Mistakes Flashcards

1
Q
A

Up -> serine

Down -> Threonine

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2
Q

Which of the following amino acids have a negatively charged side chain at neutral pH?
Select one or more:

a. Arginine
b. Alanine
c. Asparagine
d. Aspartate
e. Glutamate

A

d. Aspartate

e. Glutamate

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3
Q

Which of the following amino acids have sulfur-containing side chains?
Select one or more:

a. Histidine
b. Cysteine
c. Methionine
d. Proline
e. Valine

A

b. Cysteine

c. Methionine

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4
Q

Which amino acid has a guanidine group in its side chain?

Select one:

a. Histidine
b. Lysine
c. Tyrosine
d. Arginine
e. Tryptophan

A

d. Arginine

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5
Q

Which of the following amino acids have four carbon atoms?
Select one or more:

a. Aspartate
b. Threonine
c. Asparagine
d. Proline

A

a. Aspartate
b. Threonine
c. Asparagine

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6
Q

Which of the following amino acids have five carbon atoms?

Select one or more:

a. Glutamate
b. Glutamine
c. Histidine
d. Proline
e. Glycine

A

a. Glutamate
b. Glutamine
d. Proline

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7
Q

Which of the following amino acids have six carbon atoms?

Select one or more:

a. Leucine
b. Isoleucine
c. Histidine
d. Proline
e. Glycine

A

a. Leucine
b. Isoleucine
c. Histidine

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8
Q

Pair the amino acids with their character! 1. Proline 2. Arginine 3. Glutamate
a. neutral b. acidic c. basic

Select one:

a. 1-a, 2-c, 3-b
b. 1-a, 2-b, 3-c
c. 1-b, 2-c, 3-a
d. 1-b, 2-a, 3-c
e. 1-c, 2-a, 3-b

A

a. 1-a, 2-c, 3-b

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9
Q

Select the correct statements! I

Select one or more:

a. Acidic amino acids have a net negative charge at neutral pH.
b. The isoelectric point of acidic amino acids is at acidic pH.
c. The isoelectric point of the acidic amino acids can be calculated as the average of their three pKa values.
d. Asparagine is an acidic amino acid.

A

a. Acidic amino acids have a net negative charge at neutral pH.
b. The isoelectric point of acidic amino acids is at acidic pH.

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10
Q

What is the dominant form of Arginine at pH 6.0? (pKa values of Arginine are 2.2, 9.0 and 12.5).
Select one:

a. Two positive and one negative charges
b. One positive and two negative charges
c. One negative and one positive charges
d. One negative charge e. One positive charge

A

a. Two positive and one negative charges

(Why?
1st deprotonation of alpha carboxyl group.
=> Arginine is a basic amino acid
=> (-) deprotonated alpha-carboxyl group; (+) R chain; (+) alpha-amino group
=> 2 (+) & 1 (-)

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11
Q

What is the dominant form of Glutamate at pH 7.0?
(pKa values of Glutamate are 2.2, 5.6 and 9.2).

Select one:

a. One negative charge
b. One negative and one positive charges
c. One positive and two negative charges
d. One positive charge

A

c. One positive and two negative charges

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12
Q

What is the dominant form of Histidine at pH 8.0? (pKa values of Histidine are 1.8, 6.0 and 9.2).

Select one:

a. One positive and one negative charges
b. Two negative and one positive charges
c. One negative charge
d. One positive charge

A

a. One positive and one negative charges

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13
Q

Select the correct statements!

Select one or more:

a. Glutamate has a negative charge on its side chain at the isoelectric pH.
b. Glutamate has a negative charge on its side chain at neutral pH.
c. Arginine has a positive charge on its side chain at the isoelectric pH.
d. Arginine has a positive charge on its side chain at neutral pH.

A

b. Glutamate has a negative charge on its side chain at neutral pH.
c. Arginine has a positive charge on its side chain at the isoelectric pH.
d. Arginine has a positive charge on its side chain at neutral pH.

( A is incorrect -> at isoelectric point, the deprotonation of side chain does not occur before the next pKa value)

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14
Q

Which of the following statements are true for the isoelectric form of amino acids?

Select one or more:

a. All the naturally occurring amino acids have one positive and one negative charges.
b. The a-amino group of all the naturally occurring amino acids has a positive charge.
c. The a-carboxyl group of all the naturally occurring amino acids has a negative charge.

A

All are correct

(at isoelectric point, the a-amino group is not deprotonated and have (+), whereas deprotonated carboxyl group ihas (-)
=> net charge = 0 (aka isoelectric point)

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15
Q

At neutral pH a tetrapeptide of glycylalanylarginylglutamate has…

Select one:

a. two positive and three negative charges
b. two positive and one negative charges
c. one positive and one negative charges
d. one positive and two negative charges
e. two positive and two negative charges

A

e. two positive and two negative charges

(glycine has a free amino group => (+)
Glutamate has a free carboxyl group = 1 (-)
Glutamate is acidic => 1 (-)
Arginine is basic => 1 (+)
The bonds between amino acids => 0 charge
=> Total = 2 (+) & 2 (-) )

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16
Q

The arginyllysylaspartate tripeptide has
Select one or more:

a. its isoelectric point at basic pH.
b. three positive and two negative charges at neutral pH.
c. two positive and two negative charges at its isoelectric point

A

All are correct

this tripeptide has 2 basic aa => pKI is basic

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17
Q

The chirality of an amino acid results from the fact that its a—carbon…

Select one:

a. is bonded to four different chemical groups.
b. is a carboxylic acid.
c. is symmetric.
d. is in the L absolute configuration in naturally occurring proteins.
e. has no net charge.

A

a. is bonded to four different chemical groups.

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18
Q

For amino acids with neutral side chain, at any pH below the pI of the amino acid, the population of amino acids in solution will:
Select one:

a. have a net positive charge.
b. have no charged groups.
c. have no net charge.
d. have positive and negative charges in equal concentration.
e. have a net negative charge.

A

a. have a net positive charge.

because of protonated alpha amino group

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19
Q

An octapeptide composed of four repeating glycylalanyl units has:

Select one:

a. a single free amino group on an alanyl residue.
b. two free amino and two free carboxyl groups.
c. a single free amino group on a glycyl residue and a single free carboxyl group on an alanyl residue
d. two free carboxyl groups, both on glycyl residues.
e. a single free amino group on an alanyl residue and a single free carboxyl group on a glycyl residue.

A

c. a single free amino group on a glycyl residue and a single free carboxyl group on an alanyl residue

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20
Q

The backbone of two amino acid residues in a protein can be described as (where Ca is C-alpha):

Select one:

a. Ca–C–N–Ca–C–N
b. Ca–N–Ca–C–Ca–N–Ca–C
c. Ca–N–C–C–N–Ca–
d. C–N–Ca–Ca–C–N
e. Ca–Ca–C–N–Ca–Ca–C

A

a. Ca–C–N–Ca–C–N

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21
Q

By adding SDS (sodium dodecyl sulfate) during the electrophoresis of proteins, it is possible to:

Select one:

a. preserve a protein’s native structure and biological activity
b. separate proteins exclusively on the basis of molecular weight.
c. determine a protein’s isoelectric point.
d. determine the amino acid composition of the protein.
e. determine an enzyme’s specific activity.

A

b. separate proteins exclusively on the basis of molecular weight.

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22
Q

Specific enzyme activity:
Select one:

a. is the enzyme activity (expressed as units'') of a specific protein. b. is the enzyme activity (enzyme asunits’’) in a milligram of protein.
c. is the enzyme activity (expressed as ``units’’) in a mol of protein.
d. refers to proteins other than enzymes.
e. refers only to purified proteins.

A

b. is the enzyme activity (enzyme as ``units’’) in a milligram of protein.

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23
Q

In the a helix the hydrogen bonds:
Select one:

a. occur only between some of the amino acids of the helix.
b. occur mainly between electronegative atoms of the R groups.
c. are perpendicular to the axis of the helix.
d. occur mainly between electronegative atoms of the backbone.
e. occur only near the amino and carboxyl termini of the helix.

A

d. occur mainly between electronegative atoms of the backbone.

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24
Q

Thr and/or Leu residues tend to disrupt an a-helix when they occur next to each other in a protein because:

Select one:
a. of the possible covalent interactions between the Thr and/or Leu side chains.

b. both amino acids are highly hydrophobic.
c. the R group of neither amino acid can form a hydrogen bond.
d. of electrostatic repulsion between the Thr and/or Leu side chains.
e. of steric hindrance between the bulky Thr and/or Leu side chains

A

e. of steric hindrance between the bulky Thr and/or Leu side chains

( This is when a large group in a molecule makes reactions not work)

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25
Q

Amino acid residues commonly found at the end of b turn are:

Select one:

a. Pro and Gly.
b. Ala and Gly.
c. two Cys.
d. hydrophobic.
e. those with ionized R groups.

A

a. Pro and Gly.

(Proline alpha-imino group cannot form H-bond => cause a break/kink
Glycine does not have beta carbon)

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26
Q

A sequence of amino acids in a certain protein is found to be -Ser-Gly-Pro- Gly-. The sequence is most probably part of:

Select one:

a. b turn.
b. parallel b sheet.
c. a helix.
d. a–sheet.

A

a. b turn.

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27
Q

The three-dimensional conformation of a protein may be strongly influenced by amino acid residues that are very far apart in sequence. This relationship is in contrast to secondary structure, where the amino acid residues are:

Select one:

a. restricted to only about seven of the twenty standard amino acids found in proteins
b. always side by side.
c. generally on different polypeptide strands.
d. generally near the polypeptide chain’s amino terminus or carboxyl terminus.
e. generally near each other in sequence.

A

e. generally near each other in sequence.

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28
Q

Which of the following statements is false?
Select one:

a. a-keratin is a protein in which the polypeptides are mainly in the a-helix conformation
b. Silk fibroin is a protein in which the polypeptide is almost entirely in the b conformation.
c. Collagen is a protein in which the polypeptides are mainly in the a-helix conformation
d. Gly residues are particularly abundant in collagen.
e. Mutations in collagen have been shown to be responsible for some human diseases

A

c. Collagen is a protein in which the polypeptides are mainly in the a-helix conformation

(single collagen polypeptides -> left handed helices
3 collagen polypeptide bundles -> right-handed helix)

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29
Q

To alter the shape of the a-keratin chains–as in hair waving– the a-keratin chains have undergone one chemical step resulting the conversion of disulfide bridges to Cysteine. What subsequent steps are required?

Select one:

a. chemical reduction and then chemical oxidation
b. chemical oxidation and then shape remodeling
c. shape remodeling and then chemical reduction
d. shape remodeling and then chemical oxidation
e. chemical reduction and then shape remodeling

A

d. shape remodeling and then chemical oxidation

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30
Q

When oxygen binds to a heme-containing protein, the two open coordination bonds of Fe2+ are occupied by:

Select one:

a. two O2 molecules.
b. two O atoms.
c. one O2 molecule and one heme atom.
d. one O2 molecule and one amino acid atom.
e. one O atom and one amino acid atom.

A

d. one O2 molecule and one amino acid atom.

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31
Q

In haemoglobin, the transition from T state to R state (low to high affinity) is triggered by:
Select one:
a. subunit dissociation. b. oxygen binding.
c. Fe2+ binding.
d. heme binding.
e. subunit association.

A

b. oxygen binding.

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32
Q

Which of the following is not correct concerning 2,3-bisphosphoglycerate (BPG)?
Select one:

a. It is normally found associated with the haemoglobin molecules that are
extracted from red blood cells.
b. It decreases the affinity of haemoglobin for oxygen.
c. It binds to the heme groups of haemoglobin.
d. It is an allosteric modulator.
e. It binds with lower affinity to foetal haemoglobin than to adult haemoglobin.

A

c. It binds to the heme groups of haemoglobin.

binds to the central compartment of the hemoglobin tetrame

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33
Q

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

Select one or more:

a. initial velocity of the catalyzed reaction at low [S].
b. initial velocity of the catalyzed reaction at [S]&raquo_space; KM.
c. KM for the substrate.
d. enzyme concentration.

A

b. initial velocity of the catalyzed reaction at [S]&raquo_space; KM.

d. enzyme concentration.

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34
Q

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:

Select one:

a. the enzyme is found in gastric secretions
b. a Lysine residue on the enzyme is involved in the reaction.
c. a Glutamate residue on the enzyme is involved in the reaction.
d. a Histidine residue on the enzyme is involved in the reaction.
e. the enzyme has a metallic cofactor.

A

d. a Histidine residue on the enzyme is involved in the reaction.

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35
Q

A good transition-state analog:

Select one:

a. binds to the enzyme more tightly than the substrate.
b. binds covalently to the enzyme.
c. is too unstable to isolate.
d. binds very weakly to the enzyme.
e. does not react with the native enzyme

A

a. binds to the enzyme more tightly than the substrate.

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36
Q

A transition-state analog:

Select one:

a. resembles the active site of general acid-base enzymes.
b. typically reacts more rapidly with an enzyme than the normal substrate.
c. is less stable when binding to an enzyme than the normal substrate.
d. stabilizes the transition state for the normal enzyme-substrate complex.
e. resembles the transition-state structure of the normal enzyme-substrate complex

A

e. resembles the transition-state structure of the normal enzyme-substrate complex

37
Q

Both water and glucose share an –OH that can serve as a substrate for a reaction with the terminal phosphate of ATP catalyzed by hexokinase. Glucose, however, is about a million times more reactive as a substrate than water. The best explanation is that:

Select one:

a. the larger glucose binds better to the enzyme; it induces a conformational change in hexokinase that brings active-site amino acids into position for catalysis.
b. glucose has more –OH groups per molecule than does water.
c. water normally will not reach the active site because it is hydrophobic. y
d. water and ATP compete for the active site resulting in a competitive inhibition of the enzyme.
e. the –OH group of water is attached to an inhibitory H atom while the glucose –OH group is attached to C.

A

a. the larger glucose binds better to the enzyme; it induces a conformational change in hexokinase that brings active-site amino acids into position for catalysis

38
Q

Which of the following statements about allosteric control of enzymatic activity is false?

Select one:
Ia. Allosteric proteins are generally composed of several subunits.
b. Heterotropic allosteric effectors compete with substrate for binding sites.
c. Binding of the effector changes the conformation of the enzyme molecule.
d. An effector may either inhibit or activate an enzyme.
e. Homotropic allosteric effectors do not have a separate binding site.

A

e. Homotropic allosteric effectors do not have a separate binding site.

39
Q

Which of the following statements are true for the enzyme at the rate-limiting step of a metabolic pathway?

a. Concentration of its substrate is higher than its Km value
b. The measured reaction rate is close to its Vmax
c. Its Vmax is higher than that of other enzymes in the pathway
d. Its Km value is higher than that of other enzymes in the pathway e. Its Km value is lower than that of other enzymes in the pathway

A

a. Concentration of its substrate is higher than its Km value
b. The measured reaction rate is close to its Vmax

40
Q

Which of the following statements is true for a reaction pathway under conditions of steady-state?

a. Concentrations of intermediers are unaltered
b. Vmax values of enzymes involved are equal
c. Reaction rate at the rate-limiting step is the lowest d. Concentrations of intermediers are equal
e. The system is in thermodynamic equilibrium

A

a. Concentrations of intermediers are unaltered

41
Q

Which conditions are necessary for two reactions to be enzymatically coupled? (Eact: activation energy)

a. Both reactions include phosphoryl transfer.
b. Eact of both reactions is high.
c. At least one of the reactions is oxidoreduction.
d. ΔG of the two reactions has different signs (one negative and one positive).
e. Eact of both reactions is low.

A

d. ΔG of the two reactions has different signs (one negative and one positive).

42
Q

Which conditions rule out the enzymatic coupling of two reactions? (Eact: activation energy)

a. One of the reactions has low Eact.
b. Eact of both reactions is high.
c. ΔG of both reactions is negative.
d. ΔG of the two reactions has different signs (one negative and one positive).
e. One of the reactions is oxidoreduction.

A

a. One of the reactions has low Eact.

c. ΔG of both reactions is negative.

43
Q

Which statement is true regarding the group transfer potential (gtp)?

Select one or more:

a. Gtp is the absolute value of the ΔG of hydrolysis (when the group is released).
b. Functional groups have a natural tendency to move from the lower toward the higher gtp.
c. Functional groups have a natural tendency to move from the higher toward the lower gtp.
d. ΔG of a group transfer equals the gtp of the group acceptor plus the gtp of the group donor.
e. ΔG of a group transfer equals the gtp of the group acceptor minus the gtp of the group donor.

A

a. Gtp is the absolute value of the ΔG of hydrolysis (when the group is released).
c. Functional groups have a natural tendency to move from the higher toward the lower gtp.
e. ΔG of a group transfer equals the gtp of the group acceptor minus the gtp of the group donor.

44
Q

Which statement is false regarding the group transfer potential (gtp)?

Select one or more:

a. The molecule of the lowest gtp is suitable as a group carrier.
b. Functional groups have a natural tendency to move from the lower toward the higher gtp.
c. ΔG of a group transfer equals the gtp of the group donor minus the gtp of the group acceptor.
d. Low gtp means that the group is attached to the molecule with a weak bond.
e. High gtp indicates a great tendency of the molecule to accept the group.

A

All are correct

45
Q

Which statement is false regarding oxidative decarboxylation of pyruvate in human cells?

Select one or more:

a. It is an irreversible reaction but it can be undone (i.e. pyruvate can be regenerated from the products) by other enzymes.
b. It is catalyzed by a large enzyme complex (E1, E2 and E3) in the cytosol.
c. The process can occur in anaerobic conditions because the complex does not use O2.
d. It belongs to substrate level phosphorylation because an ATP is produced.
e. The prosthetic group of E1 is biotin, which is reoxidized by E3 in each catalytic cycle.

A

All correct

for b, the enzyme complex is in mitochondria

46
Q

Which statement is false regarding oxidative decarboxylation of pyruvate in human cells?

Select one or more:

a. It is catalyzed by homodimers of pyruvate decarboxylase in the mitochondrial matrix.
b. The acetaldehyde intermediate is covalently bound to the enzyme as a hydroxyethyl group.
c. The product, acetate is bound to CoA in a macroergic thioester bond.
d. It is coupled to the mitochondrial electron transfer chain by NAD+ and NADH.
e. It is the last step of anaerobic glycolysis and it produces lactate

A

a. It is catalyzed by homodimers of pyruvate decarboxylase in the mitochondrial matrix. (=> catalyzed by pyruvate dehydrogenase to covert into acetyl-coA)
e. It is the last step of anaerobic glycolysis and it produces lactate

47
Q

Which statement is true?

Select one or more:

a. Oxidative phosphorylation is activated by ATP in starvation.
b. Oxidative catabolic processes in the mitochondrial matrix are coupled to respiration.
c. Citrate cycle is inhibited by high NADH/NAD+ ratio.
d. Pyruvate dehydrogenase is activated by low ATP/ADP ratio.
e. Malate/aspartate shuttle transports electrons from fatty acid oxidation to respiration.

A

b. Oxidative catabolic processes in the mitochondrial matrix are coupled to respiration.
c. Citrate cycle is inhibited by high NADH/NAD+ ratio.
d. Pyruvate dehydrogenase is activated by low ATP/ADP ratio.

48
Q

Which statement is false?

Select one or more:

a. Substrate level phosphorylation occurs both in glycolysis and in citrate cycle.
b. Uncouplers of oxidative phosphorylation cause inhibition of oxidative catabolism.
c. Pyruvate dehydrogenase and citrate cycle cannot function in anaerobic conditions.
d. ADP activates oxidative phosphorylation as a substrate of FoF1 ATPase.
e. FoF1 ATPase is an active transporter, which can pump protons into the matrix.

A

b. Uncouplers of oxidative phosphorylation cause inhibition of oxidative catabolism.
e. FoF1 ATPase is an active transporter, which can pump protons into the matrix.

49
Q

Which statement is false?

Select one or more:

a. Citrate cycle does not use O2, therefore it can function in anaerobic conditions.
b. Uncouplers of oxidative phosphorylation cause activation of oxidative catabolism.
c. Oxidative phosphorylation is uncoupled when the inner mitochondrial membrane is permeable for ions.
d. Respiration can be inhibited by KCN when oxidative phosphorylation is uncoupled.
e. Respiration can be inhibited by oligomycin when oxidative phosphorylation is uncoupled

A

a. Citrate cycle does not use O2, therefore it can function in anaerobic conditions.
e. Respiration can be inhibited by oligomycin when oxidative phosphorylation is uncoupled

(Oligomycin A is an inhibitor of ATP synthase)

50
Q

Which is prosthetic group in pyruvate-dehydrogenase complex?

Select one or more:

a. flavine mononucleotide (FMN),
b. CoA,
c. thiamine pyrophosphate (TPP),
d. heme,
e. flavine adenine dinucleotide (FAD).

A

c. thiamine pyrophosphate (TPP),

e. flavine adenine dinucleotide (FAD).

51
Q

Which cofactor is involved in the oxidative decarboxylation of pyruvate?

Select one or more:

a. CoA,
b. flavine mononucleotide (FMN),
c. CoQ,
d. NAD+,
e. biotine.

A

a. CoA,

d. NAD+,

52
Q

Which enzyme contains FAD prosthetic group?

Select one or more:

a. α-ketoglutarate dehydrogenase complex,
b. E3 of PDH complex,
c. mitochondrial glycerol 3-phosphate dehydrogenase,
d. succinate dehydrogenase,
e. malate dehydrogenase.

A

a. α-ketoglutarate dehydrogenase complex,
c. mitochondrial glycerol 3-phosphate dehydrogenase,
b. E3 of PDH complex,
d. succinate dehydrogenase,

53
Q

Which enzyme contains FAD prosthetic group? Select one or more:

a. Complex I of the respiratory chain,
b. α -ketoglutarate dehydrogenase,
c. malate dehydrogenase,
d. pyruvate dehydrogenase complex,
e. isocitrate dehydrogenase.

A

b. α -ketoglutarate dehydrogenase,

d. pyruvate dehydrogenase complex,

54
Q

Which enzyme uses NAD+/NADH?

Select one or more:

a. Complex I of the respiratory chain,
b. succinate dehydrogenase,
c. malate dehydrogenase,
d. acyl-CoA dehydrogenase,
e. glyceraldehyde 3-phosphate dehydrogenase.

A

a. Complex I of the respiratory chain,
c. malate dehydrogenase,
e. glyceraldehyde 3-phosphate dehydrogenase.

55
Q

Which enzyme consumes ATP in glycolysis?

Select one or more:

a. 3-Phosphoglycerate kinase,
b. phosphofructokinase,
c. hexokinase,
d. pyruvate kinase,
e. pyruvate dehydrogenase kinase.

A

b. phosphofructokinase,

c. hexokinase,

56
Q

Which compound is allosteric activator for phosphofructokinase 1 (PFK1)?

Select one or more:

a. AMP,
b. citrate,
c. fructose 2,6-bisphosphate,
d. glucagon,
e. acyl-CoA.

A

c. fructose 2,6-bisphosphate,

(Fructose 2,6-bisphosphate is synthesized from fruc- tose 6-phosphate and ATP by an enzyme called PFK 2 and it is hydrolyzed into fruc- tose 6-phosphate and P. by a specific fruc- tose 2,6-bisphosphatase also called FBPase 2.)

57
Q

Which compound is allosteric inhibitor for phosphofructokinase 1 (PFK1)?

Select one or more:

a. AMP,
b. citrate,
c. fructose 2,6-bisphosphate,
d. glucagon,
e. acyl-CoA.

A

b. citrate,

e. acyl-CoA.

58
Q

Which is the major role of lactate dehydrogenase (LDH) reaction in anaerobic glycolysis?

Select one:

a. production of ATP,
b. elimination of hydrogen, c. elimination of lactate,
d. regeneration of NAD+,
e. regeneration of pyruvate.

A

d. regeneration of NAD+,

59
Q

Which is not involved in oxidative decarboxylation of pyruvate by PDH complex?

Select one:

a. lipoamide,
b. biotin,
c. FAD,
d. CoA,
e. NAD+

A

b. biotin,

60
Q

Which is not involved in oxidative decarboxylation of pyruvate by PDH complex?

Select one:

a. thiamine pyrophosphate,
b. FAD,
c. NAD+,
d. ubiquinone,
e. CoA.

A

ubiquinone

61
Q

Chose the correct/right sentence regarding hepatic phosphofructokinase1 (PFK1).
Select one:
a. Insulin increases fructose 2,6-bisphosphate level and hence activates PFK1.
b. Insulin decreases fructose 2,6-bisphosphate level and hence activates PFK1.
c. Insulin causes phosphorylation and activation of PFK1.
d. Glucagon causes phosphorylation and activation of PFK1.
e. Glucagon decreases fructose 2,6-bisphosphate level and hence activates PFK1.

A

a. Insulin increases fructose 2,6-bisphosphate level and hence activates PFK1.

62
Q

Chose the wrong/false sentence regarding hepatic phosphofructokinase (PFK) enzymes.

Select one:

a. Insulin causes dephosphorylation of PFK2 and activation of PFK1.
b. PFK2 uses ATP for irreversible phosphorylation of fructose 6-phosphate.
c. PFK1 is allosterically activated by AMP.
d. PFK1 is allosterically inhibited by citrate.
e. PFK1 is allosterically inhibited by fructose 2,6-bisphosphate.

A

e. PFK1 is allosterically inhibited by fructose 2,6-bisphosphate.

(PFK2 produce F 2.6 BP, which in turn activates PFK1)

63
Q

Chose the correct/right sentence regarding hepatic glycolysis.

Select one:

a. Hepatic glycolysis is activated in starvation for ATP production.
b. Hepatic glycolysis is inhibited by glucagon at two irreversible steps.
c. Hepatic glycolysis results in lactate production.
d. Hepatic glycolysis is activated when fructose 2,6-bisphosphate level decreases.
e. Hepatic glycolysis is inhibited when AMP level increases.

A

b. Hepatic glycolysis is inhibited by glucagon at two irreversible steps.

(In addition to increasing gluconeogenesis, glucagon inhibits glycolysis. Phosphofructokinase-1 (PFK-1) phosphorylates the C-1 position of F-6-P, converting F-6-P into F(1,6)P2, an early and rate-limiting step in glycolysis.)

64
Q

Chose the wrong/false sentence regarding hepatic phosphofructokinase (PFK) enzymes.

Select one:

a. Hepatic glycolysis is aerobic and it is followed by conversion of pyruvate to acetyl-CoA.
b. PFK-1 becomes activated if PFK-2 is dephosphorylated.
c. Hepatic glycolysis is inhibited when citrate level increases.
d. Hepatic glycolysis is activated in starvation by fructose 2,6-bisphosphate. e. Hepatic glycolysis is activated when AMP level increases.

A

d. Hepatic glycolysis is activated in starvation by fructose 2,6-bisphosphate.

65
Q

Chose the correct/right sentence (PDH: pyruvate dehydrogenase complex).

Select one:

a. Pyruvate activates PDH kinase and hence inhibits PDH.
b. Insulin activates PDH kinase and hence activates PDH.
c. ADP inhibits PDH kinase and hence activates PDH.
d. Ca2+ activates PDH phosphatase and hence inhibits PDH.
e. NADH activates PDH phosphatase and hence activates PDH.

A

c. ADP inhibits PDH kinase and hence activates PDH.

66
Q

Which compound can deliver electrons to the respiratory chain directly?

Select one:

a. Fatty acyl-CoA
b. Fumarate
c. Succinyl-CoA
d. Pyruvate
e. Oxaloacetate

A

a. Fatty acyl-CoA

carnitine carrier system

67
Q
Which compound cannot deliver electrons to the respiratory chain directly?
Select one:
a. Glycerol 3-phosphate 
b. NADH
c. Acetyl-CoA
d. Fatty acyl-CoA
e. Succinate
A

c. Acetyl-CoA

68
Q

Which component of the oxidative phosphorylation is localized in the inter-membrane space?

Select one:

a. Cytochrome a3
b. Ubiquinone (CoQ)
c. Fo subunit of ATP synthase
d. Cytochrome c
e. F1 subunit of ATP synthase

A

d. Cytochrome c

69
Q

The branches in glycogen consist of glucose molecules linked by

Select one:

a. alpha-1,5 linkages
b. alpha-1,4 linkages
c. alpha-1,6 linkages
d. alpha-1,2 linkages

A

c. alpha-1,6 linkages

70
Q

The straight glucose chains of glycogen molecules are broken down initially to

Select one:

a. glucose
b. glucose- 6- phosphate
c. glucose-1- phosphate
d. fructose diphosphate
e. UDP-glucose

A

c. glucose-1- phosphate

71
Q

The branch points of glycogen are broken down to

Select one:

a. fructose diphosphate
b. glucose
c. glucose- 1- phosphate
d. glucose -6- phosphate
e. UDP-glucose

A

b. glucose

72
Q

The straight chains of glycogen molecules are broken down by

Select one:

a. adenylate cyclase
b. glycogen glicosidase
c. glycogen phosphorylase
d. glycogen-glycosidase
e. protein kinase

A

c. glycogen phosphorylase

73
Q

The binding of epinephrine to a receptor

Select one:

a. deactivates protein kinase A
b. deactivates adenylate cyclase
c. causes the breakdown of cyclic AMP to ATP
d. activates phosphodiesterase
e. activates adenylate cyclase

A

e. activates adenylate cyclase

74
Q

The binding of glucagon to its receptor
Select one:

a. deactivates protein kinase
b. deactivates adenylate cyclase
c. causes the breakdown of cyclic AMP to ATP
d. activates adenylate cyclase
e. activates phosphodiesterase

A

d. activates adenylate cyclase

75
Q

Which of the following statements are true?

Select one:

a. Fructose-1-phosphate activates glucokinase
b. Fructose-6-phosphate activates glucokinase
c. Glucokinase is inhibited by glucose-6-phosphate
d. Glucokinase is inhibited by high glucose level
e. Glucokinase is sequestered in the nucleus when glucose level is high.

A

a. Fructose-1-phosphate activates glucokinase

76
Q
Protein kinase A directly
Select one:
a. deactivates glucokinase
b. deactivates glycogen phosphorylase c. activates glycogen phosphorylase
d. deactivates phosphorylase kinase
e. activates phosphorylase kinase
A

e. activates phosphorylase kinase

77
Q

In glycogenesis, the enzyme (i)________ uses a molecule of
(ii)_________ to lengthen the glycogen chain

Select one:

a. (i) glycogen synthase (ii) glucose
b. (i)glycogen phosphorylase (ii) glucose
c. (i) glycogen phosphorylase (ii) UDP-glucose
d. (i) glycogen synthase (ii) UDP-glucose
e. (i) glycogenin (ii) glucose-1-phosphate

A

c. (i) glycogen phosphorylase (ii) UDP-glucose

78
Q

Patients suffering from Von Gierke’s disease
Select one:
a. cannot convert glucose-6-phosphate to glucose b. have enlarged livers
c. cannot convert glycogen to glucose
d. have high plasma levels of lactate
e. all of them are correct

A

e. all of them are correct

79
Q

A person is suffering from a disease which is caused by a defective glucose-6-phosphatase. Such a person
Select one:
a. cannot breakdown glycogen completely to glucose
b. can convert pyruvate to glucose
c. can dephosphorylate glucose-6-phosphate
d. can convert glycogen to pyruvate
e. can convert acetyl-CoA to glucose

A

a. cannot breakdown glycogen completely to glucose

80
Q

In glycogenolysis, the enzyme (i)________ breaks an (ii) _______ bond to release a molecule of (iii)_________.

Select one:

a. (i) glycogen synthase (ii) alpha 1-4 (iii) glucose
b. (i) glycogen synthase (ii) alpha 1-4 (iii) UDP-glucose
c. (i) glycogen phosphorylase (ii) alpha 1-4 (iii) glucose-1-phosphate
d. (i) glycogen phosphorylase (ii) alpha 1-6 (iii) glucose-6-phosphate
e. (i) debranching enzyme (ii) alpha 1-6 (iii) glucose-1-phosphate

A

(i) glycogen phosphorylase
(ii) alpha 1-4
(iii) glucose-1-phosphate

81
Q

In glycogenolysis, the enzyme (i)________ breaks an (ii) _______ bond to release a molecule of (iii)_________.
Select one:

a. (i) glycogen synthase (ii) alpha 1-4 (iii) glucose
b. (i) glycogen synthase (ii) alpha 1-4 (iii) UDP-glucose
c. (i) glycogen phosphorylase (ii) alpha 1-4 (iii) glucose-1-phosphate
d. (i) glycogen phosphorylase (ii) alpha 1-6 (iii) glucose-6-phosphate
e. (i) debranching enzyme (ii) alpha 1-6 (iii) glucose-1-phosphate

A

(i) glycogen phosphorylase
(ii) alpha 1-4
(iii) glucose-1-phosphate

82
Q

What is true concerning glucose-6-phosphatase enzyme system?

Select one or more:

a. responsible for dephosphorylation of glucose-6-phosphate
b. expressed in the endoplasmic reticulum of hepatocytes
c. an enzyme system in gluconeogenic pathway
d. is involved in pentose-phosphate pathway

A

a. responsible for dephosphorylation of glucose-6-phosphate
b. expressed in the endoplasmic reticulum of hepatocytes
c. an enzyme system in gluconeogenic pathway

83
Q

Activity of phosphofructokinase1 is inhibited by

Select one or more:

a. ATP
b. citrate
c. fructose 2,6 bisphosphate
d. AMP

A

a. ATP

b. citrate

84
Q

Which are the ATP producing steps of glycolysis?
Select one or more:
a. phosphofructokinase 1
b. lactate-dehydrogenase
c. pyruvate kinase
d. glyceraldehyde 3-phosphate dehydrogenase
e. phosphoglycerate kinase

A

pyruvate kinase, phosphoglycerate kinase

85
Q
Which are the ATP consuming steps of glycolysis?
Select one or more:
a. phosphofructokinase 1 
b. lactate dehydrogenase 
c. pyruvate kinase
d. hexokinase
e. phosphoglycerate kinase
A

phosphofructokinase 1, hexokinase

86
Q

Upon phosphorylation of phosphofructokinase 2 by protein kinase A in liver:

Select one:

a. it becomes active.
b. it becomes inactive.
c. phosphatase function is activated, kinase function is inactivated.
d. kinase function is activated, phosphatase function is inactivated.
e. phosphofructokinase 2 is not covalently regulated.

A

c. phosphatase function is activated, kinase function is inactivated.

87
Q

Which enzyme deficiency may result in lactic acidosis?

Select one or more:

a. Pyruvate kinase
b. Pyruvate dehydrogenase
c. Pyruvate carboxylase
d. Lactate dehydrogenase

A

b. Pyruvate dehydrogenase
c. Pyruvate carboxylase

(=> accumulation of pyruvate)

88
Q

Which condition is not found in pyrvate carboxylase deficiency?

Select one:

a. Demyelination
b. Hyperammonemia
c. Hyperglycemia
d. Hypoglycemia
e. Lactic acidosis

A

c. Hyperglycemia

high. blood sugar