BCH: Chapter 6

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1. A The amount of energy released during a reaction tells 8. A The KM of hexokinase for glucose = 0.15 mM and for
nothing about the rate at which that fructose, KM = 1.5 mM. Which is the
reaction will occur. preferred substrate?
A. True A. Glucose.
B. False B. Fructose.
C. Neither substrate is preferred over the other.
2. A Refer to Exhibit 6A. What is the equilibrium constant for
D. You cannot tell from the data given.
the uncatalyzed reaction?
E. None of these answers is correct.
A. 0.9
B. 1.1 9. A Most enzyme reactions display first order kinetics for the
C. 2.5 individual substrates when the
D. Cannot be determined from the information provided. substrate concentration is low.
A. True
3. A Refer to Exhibit 6A. What is the Vmax of the enzyme?
B. False
A. 90 nM/s
B. 4500 µM/s 10. A Thermodynamically favorable reactions all release energy.
C. 200 µM/s A. True
D. 0.5 M/s B. False
4. A Refer to Exhibit 6A. What is the equilibrium constant for 11. A The E-S complex often shows as a slight depression in the
the enzyme-catalyzed reaction? energy profile for the reaction.
A. 0.9 A. True
B. 1.1 B. False
C. 2.5
12. A All catalysts work by lowering the activation energy for a
D. Cannot be determined from the information provided.
reaction.
5. A A transition state analogue A. True
A. binds tightly to the enzyme B. False
B. enhances the activity of the enzyme when bound to it
13. A A noncompetitive inhibitor
C. forms a complex with the enzyme that is energetically
A. binds to the enzyme at a site other than the active site
stable compared to the enzymesubstrate
B. is structurally related to the substrate
complex
C. does not affect the value of Vmax
D. will bind to the enzyme by the lock-and-key mechanism
D. decreases the value of KM
rather than the induced-fit
mechanism 14. A A Lineweaver-Burk plot is useful in the analysis of
enzymatic reactions because
6. A Refer to Exhibit 6A. "Restrainin" is an inhibitor of triose
A. it is easier to see whether points deviate from a straight
phosphate isomerase. When it is
line than from a curve
added to cells at a concentration of 0.4 nM, the enzyme's
B. it is not affected by the presence of inhibitors
apparent KM for the substrate is
C. it can be used whether or not the enzyme displays
altered to 100 µM, but the Vmax is unchanged.
Michaelis-Menten kinetics
A. This is a competitive inhibitor.
D. all of the above
B. This is an uncompetitive inhibitor.
C. This is a noncompetitive inhibitor. 15. A Generally speaking, a competitive inhibitor and the
D. This is an irreversible inhibitor substrate cannot both bind to the enzyme
at the same time.
7. A To study the nature of an enzyme, Vmax is not as good a
A. True
measurement as the catalytic rate
B. False
constant kcat because:
A. The Vmax is not a true constant since it depends on the 16. A What effect is seen on a Lineweaver-Burk graph when a
concentration of enzyme non-competitive inhibitor is added?
B. The Vmax cannot be measured A. The y-intercept is changed, but not change the slope of
C. The Vmax is only valid for allosteric enzymes the line.
D. none of these B. The slope of the line is changed, but not the y-intercept.
C. Both the y-intercept and the slope of the line are
changed.
D. Neither the y-intercept not the slope of the line is
changed.
17. A When an enzyme is saturated with substrates, 25. B It is important that at physiological conditions, enzymes
A. it will display zero-order kinetics. work at Vmax.
B. it will display first-order kinetics. A. True
C. it will display second-order kinetics. B. False
D. it will denature and cease to function.
26. B The value of Vmax changes in
18. A The main difference between a catalyzed and an A. competitive inhibition
uncatalyzed reaction is that B. noncompetitive inhibition
A. the activation energy of the catalyzed reaction is lower. C. both forms of inhibition
B. the catalyzed reaction has a more favorable free D. neither form of inhibition
energy change.
27. B Which of the following is more likely to inhibit regulatory
C. the catalyzed reaction has a more favorable enthalpy
subunits of an allosteric enzyme?
change.
A. A competitive inhibitor
D. the catalyzed reaction has a more favorable entropy
B. A non-competitive inhibitor
change.
C. An irreversible inhibitor
19. A If an inhibitor changes the slope of the Lineweaver-Burk D. All of these are equally likely to inhibit a regulatory
graph, but not the y-intercept, it is this subunit
type of inhibition:
28. B What effect is seen on a Lineweaver-Burk graph when a
A. Competitive.
competitive inhibitor is added?
B. Non-competitive.
A. The y-intercept is changed, but not change the slope of
C. Mixed Inhibition (uncompetitive inhibition).
the line.
D. You cannot tell from the data given.
B. The slope of the line is changed, but not the y-intercept.
E. More than one answer is correct.
C. Both the y-intercept and the slope of the line are
20. A In the reaction catalyzed by aspartate transcarbamoylase, changed.
a graph in which the rate is plotted D. Neither the y-intercept not the slope of the line is
against the concentration of substrate changed.
A. is sigmoidal, characteristic of an allosteric enzyme
29. B Non-competitive inhibitors have this effect:
B. shows that noncooperative kinetics are observed
A. Modifying the KM value.
C. shows that the reaction is zero order
B. Changing the value for Vmax.
D. is hyperbolic, characteristic of a nonallosteric enzyme
C. Interfering with substrate binding.
21. B If the y-intercept of a Lineweaver-Burk plot = 1.91 D. This type of inhibitor both changes the Vmax and
(sec/millimole) and the slope = 75.3 L/sec, interferes with substrate binding.
Vmax equals: E. All of these are correct.
A. 0.0254 millimoles per second.
30. B If an inhibitor changes the slope of the Lineweaver-Burk
B. 0.523 millimoles per second.
graph, but not the x-intercept, it is this
C. 5.23 millimoles per second.
type of inhibition:
D. 39.4 millimoles per second.
A. Competitive.
E. 75.3 millimoles per second.
B. Non-competitive.
22. B The Michaelis constant determines the Vmax of an C. Mixed Inhibition (uncompetitive inhibition).
enzymatic reaction. D. You cannot tell from the data given.
A. True E. More than one answer is correct.
B. False
31. B When the substrate concentration is low, an enzyme
23. B The KM expression is equal to reaction
A. (k1 + k2) / k-1 A. will display zero-order kinetics.
B. (k-1 + k2) / k1 B. will display first-order kinetics.
C. (k1 + k-1) / k2 C. will display second-order kinetics.
D. k-1 / k1 D. will denature and cease to function
24. B Which of the following inhibitors binds to the enzyme at a
site other than the active site?
A. competitive inhibitor
B. noncompetitive inhibitor
C. irreversible inhibitor
D. all of these
E. none of these
32. B Which of the following diseases has not been successfully 40. B The Michaelis-Menten approach to describing the kinetics
treated using the principles of of an enzyme-catalyzed reaction
enzyme inhibition? makes which of the following assumptions about the
A. AIDS. conversion of product into substrate?
B. Lactose intolerance A. The product binds reversibly to the enzyme in order to
C. Virus infection be converted into the substrate.
D. Neither AIDS nor virus infection. B. The product is not converted to substrate to any
E. All of these have been successfully treated using appreciable extent.
enzyme inhibitors. C. The product is converted to substrate following simple
first order kinetics.
33. B The initial rate of an enzymatic reaction is usually
D. The product is converted to substrate following simple
determined in order to assure that
second order kinetics.
A. the enzyme is active
B. there is no reverse reaction of product to the enzyme- 41. B The rate of a reaction depends on
substrate complex A. the free energy change
C. the substrate is not used up B. the activation energy
D. the experiment can be completed quickly C. the enthalpy change
D. the entropy chang
34. B The sign of Gibb's Free Energy is positive ("+") when energy
is released. 42. C Which of the following are related for a given enzyme?
A. True A. Vmax, KM, and percentage of a-helix
B. False B. Vmax, kcat, and percentage of b-sheet
C. Vmax, kcat, and turnover number
35. B The substrate will only bind to the enzyme when the
D. Vmax, KM, and molecular weight
shapes fit together rigidly.
A. True 43. C Which of the following statements regarding the Michaelis
B. False constant is false?
A. It is similar to the affinity constant between the enzyme
36. B The kinetic order of a reaction
and substrate.
A. can be determined by inspection from the coefficients
B. The dimension for the Michaelis constant is
of the balanced equation
concentration, such as molarity.
B. must be determined experimentally
C. The Michaelis constant determines the Vmax.
C. always depends on the concentration of enzyme
D. It is the substrate concentration necessary to reach 1/2
D. never depends on concentrations of reactants
Vmax.
37. B The order of a reaction can be determined from the
44. C Refer to Exhibit 6A. "Hindrate" is an inhibitor of triose
balanced equation for the reaction.
phosphate isomerase. When it is added
A. True
to cells at a concentration of 0.1 nM, the enzyme's KM for
B. False
the substrate is unchanged, but the
38. B The rate of a reaction is always dependent on the apparent Vmax is altered to 50 nM/sec.
concentration(s) of the reactant(s). A. This is a competitive inhibitor.
A. True B. This is an uncompetitive inhibitor.
B. False C. This is a noncompetitive inhibitor.
39. B First order kinetics means: D. This is an irreversible inhibitor
A. The rate of a reaction is independent of the amount of 45. C Refer to Exhibit 6A. "Restrainin" is an inhibitor of triose
reactant measured. phosphate isomerase. When it is
B. The rate of the reaction varies directly with the amount added to cells at a concentration of 0.4 nM, the enzyme's
of reactant measured. apparent KM for the substrate is
C. The rate of the reaction varies with the square of the altered to 100 µM, but the Vmax is unchanged.
amount of the reactant measured. In the following graph, which line best represents the
D. More information is needed to answer this question. Lineweaver-Burk plot obtained in the
E. None of these is correct. presence of restrainin?
A. A
B. B
C. C
D. D
E. E
46. C According to the steady-state assumption 53. C The reaction catalyzed by aspartate transcarbamoylase is
A. the product concentration does not change A. the first step in the synthesis of amino acids.
significantly B. the first step in the synthesis of fatty acids.
B. the substrate concentration is large and does not C. the first step in the synthesis of CTP and UTP.
change significantly D. is part of glycolysis.
C. the concentration of enzyme-substrate complex
54. C What effect is seen on a Lineweaver-Burk graph when a
remains constant with time
mixed-type inhibitor is added?
D. the free enzyme concentration is always in great excess
A. The y-intercept is changed, but not change the slope of
to the concentration of enzymesubstrate
the line.
complex
B. The slope of the line is changed, but not the y-
47. C In the induced-fit model of substrate binding to enzymes intercept.
A. the substrate changes its conformation to fit the active C. Both the y-intercept and the slope of the line are
site changed.
B. the active site changes its conformation to fit the D. Neither the y-intercept not the slope of the line is
substrate changed
C. there is a conformational change in the enzyme when
55. C What effect does a catalyst have on the DG° of a
the substrate binds
reaction?
D. there is aggregation of several enzyme molecules
A. A catalyst lowers the DG°.
when the substrate binds
B. A catalyst raises the DG°.
48. C As catalysts, enzymes are C. A catalyst has no effect on the DG°.
A. significantly less effective than nonenzymatic catalysts D. It depend on the specific catalyst.
B. slightly less effective than nonenzymatic catalysts
56. D The fundamental difference between competitive and
C. significantly more effective than nonenzymatic
noncompetitive inhibition is
catalysts
A. the degree of cooperativity of the reaction
D. slightly more effective than nonenzymatic catalysts
B. the size of the active site of the enzyme
49. C For competitive inhibition C. the manner of binding of substrate to the enzyme
A. the value of KM decreases D. the manner of binding of inhibitor to the enzyme
B. the value of Vmax decreases
57. D Enzymatic activity has an optimum temperature because
C. it is possible to overcome the effect of the inhibitor by
A. the component amino acids have varying melting
increasing the concentration of
points
substrate
B. the rate of reactions is thermodynamically controlled
D. none of the above
C. the side chains of essential residues are chemically
50. C Irreversible inhibitors of enzymatic reactions degraded at higher temperatures
A. bind to the enzyme only at low temperatures. D. raising the temperature speeds up the reaction until
B. affect only serine side chains. protein denaturation sets in
C. react with the enzyme to produce a protein that is not
58. D Which of the following is most directly related to the
enzymatically active and from which
speed of a reaction?
the original enzyme cannot be regenerated.
A. The temperature
D. are bound to the enzyme by the lock-and-key
B. The DG0 of the reaction
mechanism.
C. The DG of the reaction
51. C Given the rate law, rate = k[A][B], the overall reaction D. The DG0‡ of the reaction
order is E. None of these is correct.
A. zero
59. D Which of the following is not true?
B. one
A. In thermodynamics, spontaneous does not mean
C. two
instantaneous or even fast.
D. cannot be determined
B. If a reaction is spontaneous then it has a negative DG.
52. C A rate constant is C. Speed of a reaction is a kinetic parameter, not a
A. the rate of a reaction at standard temperature and thermodynamic one.
pressure. D. A reaction with a positive DG0 can never happen
B. the rate of a reaction at equilibrium.
C. a proportionality constant relating the rate of a reaction
to the concentration(s) of the
reactant(s).
D. a kind of transition state.
60. D The active site of an enzyme 67. D Which of the following is true?
A. is frequently located in a cleft in the enzyme. A. The E-S complex often dissociates with no reaction
B. is the portion of the enzyme to which the substrate taking place.
binds. B. The E-S complex must form before a reaction can take
C. contains the reactive groups that catalyze the reaction. place
D. all of these C. Once the E-S complex forms, it can go on to form
product or dissociate to E + S
61. D Competitive inhibitors have this effect:
D. All of these
A. Modifying the KM value.
B. Changing the value for Vmax. 68. D If the y-intercept of a Lineweaver-Burk plot = 1.91
C. Interfering with substrate binding. (sec/millimole) and the slope = 75.3 L/sec,
D. This type of inhibitor both changes the KM and KM equals:
interferes with substrate binding. A. 0.0254 millimolar (mM).
E. All of these are correct. B. 0.523 millimolar (mM).
C. 5.23 millimolar (mM).
62. D The Michaelis constant is
D. 39.4 millimolar (mM).
A. the rate constant for the formation of the substrate-
E. 75.3 millimolar (mM)
enzyme (E-S) complex.
B. the rate constant for the breakdown of the substrate- 69. D Refer to Exhibit 6A. What is the actual velocity of the
enzyme (E-S) complex to form free forward reaction under physiologic
enzyme and substrate. conditions?
C. the rate constant for the breakdown of the substrate- A. 2 nM/s
enzyme (E-S) complex to form free B. 45 nM/s
enzyme and product. C. 500 nM/s
D. a compilation of several rate constants for the reaction. D. 30 nM/s
63. D Which of the following describes the unique importance 70. D The steady state of an enzyme reaction is the following:
of protein Kinase Mæ (PKMæ)? A. The rate observed just after mixing the enzyme and
A. It is a protein kinase substrate.
B. It uses ATP to phosphorylate a substrate B. The rate observed and Vmax.
C. It is an allosteric enzyme C. The rate of product formation.
D. It has been implicated in the formation of long-term D. The state which exists when E-S complex is forming as
memories fast as it is breaking down.
E. The state which exists when substrate concentration
64. D Refer to Exhibit 6A. What is the KM of the enzyme?
equals KM
A. 10 nM
B. 0.1 µM 71. D The substrate-enzyme (E-S) complex
C. 1 µM A. always proceeds to form the products rapidly.
D. 10 µM B. always breaks down to form free enzyme and
substrate.
65. D The active site of an enzyme is the place where the
C. always breaks down to form free enzyme and product.
following happens:
D. may break down to form free enzyme and substrate, or
A. The enzyme substrate complex forms here.
free enzyme and product.
B. The catalytic reaction happens here.
C. Allosteric regulation of enzyme rate occurs here. 72. D The Michaelis constant is
D. The enzyme-substrate complex forms and the reaction A. related to the molecular weight of the enzyme
occurs at the active site. B. a measure of the resistance of the enzyme to
E. All of these are correct denaturation
C. a reflection of the percentage of polar amino acids in
66. D In the reaction catalyzed by chymotrypsin, a graph in
the enzyme
which the rate is plotted against the
D. a measure of how tightly the substrate is bound to the
concentration of substrate
enzyme
A. is sigmoidal, characteristic of an allosteric enzyme
B. shows that cooperative kinetics are observed
C. shows that the reaction is zero order
D. is hyperbolic, characteristic of a nonallosteric enzyme
73. E Which of the following is true about the enzyme chymotrypsin?
A. The enzyme can cleave peptides.
B. The enzyme can cleave esters.
C. The enzyme only binds to aromatic substrates.
D. The enzyme can cleave substrates which are not naturally occurring.
E. All of these are true.
74. E The drug acetazolamide:
A. Is used to help fight altitude sickness
B. Was found to ruin the taste of carbonated beverages
C. Does not affect the taste of non-carbonated liquors
D. Causes its effect on taste by inhibiting carbonic anhydrase 4
E. All of these
75. E Which of the following is implied by induced fit between the enzyme's active site and the
substrate?
A. The enzyme is a flexible molecule.
B. An enzyme will work equally well with different substrates.
C. An active site can bind to different substrates.
D. The enzyme is a flexible molecule so different substrates can bind.
E. All of these
76. E Inhibitors can have the following effects on enzyme kinetics:
A. Modifying the KM value.
B. Changing the value for Vmax.
C. Interfering with substrate binding.
D. An inhibitor can change the KM and interfere with substrate binding.
E. All of these are correct
77. E How much faster is a reaction with the fastest enzyme than without a catalyst?
A. About 10 times faster.
B. About 100 times faster.
C. About 1,000 times faster.
D. About 10,000 times faster.
E. About 1020 times faster.