Soal-Soal Enzymes (English)

Enzymes
An introduction to enzymes
Pages: 183184 Difficulty: 1 Ans: A
1. One of the enzymes involved in glycolysis, aldolase, requires Zn2+ for
catalysis. Under conditions of zinc deficiency, when the enzyme may lack
zinc, it would be referred to as the:
A) apoenzyme.
B) coenzyme.
C) holoenzyme.
D) prosthetic group.
E) substrate.
Page: 185 Difficulty: 1 Ans: D
2. Which one of the following is not among the six internationally accepted
classes of enzymes?
A) Hydrolases
B) Ligases
C) Oxidoreductases
D) Polymerases
E) Transferases
How enzymes work

Pages: 186187 Difficulty: 2 Ans: E
3. Enzymes are potent catalysts because they:
A) are consumed in the reactions they catalyze.

B) are very specific and can prevent the conversion of products back to substrates.
C) drive reactions to completion while other catalysts drive reactions to equilibrium.
D) increase the equilibrium constants for the reactions they catalyze.
E) lower the activation energy for the reactions they catalyze.
How enzymes work

Pages: 186187 Difficulty: 1 Ans: D
4. The role of an enzyme in an enzyme-catalyzed reaction is to:
A) bind a transition state intermediate, such that it cannot be converted back to

substrate.
B) ensure that all of the substrate is converted to product.
C) ensure that the product is more stable than the substrate.
D) increase the rate at which substrate is converted into product.
E) make the free-energy change for the reaction more favorable.
How enzymes work
Pages: 186188 Difficulty: 2 Ans:D
5. Which one of the following statements is true of enzyme catalysts?
A) Their catalytic activity is independent of pH.

B) They are generally equally active on D and L isomers of a given substrate.
C) They can increase the equilibrium constant for a given reaction by a thousand fold
or more.
D) They can increase the reaction rate for a given reaction by a thousand-fold or
more.
E) To be effective, they must be present at the same concentration as their
substrate.
How enzymes work

6. Which one of the following statements is true of enzyme catalysts?
A) They bind to substrates but are never covalently attached to substrate or product.
B) They increase the equilibrium constant for a reaction, thus favoring product
formation.
C) They increase the stability of the product of a desired reaction by allowing
ionizations, resonance, and isomerizations not normally available to substrates.
D) They lower the activation energy for the conversion of substrate to product.
E) To be effective, they must be present at the same concentration as their
substrates.
How enzymes work

Pages: 186188 Difficulty: 1 Ans: C
7. Which of the following statements is false?
A) A reaction may not occur at a detectable rate even though it has a favorable
equilibrium.
B) After a reaction, the enzyme involved becomes available to catalyze the reaction
again.
C) For S  P, a catalyst shifts the reaction equilibrium to the right.
D) Lowering the temperature of a reaction will lower the reaction rate.
E) Substrate binds to an enzyme's active site.
How enzymes work

Pages: 189190 Difficulty: 1 Ans: B
8. Enzymes differ from other catalysts in that only enzymes:
A) are not consumed in the reaction.

B) display specificity toward a single reactant.
C) fail to influence the equilibrium point of the reaction.
D) form an activated complex with the reactants.
E) lower the activation energy of the reaction catalyzed.
How enzymes work

Page: 190 Difficulty: 2 Ans: A
9. Compare the two reaction coordinate diagrams below and select the answer
that correctly describes their relationship. In each case, the single
intermediate is the ES complex.
A) (a) describes a strict “lock and key” model, whereas (b) describes a transition-
state complementarity model.
B) The activation energy for the catalyzed reaction is 5 in (a) and is 7 in (b).
C) The activation energy for the uncatalyzed reaction is given by 5 + 6 in (a) and by
7 + 4 in (b).
D) The contribution of binding energy is given by 5 in (a) and by 7 in (b).
E) The ES complex is given by 2 in (a) and 3 in (b).
How enzymes work

10. Which of the following is true of the binding energy derived from enzyme-
substrate interactions?
A) It cannot provide enough energy to explain the large rate accelerations brought
about by enzymes.
B) It is sometimes used to hold two substrates in the optimal orientation for reaction.
C) It is the result of covalent bonds formed between enzyme and substrate.
D) Most of it is derived from covalent bonds between enzyme and substrate.
E) Most of it is used up simply binding the substrate to the enzyme.
Enzyme kinetics as an approach to understanding mechanism

11. The concept of “induced fit” refers to the fact that:
A) enzyme specificity is induced by enzyme-substrate binding.
B) enzyme-substrate binding induces an increase in the reaction entropy, thereby
catalyzing the reaction.
C) enzyme-substrate binding induces movement along the reaction coordinate to the
transition state.
D) substrate binding may induce a conformational change in the enzyme, which then
brings catalytic groups into proper orientation.
E) when a substrate binds to an enzyme, the enzyme induces a loss of water
(desolvation) from the substrate.

12. In the following diagram of the first step in the reaction catalyzed by the
protease chymotrypsin, the process of general base catalysis is illustrated by
the number ________, and the process of covalent catalysis is illustrated by
the number _________.
A) 1; 2
B) 1; 3
C) 2; 3
D) 2; 3
E) 3; 2

Page: 194 Difficulty: 1 Ans: B
13. The benefit of measuring the initial rate of a reaction V0 is that at the
beginning of a reaction:
A) [ES] can be measured accurately.

B) changes in [S] are negligible, so [S] can be treated as a constant.
C) changes in Km are negligible, so Km can be treated as a constant.
D) V0 = Vmax.
E) varying [S] has no effect on V0.

14. Which of the following statements about a plot of V0 vs. [S] for an enzyme
that follows Michaelis-Menten kinetics is false?
A) As [S] increases, the initial velocity of reaction V0 also increases.

B) At very high [S], the velocity curve becomes a horizontal line that intersects the y-
axis at Km.
C) Km is the [S] at which V0 = 1/2 Vmax.
D) The shape of the curve is a hyperbola.
E) The y-axis is a rate term with units of m/min.

15. Michaelis and Menten assumed that the overall reaction for an enzyme-
catalyzed reaction could be written as
Using this reaction, the rate of breakdown of the enzyme-substrate complex can be
described by the expression:
A) k1 ([Et] - [ES]).
B) k1 ([Et] - [ES])[S].
C) k2 [ES].
D) k-1 [ES] + k2 [ES].
E) k-1 [ES].

Page: 196 Difficulty: 2 Ans: C
16. The steady state assumption, as applied to enzyme kinetics, implies:
A) Km = Ks.
B) the enzyme is regulated.
C) the ES complex is formed and broken down at equivalent rates.
D) the Km is equivalent to the cellular substrate concentration.
E) the maximum velocity occurs when the enzyme is saturated.

17. An enzyme-catalyzed reaction was carried out with the substrate
concentration initially a thousand times greater than the K m for that substrate.
After 9 minutes, 1% of the substrate had been converted to product, and the
amount of product formed in the reaction mixture was 12 µmol. If, in a
separate experiment, one-third as much enzyme and twice as much substrate
had been combined, how long would it take for the same amount (12 µmol) of
product to be formed?
A) 1.5 min
B) 13.5 min
C) 27 min
D) 3 min
E) 6 min

18. Which of these statements about enzyme-catalyzed reactions is false?
A) At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is

proportional to the enzyme concentration.
B) If enough substrate is added, the normal V max of a reaction can be attained even
in the presence of a competitive inhibitor.
C) The rate of a reaction decreases steadily with time as substrate is depleted.
D) The activation energy for the catalyzed reaction is the same as for the
uncatalyzed reaction, but the equilibrium constant is more favorable in the enzyme-
catalyzed reaction.
E) The Michaelis-Menten constant Km equals the [S] at which V = 1/2 Vmax.

19. The following data were obtained in a study of an enzyme known to follow
Michaelis-Menten kinetics:
The Km for this enzyme is approximately:

A) 1 mM.
B) 1000 mM.
C) 2 mM.
D) 4 mM.
E) 6 mM.

Page: 196197 Difficulty: 2 Ans: C
20. For enzymes in which the slowest (rate-limiting) step is the reaction
k2
ES  P
Km becomes equivalent to:

A) kcat.
B) the [S], where V0 = Vmax.
C) the dissociation constant, Kd, for the ES complex.
D) the maximal velocity.
E) the turnover number.

Page: 201-202 Difficulty: 3 Ans: D
21. For the simplifed representation of an enzyme-catalyzed reaction shown
below, the statement “ES is in steady-state” means that
A) k2 is very slow.
B) k1= k2.
C) k1= k-1.
D) k1[E][S] = k-1[ES] + k2[ES].
E) k1[E][S] = k-1[ES].

22. The Lineweaver-Burk plot is used to:
A) determine the equilibrium constant for an enzymatic reaction.

B) extrapolate for the value of reaction rate at infinite enzyme concentration.
C) illustrate the effect of temperature on an enzymatic reaction.
D) solve, graphically, for the rate of an enzymatic reaction at infinite substrate
concentration.
E) solve, graphically, for the ratio of products to reactants for any starting substrate
concentration.

Page: 197 Difficulty: 3 Ans: A
23. The double-reciprocal transformation of the Michaelis-Menten equation, also
called the Lineweaver-Burk plot, is given by
1/V0 = Km /(Vmax[S]) + 1/Vmax

To determine Km from a double-reciprocal plot, you would:
A) multiply the reciprocal of the x-axis intercept by -1.

B) multiply the reciprocal of the y-axis intercept by -1.
C) take the reciprocal of the x-axis intercept.
D) take the reciprocal of the y-axis intercept.
E) take the x-axis intercept, where V0 = 1/2 Vmax.

Page: 198 Difficulty: 2 Ans: E
24. To calculate the turnover number of an enzyme, you need to know:
A) the enzyme concentration.

B) the initial velocity of the catalyzed reaction at [S] >> K m.
C) the initial velocity of the catalyzed reaction at low [S].
D) the Km for the substrate.
E) both A and B.

Page: 198 Difficulty: 1 Ans: E
25. The number of substrate molecules converted to product in a given unit of
time by a single enzyme molecule at saturation is referred to as the:
A) dissociation constant.
B) half-saturation constant.
C) maximum velocity.
D) Michaelis-Menten number.
E) turnover number.

26. In a plot of l/V against 1/[S] for an enzyme-catalyzed reaction, the presence of
a competitive inhibitor will alter the:
A) curvature of the plot.

B) intercept on the l/[S] axis.
C) intercept on the l/V axis.
D) pK of the plot.
E) Vmax.

27. In competitive inhibition, an inhibitor:
A) binds at several different sites on an enzyme.

B) binds covalently to the enzyme.
C) binds only to the ES complex.
D) binds reversibly at the active site.
E) lowers the characteristic Vmax of the enzyme.
28. Vmax for an enzyme-catalyzed reaction:
A) generally increases when pH increases.

B) increases in the presence of a competitive inhibitor.
C) is limited only by the amount of substrate supplied.
D) is twice the rate observed when the concentration of substrate is equal to the K m.
E) is unchanged in the presence of a uncompetitive inhibitor.

29. 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:
A) a Glu residue on the enzyme is involved in the reaction.

B) a His residue on the enzyme is involved in the reaction.
C) the enzyme has a metallic cofactor.
D) the enzyme is found in gastric secretions.
E) the reaction relies on specific acid-base catalysis.
Examples of enzymatic reactions

30. Phenyl-methane-sulfonyl-fluoride (PMSF) inactivates serine proteases by
binding covalently to the catalytic serine residue at the active site; this
enzyme-inhibitor bond is not cleaved by the enzyme. This is an example of
what kind of inhibition?
A) Irreversible
B) Competitive
C) Non-competitive
D) Mixed
E) pH inhibition

31. 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:
A) glucose has more —OH groups per molecule than does water.
B) 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.
C) the —OH group of water is attached to an inhibitory H atom, while the glucose —
OH group is attached to C.
D) water and the second substrate, ATP, compete for the active site resulting in a
competitive inhibition of the enzyme.
E) water normally will not reach the active site because it is hydrophobic.

Pages: 210-211 Difficulty: 2 Ans: B
32. A good transition-state analog:
A) binds covalently to the enzyme.

B) binds to the enzyme more tightly than the substrate.
C) binds very weakly to the enzyme.
D) is too unstable to isolate.
E) must be almost identical to the substrate.

33. A transition-state analog:
A) is less stable when binding to an enzyme than the normal substrate.

B) resembles the active site of general acid-base enzymes.
C) resembles the transition-state structure of the normal enzyme-substrate complex.
D) stabilizes the transition state for the normal enzyme-substrate complex.
E) typically reacts more rapidly with an enzyme than the normal substrate.

34. The role of the metal ion (Mg2+) in catalysis by enolase is to:
A) act as a general acid catalyst.

B) act as a general base catalyst.
C) facilitate general acid catalysis.
D) facilitate general base catalysis.
E) stabilize protein conformation.

Page: 216217 Difficulty: 2 Ans: C
35. Penicillin and related drugs inhibit the enzyme_______; this enzyme is
produced by_______
A) ß-lacamase; bacteria
B) transpeptidase; human cells
C) transpeptidase; bacteria
D) lysozyme; human cells
E) aldolase; bacteria
Regulatory enzymes
Pages: 220221 Difficulty: 2 Ans: E
36. Which of the following statements about allosteric control of enzymatic activity
is false?
A) Allosteric effectors give rise to sigmoidal V0 vs. [S] kinetic plots.

B) Allosteric proteins are generally composed of several subunits.
C) An effector may either inhibit or activate an enzyme.
D) Binding of the effector changes the conformation of the enzyme molecule.
E) Heterotropic allosteric effectors compete with substrate for binding sites.
Regulatory enzymes
37. A small molecule that decreases the activity of an enzyme by binding to a site
other than the catalytic site is termed a(n):
A) allosteric inhibitor.
B) alternative inhibitor.
C) competitive inhibitor.
D) stereospecific agent.
E) transition-state analog.
Regulatory enzymes
38. Allosteric enzymes:
A) are regulated primarily by covalent modification.

B) usually catalyze several different reactions within a metabolic pathway.
C) usually have more than one polypeptide chain.
D) usually have only one active site.
E) usually show strict Michaelis-Menten kinetics.
Regulatory enzymes
Pages: 223-226 Difficulty: 3 Ans: A
39. Which of the following has not been shown to play a role in determining the
specificity of protein kinases?
A) Disulfide bonds near the phosphorylation site

B) Primary sequence at phosphorylation site
C) Protein quaternary structure
D) Protein tertiary structure
E) Residues near the phosphorylation site
Regulatory enzymes
40. How is trypsinogen converted to trypsin?
A) A protein kinase-catalyzed phosphorylation converts trypsinogen to trypsin.

B) An increase in Ca2+ concentration promotes the conversion.
C) Proteolysis of trypsinogen forms trypsin.
D) Trypsinogen dimers bind an allosteric modulator, cAMP, causing dissociation into
active trypsin monomers.
E) Two inactive trypsinogen dimers pair to form an active trypsin tetramer.
Regulatory enzymesPage: 227 Difficulty: 1 Ans: B

41. The allosteric enzyme ATCase is regulated by CTP, which binds to the T-
state of ATCase. CTP is a:
A) positive regulator.
B) negative regulator.
C) co-factor.
D) competitive inhibitor.
E) coenzyme.
Regulatory enzymes
Page: 232234 Difficulty: 2 Ans: E
42. Blood coagulation involves:
A) a kinase cascade.
B) zymogen activation.
C) serine proteases.
D) A and B.
E) B and C.
Short Answer Questions
Page: 184 Difficulty: 1
43. Define the terms “cofactor” and “coenzyme.”
Ans: A cofactor is any chemical component required for enzyme activity; it includes
both organic molecules, called “coenzymes,” and inorganic ions.
How enzymes workPage: 187 Difficulty: 2

44. Draw and label a reaction coordinate diagram for an uncatalyzed reaction, S
 P, and the same reaction catalyzed by an enzyme, E.
Ans: See Fig. 6-3, p. 187.
How enzymes work

45. The difference in (standard) free energy content, ΔG'°, between substrate S
and product P may vary considerably among different reactions. What is the
significance of these differences?
Ans: The difference in free energy content between substrate (or reactant) and
product for each reaction reflects the relative amounts of each compound present at
equilibrium. The greater the difference in free energy, the greater the difference in
amounts of each compound at equilibrium.
How enzymes work

46. For a reaction that can take place with or without catalysis by an enzyme,
what would be the effect of the enzyme on the:
(a) standard free energy change of the reaction?
(b) activation energy of the reaction?
(c) initial velocity of the reaction?
(d) equilibrium constant of the reaction?
Ans: (a) no change; (b) decrease; (c) increase; (d) no change.
How enzymes work

Pages: 187188 Difficulty: 2
47. Sometimes the difference in (standard) free-energy content, ΔG'°, between a
substrate S and a product P is very large, yet the rate of chemical conversion,
S  P, is quite slow. Why?
Ans: The rate of conversion from substrate to product (or the reverse reaction, from
product to substrate) does not depend on the free-energy difference between them.
The rate of the reaction depends on the activation energy of the reaction ΔG'‡, which
is the difference between the free-energy content of S (or P) and the reaction
transition state.
How enzymes work

48. Write an equilibrium expression for the reaction S  P and briefly explain the
relationship between the value of the equilibrium constant and free energy.
Ans: Keq' = [P]/[S]. The value of Keq' reflects the difference between the free energy
content of S and P. Free energy and equilibrium constant are related by the
expression:
ΔG'° = -RT ln Keq'
For each change in Keq' by one order of magnitude, ΔG'° changes by 5.7
Kjoule/mole.
49. What is the difference between general acid-base catalysis and specific acid-
base catalysis? (Assume that the solvent is water.)
Ans: Specific acid-base catalysis refers to catalysis by the constituents of water; that
is, the donation of aproton by the hydronium ion, H3O+ or the acceptance of a
proton by the hydroxyl ion OH-. General acid-base catalysis refers to the donation or
acceptance of a proton by weak acids and bases other than water.

50. Michaelis-Menten kinetics is sometimes referred to as “saturation” kinetics.
Why?
Ans: According to the Michaelis-Menten model of enzyme-substrate interaction,

when [S] becomes very high, an enzyme molecule's active site will become occupied
with a new substrate molecule as soon as it releases a product. Therefore, at very
high [S], V0 does not increase with additional substrate, and the enzyme is said to
be “saturated” with substrate.

51. Two different enzymes are able to catalyze the same reaction, A  B. They
both have the same Vmax, but differ their Km the substrate A. For enzyme 1,
the Km is 1.0 mM; for enzyme 2, the K m is 10 mM. When enzyme 1 was
incubated with 0.1 mM A, it was observed that B was produced at a rate of
0.0020 mmoles/minute. a) What is the value of the Vmax of the enzymes? b)
What will be the rate of production of B when enzyme 2 is incubated with 0.1
mM A? c) What will be the rate of production of B when enzyme 1 is
incubated with 1 M (i.e., 1000 mM) A?
Ans: a) 0.022 mmol/min; b) 0.0022 mmol/min; c) 0.022 mmol/min.

52. An enzyme can catalyze a reaction with either of two substrates, S 1 or S2.
The Km for S1 was found to be 2.0 mM, and the K m, for S2 was found to be 20
mM. A student determined that the V max was the same for the two substrates.
Unfortunately, he lost the page of his notebook and needed to know the value
of Vmax. He carried out two reactions: one with 0.1 mM S 1, the other with 0.1
mM S2. Unfortunately, he forgot to label which reaction tube contained which
substrate. Determine the value of Vmax from the results he obtained:
Tube number Rate of formation of product

1 0.5
2 4.8
Ans: Vmax = 101

53. Write out the equation that describes the mechanism for enzyme action used
as a model by Michaelis and Menten. List the important assumptions used by
Michaelis and Menten to derive a rate equation for this reaction.
Ans: The two equations are
One assumption is that [P] = 0 so that the rate of the reaction depends exclusively on
the breakdown of ES and is not influenced by the reverse reaction; that is, k -2 can be
ignored and V0 = k2 [ES]. This condition is possible only if early reaction times are
measured; the velocity, therefore, is an initial velocity. A second assumption is that
the rate of ES formation equals the rate of ES breakdown; in other words, the
reaction is at a steady state. A third assumption is [S] >> [Et], so that total [S], which
equals free substrate and enzyme-bound substrate, is essentially equal to [S].

54. For the reaction E + S  ES  P the Michaelis-Menten constant, K m, is
actually a summary of three terms. What are they? How is Km determined
graphically?
Ans: Km = (k2 + k-1)/ k1, where k-1 and k1 are the rate constants for the breakdown
and association, respectively, of the ES complex and k 2 is the rate constant for the
breakdown of ES to form E + P. K m can be determined graphically on a plot of V0 vs.
[S] by finding the [S] at which V0 = 1/2 Vmax. More conveniently, on a double-
reciprocal plot, the x-axis intercept = –1/ Km.

55. An enzyme catalyzes a reaction at a velocity of 20 µmol/min when the
concentration of substrate (S) is 0.01 M. The K m for this substrate is 1 X 10-5
M. Assuming that Michaelis-Menten kinetics are followed, what will the
reaction velocity be when the concentration of S is (a) 1 X 10 -5 M and (b) 1
X10-6 M?
Ans: The velocity of 20 µmol/min is essentially Vmax because it is measured at [S]

>> Km. (a) When [S] = 10-5 M = Km, V = 1/2 Vmax, or 10 µmol/min. (b) When [S] is 10 -6
M, velocity can be calculated from the Michaelis-Menten equation:
V0 = Vmax [S]/(Km + [S]) = (20 µmol/min)(10-6 M)/(10-5 + 10-6) = 1.8 µmol/min.

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Enzymes

How enzymes work

3. Enzymes are potent catalysts because they:

A) are consumed in the reactions they catalyze.

How enzymes work

A) bind a transition state intermediate, such that it cannot be converted back to

5. Which one of the following statements is true of enzyme catalysts?

A) Their catalytic activity is independent of pH.

How enzymes work

How enzymes work

How enzymes work

A) are not consumed in the reaction.

How enzymes work

How enzymes work

Enzyme kinetics as an approach to understanding mechanism

Enzyme kinetics as an approach to understanding mechanism

Enzyme kinetics as an approach to understanding mechanism

A) [ES] can be measured accurately.

Enzyme kinetics as an approach to understanding mechanism

A) As [S] increases, the initial velocity of reaction V0 also increases.

Enzyme kinetics as an approach to understanding mechanism

Enzyme kinetics as an approach to understanding mechanism

Enzyme kinetics as an approach to understanding mechanism

Enzyme kinetics as an approach to understanding mechanism

A) At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is

Enzyme kinetics as an approach to understanding mechanism

The Km for this enzyme is approximately:

Enzyme kinetics as an approach to understanding mechanism

Km becomes equivalent to:

Enzyme kinetics as an approach to understanding mechanism

Enzyme kinetics as an approach to understanding mechanism

A) determine the equilibrium constant for an enzymatic reaction.

Enzyme kinetics as an approach to understanding mechanism

1/V0 = Km /(Vmax[S]) + 1/Vmax

A) multiply the reciprocal of the x-axis intercept by -1.

Enzyme kinetics as an approach to understanding mechanism

A) the enzyme concentration.

Enzyme kinetics as an approach to understanding mechanism

Enzyme kinetics as an approach to understanding mechanism

A) curvature of the plot.

Enzyme kinetics as an approach to understanding mechanism

A) binds at several different sites on an enzyme.

A) generally increases when pH increases.

Enzyme kinetics as an approach to understanding mechanism

A) a Glu residue on the enzyme is involved in the reaction.

Examples of enzymatic reactions

Examples of enzymatic reactions

Examples of enzymatic reactions

A) binds covalently to the enzyme.

Examples of enzymatic reactions

A) is less stable when binding to an enzyme than the normal substrate.

Examples of enzymatic reactions

A) act as a general acid catalyst.

Examples of enzymatic reactions

A) Allosteric effectors give rise to sigmoidal V0 vs. [S] kinetic plots.

A) are regulated primarily by covalent modification.

A) Disulfide bonds near the phosphorylation site

A) A protein kinase-catalyzed phosphorylation converts trypsinogen to trypsin.

Regulatory enzymesPage: 227 Difficulty: 1 Ans: B