ENZYMES Answer

Quiz Results
Your Score: 94 %
You answered 17 of 18 questions correctly.
Question 1: Correct
Select the one of the following statements that is NOT CORRECT.
A
Enzymes lower the activation energy for a reaction.
B
Enzymes often lower the activation energy by destabilizing transition state intermediates.
C
Active site histidyl residues frequently aid catalysis by acting as proton donors or acceptors.
D
Covalent catalysis is employed by some enzymes to provide an alternative reaction pathway.
E
The presence of an enzyme has no effect on ΔG°.
The correct answer is B. You answered B.
57% of users answered correctly.

Source: Harper's Illustrated Biochemistry, 31e
Question 2: Correct
Which of the following is NOT a potential function of the physiologically essential transition
metals?
A
Binding diatomic gas molecules
B
Proton carrier
C
Stabilizing protein conformation
D
Enhancing the nucleophilicity of water
E
Electron carrier

Question 3: Incorrect
A
For a given enzyme, the intracellular concentrations of its substrates tend to be close to
their Km values.
B
The sequestration of certain pathways within intracellular organelles facilitates the task of
metabolic regulation.
C
The earliest step in a biochemical pathway where regulatory control can be efficiently exerted
is the first committed step.
D
Feedback regulation refers to the allosteric control of an early step in a biochemical pathway
by the end product(s) of that pathway.
E
Metabolic control is most effective when one of the more rapid steps in a pathway is targeted
for regulation.
The correct answer is E. You answered D.

Question 4: Correct
Acute heavy metal poisoning can be treated by:
A
Administration of diuretics
B
Ingestion of chelating agents
C
Hemodialysis
D
All of the above
E
None of the above
The correct answer is D. You answered D.

Question 5: Correct
A
Acid–base catalysis is a prominent feature of the catalytic mechanism of the HIV protease.
B
Fischer’s lock-and-key model explains the role of transition state stabilization in enzymic
catalysis.
C
Hydrolysis of peptide bonds by serine proteases involves the transient formation of a
modified enzyme.
D
Many enzymes employ metal ions as prosthetic groups or cofactors.
E
In general, enzymes bind transition state analogs more tightly than substrate analogs.

Question 6: Correct
A
As used in biochemistry, the standard state concentration for products and reactants other
than protons is 1 molar.
B
ΔG is a function of the logarithm of Keq.
C
As used in reaction kinetics, the term “spontaneity” refers to whether the reaction as written
is favored to proceed from left to right.
D
ΔG° denotes the change in free energy that accompanies transition from the standard state to
equilibrium.
E
Upon reaching equilibrium, the rates of the forward and reverse reaction both drop to zero.
The correct answer is E. You answered E.

Question 7: Correct
A
Steric hindrance by histidine E7 plays a critical role in weakening the affinity of hemoglobin
for carbon monoxide (CO).
B
Carbonic anhydrase plays a critical role in respiration by virtue of its capacity to break down
2,3-bisphosphoglycerate in the lungs.
C
Hemoglobin S is distinguished by a genetic mutation that substitutes Glu6 on the β subunit
with Val, creating a sticky patch on its surface.
D
Oxidation of the heme iron from the +2 to the +3 state abolishes the ability of hemoglobin to
bind oxygen.
E
The functional differences between hemoglobin and myoglobin reflect, to a large degree,
differences in their quaternary structure.

Question 8: Correct
A
To calculate Keq, the equilibrium constant for a reaction, divide the initial rate of the forward
reaction (rate 1) by the initial velocity of the reverse reaction (rate 1).
B
The presence of an enzyme has no effect on Keq.
C
For a reaction conducted at constant temperature, the fraction of the potential reactant
molecules possessing sufficient kinetic energy to exceed the activation energy of the reaction
is a constant.
D
Enzymes and other catalysts lower the activation energy of reactions.
E
The algebraic sign of ΔG, the Gibbs free energy change for a reaction, indicates the direction
in which a reaction will proceed.
The correct answer is A. You answered A.

Question 9: Correct
A
The charge-relay network of trypsin makes the active site serine a stronger nucleophile.
B
The Michaelis constant is the substrate concentration at which the rate of the reaction is half-
maximal.
C
During transamination reactions, both substrates are bound to the enzyme before either
product is released.
D
Histidine residues act both as acids and as bases during catalysis by an aspartate protease.
E
Many coenzymes and cofactors are derived from vitamins.
The correct answer is C. You answered C.

Question 10: Correct
A
The Bohr effect refers to the release of protons that occurs when oxygen binds to
deoxyhemoglobin.
B
Shortly after birth of a human infant, synthesis of the α-chain undergoes rapid induction until
it comprises 50% of the hemoglobin tetramer.
C
The β-chain of fetal hemoglobin is present throughout gestation.
D
The term thalassemia refers to any genetic defect that results in partial or total absence of the
α- or β-chains of hemoglobin.
E
The taut conformation of hemoglobin is stabilized by several salt bridges that form between
the subunits.

A
For most enzymes, the initial reaction velocity, vi, exhibits a hyperbolic dependence on [S].
B
When [S] is much lower than Km, the term Km + [S] in the Michaelis-Menten equation closely
approaches Km. Under these conditions, the rate of catalysis is a linear function of [S].
C
The molar concentrations of substrates and products are equal when the rate of an enzyme-
catalyzed reaction reaches half of its potential maximum value (Vmax/2).
D
An enzyme is said to have become saturated with substrate when successively raising [S] fails
to produce a significant increase in vi.
E
When making steady-state rate measurements, the concentration of substrates should
greatly exceed that of the enzyme catalyst.
The correct answer is C. You answered C.

A
Interconvertible enzymes fulfill key roles in integrated regulatory networks.
B
Phosphorylation of an enzyme often alters its catalytic efficiency.
C
“Second messengers” act as intracellular extensions or surrogates for hormones and nerve
impulses impinging on cell surface receptors.
D
The ability of protein kinases to catalyze the reverse reaction that removes the phosphoryl
group is key to the versatility of this molecular regulatory mechanism.
E
Zymogen activation by partial proteolysis is irreversible under physiologic conditions.

Which of the following is NOT a benefit obtained by incorporating physiologically essential
transition metal ions into organometallic complexes?
A
Optimization of Lewis acid potency of the bound metal.
B
Ability to construct complexes containing multiple transition metal ions.
C
Attenuation of the production of reactive oxygen species.
D
Protection against unwanted oxidation.
E
To render the bound transition metal multivalent.

A
Certain monomeric enzymes exhibit sigmoidal initial rate kinetics.
B
The Hill equation is used to perform quantitative analysis of the cooperative behavior of
enzymes or carrier proteins such as hemoglobin or calmodulin.
C
For an enzyme that exhibits cooperative binding of substrate, a value of n (the Hill coefficient)
greater than unity is said to exhibit positive cooperativity.
D
An enzyme that catalyzes a reaction between two or more substrates is said to operate by a
sequential mechanism if the substrates must bind in a fixed order.
E
Prosthetic groups enable enzymes to add chemical groups beyond those present on amino
acid side chains.

A protein engineer desires to alter the active site of chymotrypsin so that it will cleave peptide
bonds to the C-terminal side of aspartyl and glutamyl residues. The protein engineer will be
most likely to succeed if he replaces the hydrophobic amino acid at the bottom of the active
site pocket with:
A
Phenylalanine
B
Threonine
C
Glutamine
D
Lysine
E
Proline

A
IC50 is a simple operational term for expressing the potency of an inhibitor.
B
Lineweaver-Burk and Dixon plots employ rearranged versions of the Michaelis-Menten
equation to generate linear representations of kinetic behavior and inhibition.
C
A plot of 1/vi versus 1/[S] can be used to evaluate the type and affinity for an inhibitor.
D
Simple noncompetitive inhibitors lower the apparent Km for a substrate.
E
Noncompetitive inhibitors typically bear little or no structural resemblance to the
substrate(s) of an enzyme-catalyzed reaction.

A
Many mitochondrial proteins are covalently modified by the acetylation of the epsilon amino
groups of lysine residues.
B
Protein acetylation is an example of a covalent modification that can be “reversed” under
physiologic conditions.
C
Increased levels of acetyl-CoA tend to favor protein acetylation.
D
Acetylation increases the steric bulk of the amino acid side chains that are subject to this
modification.
E
The side chain of an acetylated lysyl residue is a stronger base than that of an unmodified
lysyl residue.
The correct answer is E. You answered E.

Which of the following is the name of a common organometallic DNA-binding motif?
A
Zinc finger
B
Molybdopterin
C
Fe-S center
D
All of the above
E
None of the above

ENZYMES Answer

Uploaded by

Copyright:

Available Formats

ENZYMES Answer

Uploaded by

Document Information

Copyright

Available Formats

Share this document

Share or Embed Document

Sharing Options

Did you find this document useful?

Is this content inappropriate?

Copyright:

Available Formats

ENZYMES Answer

Uploaded by

Copyright:

Available Formats

Quiz Results

The correct answer is B. You answered B.

57% of users answered correctly.

The correct answer is B. You answered B.

43% of users answered correctly.

The correct answer is E. You answered D.

48% of users answered correctly.

The correct answer is D. You answered D.

63% of users answered correctly.

The correct answer is B. You answered B.

50% of users answered correctly.

The correct answer is E. You answered E.

56% of users answered correctly.

The correct answer is B. You answered B.

44% of users answered correctly.

The correct answer is A. You answered A.

46% of users answered correctly.

The correct answer is C. You answered C.

45% of users answered correctly.

The correct answer is B. You answered B.

35% of users answered correctly.

The correct answer is C. You answered C.

52% of users answered correctly.

The correct answer is D. You answered D.

51% of users answered correctly.

The correct answer is A. You answered A.

37% of users answered correctly.

The correct answer is A. You answered A.

The correct answer is D. You answered D.

52% of users answered correctly.

The correct answer is D. You answered D.

61% of users answered correctly.

The correct answer is E. You answered E.

52% of users answered correctly.

The correct answer is A. You answered A.

58% of users answered correctly.

You might also like