydrolysis;
2. alkaline hydrolysis;
3. acid hydrolysis;
Denaturation of proteins may be induced by…
1. Adding a neutral salt to protein aqueous solution.
2. Adding a heavy metal salt to protein aqueous solution.
3. Cooling of protein aqueous solution to 5C
4. Heating of protein aqueous solution to 30C.
Denaturation of proteins may be induced by…
1. Adding a large amount of neutral salt to protein aqueous solution.
2. Changes in primary structure.
3. Cooling of protein aqueous solution to 5C
4. X-rays radiation
Denaturation of proteins may be induced by…
1. Adding a neutral salt to protein aqueous solution.
2. Changes in primary structure.
3. Heating of protein aqueous solution to 60C.
4. Heating of protein aqueous solution to 30C.
Velocity of protein movement during electrophoresis is highest for protein with moecular weight…
1. 5,7 kDa;
2. 16,2 kDa;
3. 38,1 kDa;
4. 100,6 kDa
Velocity of protein movement towards cathode during electrophoresis is highest for protein with net charge…
1. -5;
2. +4;
3. +16;
4. -20;
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Denaturation of proteins may be induced by…
1. Adding a heavy metal salt to protein aqueous solution.
2. Adding a neutral salt to protein aqueous solution.
3. Heating of protein aqueous solution to 30C.
4. Cooling of protein aqueous solution to 5C.
Denaturation of proteins may be induced by…
1. Adding a large amount of neutral salt to protein aqueous solution
2. X-rays radiation
3. Cooling of protein aqueous solution to 5C
4. Changes in primary structure
Denaturation of proteins may be induced by…
1. Adding a neutral salt to protein aqueous solution.
2. Changes in primary structure.
3. Heating of protein aqueous solution to 30C.
4. Heating of protein aqueous solution to 60C.
Velocity of protein movement during electrophoresis is highest for protein with moecular weight…
1. 15,3 kDa;
2. 31,7 kDa;
3. 56,1 kDa;
4. 113,6 kDa
Velocity of protein movement towards cathode during electrophoresis is highest for protein with net charge…
1. +8;
2. -4;
3. -12;
4. -6;
Choose a ligand which may be bound with Hb (hemoglobin):
1. Fatty acids;
2. Iron (ionized form);
3. Oxygen (molecular);
4. Arginin;
Choose a ligand which may be bound with transferrin:
1. Fatty acids;
2. Iron (ionized form);
3. Oxygen (molecular);
4. Arginin;
Choose a ligand which may be bound with arginase:
1. Fatty acids;
2. Iron (ionized form);
3. Oxygen (molecular);
4. Arginin;
Choose a ligand which may be bound with albumin:
1. Fatty acids;
2. Iron (ionized form);
3. Oxygen (molecular);
4. Arginin;
Choose a ligand which may be bound with α-adrenoreceptor:
1. Fatty acids;
2. Epinephrin;
3. Glucagon;
4. Arginin;
Choose a ligand which may be bound with Hb (hemoglobin):
1. Fatty acids;
2. Iron (ionized form);
3. Arginin;
4. Oxygen (molecular);
Choose a ligand which may be bound with transferrin:
1. Iron (ionized form);
2. Fatty acids;
3. Oxygen (molecular);
4. Arginin;
Choose a ligand which may be bound with arginase:
1. Arginin;
2. Iron (ionized form);
3. Oxygen (molecular);
4. Fatty acids;
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Choose a ligand which may be bound with albumin:
1. Oxygen (molecular);
2. Fatty acids;
3. Iron (ionized form);
4. Arginin;
Choose a ligand which may be bound with β-adrenoreceptor:
1. Fatty acids;
2. Glucagon;
3. Epinephrin;
4. Arginin;
Choose type of bond which participates in stabilization of primary structure of protein:
1. hydrogen bond
2. sulfur-sulfur (disulfide) bond
3. peptide bond
4. salt bridge
Choose type of bond which participates in stabilization of secondary structure of protein:
1. hydrogen bond
2. sulfur-sulfur (disulfide) bond
3. peptide bond
4. salt bridge
Disulfide bridges participate in stabilization of …
1. primary structure;
2. secondary structure;
3. tertiary structure;
4. quaternary structure;
Ion-ion (electrostatic) interaction may be formed by functional groups in side chains of…
1. Asn and Glu;
2. Lys and Asp;
3. Phe and His;
4. Met and Gly;
Hydrophobic interactions may be formed by side chains of…
1. Asp and Glu;
2. Lys and Asp;
3. Phe and Val;
4. Trp and Gly;
Choose type of bond which participates in stabilization of primary structure of protein:
1. salt bridge
2. peptide bond
3. sulfur-sulfur (disulfide) bond
4. hydrogen bond
Choose type of bond which participates in stabilization of secondary structure of protein:
1. sulfur-sulfur (disulfide) bond
2. peptide bond
3. hydrogen bond
4. salt bridge
Disulfide bridges participate in stabilization of …
1. quaternary structure;
2. tertiary structure;
3. secondary structure;
4. primary structure;
Ion-ion (electrostatic) interaction may be formed by functional groups in side chains of…
1. Asn and Glu;
2. Met and Gly;
3. Phe and His;
4. His and Glu;
Hydrophobic interactions may be formed by side chains of…
1. Ala and Leu;
2. Asp and Glu;
3. Lys and Asn;
4. Trp and Gln;
Total serum protein concentration in healthy adult persons is within range…
1. 45-65 g/l;
2. 65-85 g/l;
3. 45-75 g/l;
4. 65-100 g/l;
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Choose essential aminoacid:
1. Asn;
2. Trp;
3. Glu;
4. Tyr;
Hypoproteinemia may be caused by…
1. Starvation;
2. Inflammation;
3. Dehydratation;
4. Large amount of protein in food;
Hypoproteinemia may be caused by…
1. Dehydratation;
2. Malabsorbtion;
3. Inflammation;
4. Large amount of protein in food;
Hyperproteinemia may be caused by…
1. Starvation;
2. Inflammation;
3. Malabsorbtion;
4. Absence of aminoacid Thr in food proteins;
Total serum protein concentration in healthy adult persons is within range…
1. 45-65 g/l;
2. 45-75 g/l;
3. 65-85 g/l;
4. 55-95 g/l;
Choose essential aminoacid:
1. Cis;
2. Asp;
3. Ser;
4. Met;
Hypoproteinemia may be caused by…
1. Large amount of protein in food;
2. Inflammation;
3. Dehydratation;
4. Absence of lysine in food proteins;
Hypoproteinemia may be caused by…
1. Large amount of protein in food;
2. Inflammation;
3. Disorders of protein digestion in intestine;
4. Dehydratation;
Hyperproteinemia may be caused by…
1. Malabsorbtion;
2. Absence of Leu in food proteins;
3. Disorders of protein digestion in intestine;
4. Dehydratation;
Name the given structure of coenzyme (full name and abbreviation) OR vitamin (name and its letter index) on Fig.1
The name of disease which is a result of severe thiamin deficiency is…
1. Beri-beri;
2. Scurvey;
3. Pellagra;
4. Rickets;
The name of disease which is a result of severe ascorbic acid deficiency is…
1. Beri-beri;
2. Pellagra;
3. Scurvey;
4. Rickets;
The name of disease which is a result of severe niacin deficiency is…
1. Beri-beri;
2. Pellagra;
3. Scurvey;
4. Rickets;
The name of disease which is a result of severe vitamin D deficiency is…
1. Pernicious anemia;
2. Scurvey;
3. Pellagra;
4. Rickets;
The name of disease which is a result of severe cobalamin deficiency is…
1. Pernicious anemia;
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2. Scurvey;
3. Pellagra;
4. Rickets;
The name of disease which is a result of severe vitamin D deficiency is…
1. Pernicious anemia;
2. Rickets;
3. Pellagra;
4. Scurvey;
The name of disease which is a result of severe cobalamin deficiency is…
1. Rickets;
2. Scurvey;
3. Pellagra;
4. Pernicious anemia;
The name of disease which is a result of severe thiamin deficiency is…
1. Pellagra;
2. Beri-beri;
3. Scurvey;
4. Rickets;
The name of disease which is a result of severe ascorbic acid deficiency is…
1. Beri-beri;
2. Pellagra;
3. Rickets;
4. Scurvey;
The name of disease which is a result of severe niacin deficiency is…
1. Pellagra;
2. Beri-beri;
3. Scurvey;
4. Rickets;
Antivitamin for folic acid is…
1. Dicumarol
2. Atabrine
3. Aminopterin
4. Avidin
Antivitamin for vitamin K is…
1. Dicumarol
2. Atabrine
3. Aminopterin
4. Avidin
Antivitamin for biotin is…
1. Dicumarol
2. Atabrine
3. Aminopterin
4. Avidin
Antivitamin for riboflavin is…
1. Dicumarol
2. Atabrine
3. Aminopterin
4. Avidin
Antivitamin for vitamin B1 is…
1. Atabrine
2. Aminopterin
3. Avidin
4. Thiaminase
Antivitamin for folic acid is…
1. Dicumarol
2. Atabrine
3. Avidin
4. Aminopterin
Antivitamin for vitamin K is…
1. Aminopterin
2. Dicumarol
3. Atabrine
4. Avidin
Antivitamin for biotin is…
1. Dicumarol
2. Aminopterin
3. Avidin
4. Atabrine
Antivitamin for riboflavin is…
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1. Dicumarol
2. Atabrine
3. Aminopterin
4. Avidin
Antivitamin for vitamin B1 is…
1. Thiaminase
2. Aminopterin
3. Avidin
4. Atabrine
Vitamin A function is…
1. Lys and Pro hydroxylation;
2. regulation of Ca metabolism;
3. γ-carboxyglutamate formation;
4. prosthetic group for light-sensitive proteins;
Vitamin E function is…
1. antioxidant;
2. regulation of Ca metabolism;
3. γ-carboxyglutamate formation;
4. prosthetic group for light-sensitive proteins;
Vitamin K function is…
1. antioxidant;
2. regulation of Ca metabolism;
3. γ-carboxyglutamate formation;
4. prosthetic group for light-sensitive proteins;
Vitamin D function is…
1. prosthetic group for light-sensitive proteins;
2. Lys and Pro hydroxylation;
3. regulation of Ca metabolism;
4. γ-carboxyglutamate formation.
Vitamin C function is…
1. Lys and Pro hydroxylation;
2. regulation of Ca metabolism;
3. prosthetic group for light-sensitive proteins;
4. γ-carboxyglutamate formation.
Vitamin A function is…
1. Lys and Pro hydroxylation;
2. regulation of Ca metabolism;
3. prosthetic group for light-sensitive proteins;
4. γ-carboxyglutamate formation.
Vitamin E function is…
1. antioxidant;
2. regulation of Ca metabolism;
3. γ-carboxyglutamate formation;
4. prosthetic group for light-sensitive proteins;
Vitamin K function is…
1. antioxidant;
2. regulation of Ca metabolism;
3. γ-carboxyglutamate formation;
4. prosthetic group for light-sensitive proteins;
Vitamin D function is…
1. Lys and Pro hydroxylation;
2. regulation of Ca metabolism;
3. prosthetic group for light-sensitive proteins;
4. γ-carboxyglutamate formation.
Vitamin C function is…
1. prosthetic group for light-sensitive proteins;
2. Lys and Pro hydroxylation;
3. regulation of Ca metabolism;
4. γ-carboxyglutamate formation.
Folic acid in its active form participates in…
1. Collagen synthesis;
2. One carbon fragments transfer;
3. Calcium-binding proteins synthesis;
4. Blood clotting proteins synthesis;
Coenzyme A participates in…
1. Fatty acids metabolism;
2. Amino acids decarboxylation;
3. Oxidative decarboxylation of α-ketoacids (pyruvate, α-ketoglutarate);
4. One-carbon fragments transfer;
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Thiamin in its active form participates in…
1. Amino acids transamination and decarboxylation;
2. One-carbon fragments transfer;
3. Amino acids oxidation;
4. Oxidative decarboxylation of α-ketoacids (pyruvate, α-ketoglutarate);
Riboflavin is necessary for…
1. Oxidation and reduction reactions;
2. Carboxylation reactions in gluconeogenesis and fatty acids synthesis;
3. Transamination of aminoacids reactions;
4. Calcium-binding proteins synthesis;
Pyridoxin in its active form participates in…
1. Methionine synthesis;
2. Oxidation and reduction reactions;
3. One carbon fragments transfer;
4. Transamination and decarboxylation of aminoacids;
Cobalamin is necessary for…
1. One carbon fragments transfer (methylation);
2. Oxidation and reduction reactions;
3. Transamination of aminoacids reactions;
4. Carboxylation reactions;
Niacin in its active form participate in…
1. Methionine synthesis;
2. Aminotransferase reaction;
3. Oxydation and reduction reactions;
4. Decarboxylation of amino acids;
Pyridoxin in its active form participates in…
1. Methionine synthesis;
2. Oxidation and reduction reactions;
3. Transamination and decarboxylation of aminoacids;
4. One carbon fragments transfer;
Cobalamin is necessary for…
1. Transamination of aminoacids reactions;
2. Isomerization reaction;
3. Oxidation and reduction reactions;
4. Carboxylation reactions;
Biotin is necessary for…
1. Transamination and decarboxylation of aminoacids;
2. Blood clotting proteins synthesis;
3. Oxidative decarboxylation of α-ketoacids (pyruvate, α-ketoglutarate);
4. Carboxylation reactions;
Tetrahydrofolate is the derivative of:
1. Fitinic acid;
2. Folic acid;
3. Fumaric acid;
4. Formic acid;
NAD is the active form of:
1. Vitamin P.
2. Vitamin F.
3. Vitamin PP.
4. Vitamin A.
FAD is the derivative of:
1. Vitamin B2;
2. Vitamin B6;
3. Vitamin B12;
4. Vitamin B1.
Thiamin pyrophosphate is the active form of:
1. Vitamin A;
2. Vitamin B6;
3. Vitamin B12;
4. Vitamin B1.
Water-soluble vitamins include:
1. Tocotrienols;
2. Calciferol;
3. Pyridoxin;
4. Retinol;
Water-soluble vitamins include…
1. Tocotrienols;
2. Cobalamin;
3. Calciferol;
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4. Retinol;
Water-soluble vitamins include…
1. Calciferol;
2. Tocoferol;
3. Riboflavin;
4. Retinol;
Lipid-soluble vitamins include…
1. Ascorbate;
2. Niacin;
3. Retinol;
4. Pyridoxin;
Lipid-soluble vitamins include…
1. Piridoxin;
2. Tocoferols;
3. Pantothenic acid;
4. Riboflavin;
HS-CoA is an active form of vitamin…
1. Pantothenic acid
2. Cobalamin;
3. Niacin;
4. Riboflavin;
Lipoic acid is a representative of enzymes cofactor class…
1. Aromatic;
2. Aliphatic;
3. Nucleotides;
4. Heterocycles;
Ubiquinone is a representative of enzymes cofactor class…
1. Heterocycles;
2. Aliphatic;
3. Nucleotides;
4. Aromatic;
Pyridoxal phosphate is a representative of enzymes cofactor class…
1. Heterocycles;
2. Aliphatic;
3. Nucleotides;
4. Aromatic;
ATP is a representative of enzymes cofactor class…
1. Heterocycles;
2. Aliphatic;
3. Nucleotides;
4. Aromatic;
Thiamin diphosphate is a representative of enzymes cofactor class…
1. Nucleotides;
2. Heterocycles;
3. Aliphatic;
4. Aromatic;
Coenzyme A is a representative of enzymes cofactor class…
1. Heterocycles;
2. Aliphatic;
3. Aromatic;
4. Nucleotides;
NAD is a representative of enzymes cofactor class…
1. Nucleotides;
2. Aliphatic;
3. Aromatic;
4. Heterocycles;
Heme is a representative of enzymes cofactor class…
1. Nucleotides;
2. Heterocycles;
3. Aromatic;
4. Aliphatic;
Biocitin is a representative of enzymes cofactor class…
1. Heterocycles;
2. Aliphatic;
3. Aromatic;
4. Nucleotides;
FMN is a representative of enzymes cofactor class…
1. Heterocycles;
2. Aliphatic;
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3. Aromatic;
4. Nucleotides;
Indicate the correct sequence of enzyme classes according to classification (6 digits):
1. Transferases
2. Hydrolases
3. Isomerases
4. Lyases
5. Lygases
6. Oxydoreductases
Indicate the correct sequence of enzyme classes according to classification (6 digits):
1. Lygases
2. Hydrolases
3. Isomerases
4. Lyases
5. Oxydoreductases
6. Transferases
Indicate the correct sequence of enzyme classes according to classification (6 digits):
1. Transferases
2. Lygases
3. Lyases
4. Isomerases
5. Hydrolases
6. Oxydoreductases
Indicate the correct sequence of enzyme classes according to classification (6 digits):
1. Lygases
2. Oxydoreductases
3. Isomerases
4. Lyases
5. Transferases
6. Hydrolases
Indicate the correct sequence of enzyme classes according to classification (6 digits):
1. Transferases
4. Hydrolases
2. Isomerases
5. Lyases
3. Lygases
6. Oxydoreductases
Indicate the correct sequence of enzyme classes according to classification (6 digits):
1.Lygases
4.Hydrolases
2.Isomerases
5.Lyases
3.Oxydoreductases
6.Transferases
Indicate the correct sequence of enzyme classes according to classification (6 digits):
1. Transferases
4. Lygases
2. Lyases
5. Isomerases
3. Hydrolases
6. Oxydoreductases
Indicate the correct sequence of enzyme classes according to classification (6 digits):
1. Lygases
4. Oxydoreductases
2. Isomerases
5. Lyases
3. Transferases
6. Hydrolases
Indicate the correct sequence of enzyme classes according to classification (6 digits):
1. Transferases
2. Oxydoreductases
3. Lyases
4. Isomerases
5. Lygases
6. Hydrolases
Indicate the correct sequence of enzyme classes according to classification (6 digits):
1. Hydrolases
2. Lygases
3. Isomerases
4. Lyases
5. Oxydoreductases
6. Transferases
Oxydoreductases are enzymes which catalyze…
1. Oxidation-reduction reactions;
2. Breakdown of bonds with the help of water;
3. Non-hydrolytic cleavage of bonds;
4. Interconversion of different types of isomers;
5. Covalent bonds formation using ATP;
6. Intermolecular group transfer;
Ligases are enzymes which catalyze…
1. Oxidation-reduction reactions;
2. Breakdown of bonds with the help of water;
3. Non-hydrolytic cleavage of bonds;
4. Interconversion of different types of isomers;
5. Covalent bonds formation using ATP;
6. Intermolecular group transfer;
Hydrolases are enzymes which catalyze…
1. Oxidation-reduction reactions;
2. Breakdown of bonds with the help of water;
3. Non-hydrolytic cleavage of bonds;
4. Interconversion of different types of isomers;
5. Covalent bonds formation using ATP;
6. Intermolecular group transfer;
Transferases are enzymes which catalyze…
1. Oxidation-reduction reactions;
2. Breakdown of bonds with the help of water;
3. Non-hydrolytic cleavage of bonds;
4. Interconversion of different types of isomers;
5. Covalent bonds formation using ATP;
6. Intermolecular group transfer;
Isomerases are enzymes which catalyze…
1. Oxidation-reduction reactions;
2. Breakdown of bonds with the help of water;
3. Non-hydrolytic cleavage of bonds;
4. Interconversion of different types of isomers;
5. Covalent bonds formation using ATP;
6. Intermolecular group transfer;
Lyases are enzymes which catalyze…
1. Oxidation-reduction reactions;
2. Breakdown of bonds with the help of water;
3. Intermolecular group transfer;
4. Interconversion of different types of isomers;
5. Covalent bonds formation using ATP;
6. Non-hydrolytic cleavage of bonds;
Isomerases are enzymes which catalyze…
1. Oxidation-reduction reactions;
2. Interconversion of different types of isomers;
3. Non-hydrolytic cleavage of bonds;
4. Breakdown of bonds with the help of water;
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5. Covalent bonds formation using ATP;
6. Intermolecular group transfer;
Hydrolases are enzymes which catalyze…
1. Breakdown of bonds with the help of water; 2. Oxidation-reduction reactions;
3. Non-hydrolytic cleavage of bonds;
4. Interconversion of different types of isomers;
5. Covalent bonds formation using ATP;
6. Intermolecular group transfer;
Oxydoreductases are enzymes which catalyze…
1. Interconversion of different types of isomers; 2. Breakdown of bonds with the help of water;
3. Non-hydrolytic cleavage of bonds;
4. Oxidation-reduction reactions;
5. Covalent bonds formation using ATP;
6. Intermolecular group transfer;
Transferases are enzymes which catalyze…
1. Oxidation-reduction reactions;
2. Breakdown of bonds with the help of water;
3. Non-hydrolytic cleavage of bonds;
4. Interconversion of different types of isomers;
5. Intermolecular group transfer;
6. Covalent bonds formation using ATP;
Choose type of functional site which is responsible for binding with phosphate group (additional enzyme is required for
this reaction):
1. Active site; 2. Allosteric site; 3. Site for covalent modification; 4. Site for protein-protein interaction;
Choose type of functional site which is responsible for binding with protein calmodulin:
1. Active site; 2. Allosteric site; 3. Site for covalent modification; 4. Site for protein-protein interaction;
Choose type of functional site which is responsible for binding with substrate:
1. Active site; 2. Allosteric site; 3. Site for covalent modification; 4. Site for protein-protein interaction;
Choose type of functional site which is responsible for binding with low-molecular weight inhibitor:
1. Active site; 2. Allosteric site; 3. Site for covalent modification; 4. Site for protein-protein interaction;
Choose type of functional site which is responsible for binding with low-molecular weight activator:
1. Active site; 2. Allosteric site; 3. Site for covalent modification; 4. Site for protein-protein interaction;
Choose type of functional site which is responsible for binding with phosphate group (additional enzyme is required for
this reaction):
1. Allosteric site; 2. Active site; 3. Site for protein-protein interaction; 4. Site for covalent modification;
Choose type of functional site which is responsible for binding with low-molecular weight activator:
1. Allosteric site; 2. Active site; 3. Site for protein-protein interaction; 4. Site for covalent modification;
Choose type of functional site which is responsible for binding with substrate:
1. Allosteric site; 2. Active site; 3. Site for protein-protein interaction; 4. Site for covalent modification;
Choose type of functional site which is responsible for binding with low-molecular weight inhibitor:
1. Allosteric site; 2. Active site; 3. Site for protein-protein interaction; 4. Site for covalent modification;
Choose type of functional site which is responsible for binding with protein calmodulin:
1. Allosteric site; 2. Active site; 3. Site for protein-protein interaction; 4. Site for covalent modification;
Find in diagrammatic representation of the free energy changes during catalyzed and non-catalyzed reaction (Fig.2 on
additional sheet of paper, letters A,B,C,D,E,S,P) activation energy for noncatalyzed reaction;
Find in diagrammatic representation of the free energy changes during catalyzed and non-catalyzed reaction (Fig.2 on
additional sheet of paper, letters A,B,C,D,E,S,P) activation energy for catalyzed reaction;
Find in diagrammatic representation of the free energy changes during catalyzed and non-catalyzed reaction (Fig.2 on
additional sheet of paper, letters A,B,C,D,E,S,P) transition state for noncatalyzed reaction;
Find in diagrammatic representation of the free energy changes during catalyzed and non-catalyzed reaction (Fig.2 on
additional sheet of paper, letters A,B,C,D,E,S,P) changes of free energy (ΔG) for noncatalyzed reaction.
Find in diagrammatic representation of the free energy changes during catalyzed and non-catalyzed reaction (Fig.2 on
additional sheet of paper, letters A,B,C,D,E,S,P) transition state for catalyzed reaction.
Find in diagrammatic representation of the free energy changes during catalyzed and non-catalyzed reaction (Fig.2 on
additional sheet of paper, letters A,B,C,D,E,S,P) changes of free energy (ΔG) for catalyzed reaction.
Find in diagrammatic representation of the free energy changes during catalyzed and non-catalyzed reaction (Fig.2 on
additional sheet of paper, letters A,B,C,D,E,S,P) activation energy for noncatalyzed reaction;
Find in diagrammatic representation of the free energy changes during catalyzed and non-catalyzed reaction (Fig.2 on
additional sheet of paper, letters A,B,C,D,E,S,P) activation energy for catalyzed reaction.
Find in diagrammatic representation of the free energy changes during catalyzed and non-catalyzed reaction (Fig.2 on
additional sheet of paper, letters A,B,C,D,E,S,P) internal energy level of substrate.
Find in diagrammatic representation of the free energy changes during catalyzed and non-catalyzed reaction (Fig.2 on
additional sheet of paper, letters A,B,C,D,E,S,P) internal energy level of reaction product.
If in the presence of inhibitor Km is increased, …
1. The affinity of enzyme to substrate is increased, it is competitive inhibition.
2. The affinity of enzyme to substrate is increased, it is noncompetitive inhibition
3. The affinity of enzyme to substrate is decreased, it is competitive inhibition.
4. The affinity of enzyme to substrate is decreased, it is noncompetitive inhibition.
If in the presence of inhibitor Vmax is decreased, …
1. The affinity of enzyme to substrate is not changed, it is competitive inhibition.
2. The affinity of enzyme to substrate is not changed, it is noncompetitive inhibition.
3. The affinity of enzyme to substrate is decreased, it is competitive inhibition
4. The affinity of enzyme to substrate is decreased, it is noncompetitive inhibition.
If in the presence of inhibitor Km remains the same, …
1. It is competitive inhibition, and affinity of enzyme to substrate is increased.
2. It is noncompetitive inhibition, and affinity of enzyme to substrate is increased.
3. It is competitive inhibition, and affinity of enzyme to substrate is not changed.
4. It is noncompetitive inhibition, and affinity of enzyme to substrate is not changed.
If in the presence of inhibitor Vmax remains the same, …
1. It is competitive inhibition, and affinity of enzyme to substrate is increased..
2. It is competitive inhibition, and affinity of enzyme to substrate is decreased.
3. It is noncompetitive inhibition, and affinity of enzyme to substrate is increased..
4. It is noncompetitive inhibition, and affinity of enzyme to substrate is decreased.
185
Fig.2
Fig.1
O
O
H
HO
CH2
H3C
O PO3H2
H3C
N
H3C
N
N
CH2
C
CH2 CH2 NH C C
H
O
O
C
O
OH
CH2 O
P O
CH3
O
NH2
N
HO P O
CH2
N
O
SH
N
CH2
P
OH
N
H2N
N
H
N
O
C
H2
N
N
H
N
H
N
H
CH2
N
H3C
N
H H H
C C C C CH2 O P
H2
OH OH OH
OH CH3
HN
NH
NH2
CH3
N
S
C
H2
OH
O
H
C
C
H2
COOH
O
C
H2
O
C
H2
O
O P O P OH
OH
OH
COOH
N
O
H3C
N
H3C
N
NH
O
N
O
H H H
C C C C CH2 O P OH
H2
OH OH OH
O
O
NH2
N
P OH
O
N
N
CH2
N
O
H
H
OH
H
OH
H
O
C
O
O
CH2
P OH
H
+
N
O
H
H
OH
H
OH
O
O
NH2
P OH
N
O CH2
N
N
O
N
H
H
OH
H
O-PO3H2
H
CONH2
O
C
O
O
CH2
H2C
NH2(CO)CH2
OH
H
OH
H3C
O CH2
N
O
+
Co
H
H
OH
H
OH
H
N
CH3
CH3
NH2(CO)CH2
COCH2CH2
CH3
H2C
H3C
N
N
N
N
NH2
N
CH2(CO)NH2
CH2CH2(CO)NH2
N
NH
P OH
H3C
H3C
H
H3C
H
O
O
CH2
N
H
H
P OH
NH2
+
O
NH2
CH3
CH2CH2(CO)NH2
N
CH3
N
CH3
CH O
P
O
OH
O
O
CH2OH