Biochemistry 9th Edition Campbell Test Bank

Biochemistry 9th Edition Campbell Test
Bank
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Chapter 06 - The Behavior of Proteins: Enzymes
1. 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.
ANSWER: e
POINTS: 1
QUESTION TYPE: Multiple Choice
HAS VARIABLES: False
LEARNING OBJECTIVES: CAFA.BIOC.15.5 - Modified from 5e
TOPICS: Enzymes Are Effective Biological Catalysts
DATE CREATED: 12/23/2013 2:14 PM
DATE MODIFIED: 12/23/2013 2:14 PM
2. As catalysts, enzymes are

a. significantly less effective than nonenzymatic catalysts
b. slightly less effective than nonenzymatic catalysts
c. significantly more effective than nonenzymatic catalysts
d. slightly more effective than nonenzymatic catalysts
e. exactly the same as nonenzymatic catalysts
ANSWER: c
POINTS: 1
LEARNING OBJECTIVES: CAFA.BIOC.15.9 - Modified for 8e
TOPICS: Enzymes Are Effective Biological Catalysts
3. The rate of a reaction depends on

a. the free energy change
b. the activation energy
c. the enthalpy change
d. the entropy change
ANSWER: b
POINTS: 1
TOPICS: Kinetics Versus Thermodynamics
4. Enzymatic activity has an optimum temperature because

Copyright Cengage Learning. Powered by Cognero. Page 1
a. the component amino acids have varying melting points

b. the rate of reactions is thermodynamically controlled
c. the side chains of essential residues are chemically degraded at higher temperatures
d. raising the temperature speeds up the reaction until protein denaturation sets in
e. the organism dies beyond a certain temperature
ANSWER: d
POINTS: 1
LEARNING OBJECTIVES: CAFA.BIOC.15.7 - Modified in 8e
5. The main difference between a catalyzed and an uncatalyzed reaction is that

a. the activation energy of the catalyzed reaction is lower.
b. the catalyzed reaction has a more favorable free energy change.
c. the catalyzed reaction has a more favorable enthalpy change.
d. the catalyzed reaction has a more favorable entropy change.
ANSWER: a
POINTS: 1
6. Which of the following is not true?

a. In thermodynamics, spontaneous does not mean instantaneous or even fast.
b. If a reaction is spontaneous then it has a negative ΔG.
c. Speed of a reaction is a kinetic parameter, not a thermodynamic one.
d. A reaction with a positive ΔG0 can never happen
ANSWER: d
POINTS: 1
LEARNING OBJECTIVES: CAFA.BIOC.15.4 - New in 7e
7. What effect does a catalyst have on the ΔG° of a reaction?

a. A catalyst lowers the ΔG°.
b. A catalyst raises the ΔG°.
c. A catalyst has no effect on the ΔG°.

d. It depend on the specific catalyst.
ANSWER: c
POINTS: 1
8. Which of the following is most directly related to the speed of a reaction?

a. The temperature
b. The ΔG0 of the reaction
c. The ΔG of the reaction
d. The ΔG0‡ of the reaction
e. None of these is correct.
ANSWER: d
POINTS: 1
9. A rate constant is
a. the rate of a reaction at standard temperature and pressure.
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.
ANSWER: c
POINTS: 1
10. The rate of a reaction is always dependent on the concentration(s) of the reactant(s).
a. True
b. False
ANSWER: b
POINTS: 1
11. All catalysts work by lowering the activation energy for a reaction.
a. True
b. False
ANSWER: a
POINTS: 1
12. The amount of energy released during a reaction tells nothing about the rate at which that reaction will occur.
a. True
b. False
ANSWER: a
POINTS: 1
13. Thermodynamically favorable reactions all release energy.

a. True
b. False
ANSWER: a
POINTS: 1
14. The sign of Gibb's Free Energy is positive ("+") when energy is released.
a. True
b. False

ANSWER: b
POINTS: 1
15. Which of the following is true about lactate dehydrogenase (LDH)?

a. There are two types of subunits, H amd M, that combine to form 5 types of isozymes
b. An increase in H-based isozymes was once used to diagnose heart attacks
c. An increase in blood levels of LDH of any kind is indicative of some sort of problem
d. One type of LDH has only H subunits
e. All of the choices
ANSWER: e
POINTS: 1
TOPICS: Kinetcis vs. Thermodynamics
16. The order of a reaction can be determined from the balanced equation for the reaction.
a. True
b. False
ANSWER: b
POINTS: 1
TOPICS: Enzyme Kinetics Equations
17. The kinetic order of a reaction

a. can be determined by inspection from the coefficients of the balanced equation
b. must be determined experimentally
c. always depends on the concentration of enzyme
d. never depends on concentrations of reactants
ANSWER: b
POINTS: 1

18. Given the rate law, rate = k[A][B], the overall reaction order is
a. zero
b. one
c. two
d. cannot be determined
ANSWER: c
POINTS: 1
19. First order kinetics means:

a. The rate of a reaction is independent of the amount of reactant measured.
b. The rate of the reaction varies directly with the amount of reactant measured.
c. The rate of the reaction varies with the square of the amount of the reactant measured.
d. More information is needed to answer this question.
e. None of these is correct.
ANSWER: b
POINTS: 1
20. The active site of an enzyme

a. is frequently located in a cleft in the enzyme.
b. is the portion of the enzyme to which the substrate binds.
c. contains the reactive groups that catalyze the reaction.
d. all of these are correct
ANSWER: d
POINTS: 1
TOPICS: Enzyme-Substrate Binding

21. The substrate will only bind to the enzyme when the shapes fit together rigidly.
a. True
b. False
ANSWER: b
POINTS: 1
22. In the induced-fit model of substrate binding to enzymes

a. the substrate changes its conformation to fit the active site
b. the active site changes its conformation to fit the substrate
c. there is a conformational change in the enzyme when the substrate binds
d. there is aggregation of several enzyme molecules when the substrate binds
ANSWER: c
POINTS: 1
23. The E-S complex often shows as a slight depression in the energy profile for the reaction.
a. True
b. False
ANSWER: a
POINTS: 1
24. The active site of an enzyme is the place where the following happens:
a. The enzyme substrate complex forms here.
b. The catalytic reaction happens here.
c. Allosteric regulation of enzyme rate occurs here.
d. The enzyme-substrate complex forms and the reaction occurs at the active site.

e. All of these are correct.

ANSWER: d
POINTS: 1
25. 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 are correct
ANSWER: e
POINTS: 1
26. Which of the following is true?

a. The E-S complex often dissociates with no reaction taking place.
b. The E-S complex must form before a reaction can take place
c. Once the E-S complex forms, it can go on to form product or dissociate to E + S
d. All of these are correct
ANSWER: d
POINTS: 1
27. 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 correct
ANSWER: e
POINTS: 1
TOPICS: Examples of Enzyme-Catalyzed Reactions
28. The reaction catalyzed by aspartate transcarbamoylase is

a. the first step in the synthesis of amino acids.
b. the first step in the synthesis of fatty acids.
c. the first step in the synthesis of CTP and UTP.
d. is part of glycolysis.
ANSWER: c
POINTS: 1
29. In the reaction catalyzed by chymotrypsin, a graph in which the rate is plotted against the concentration of substrate
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
ANSWER: d
POINTS: 1
30. In the reaction catalyzed by aspartate transcarbamoylase, a graph in which the rate is plotted against the concentration
of substrate
a. is sigmoidal, characteristic of an allosteric enzyme
b. shows that noncooperative kinetics are observed
c. shows that the reaction is zero order
d. is hyperbolic, characteristic of a nonallosteric enzyme
ANSWER: a
POINTS: 1


31. The Michaelis-Menten approach to describing the kinetics of an enzyme-catalyzed reaction makes which of the
following assumptions about the conversion of product into substrate?
a. The product binds reversibly to the enzyme in order to be converted into the substrate.
b. The product is not converted to substrate to any appreciable extent.
c. The product is converted to substrate following simple first order kinetics.
d. The product is converted to substrate following simple second order kinetics.
ANSWER: b
POINTS: 1
TOPICS: Michaelis-Menten Approach
32. The initial rate of an enzymatic reaction is usually determined in order to assure that
a. the enzyme is active
b. there is no reverse reaction of product to the enzyme-substrate complex
c. the substrate is not used up
d. the experiment can be completed quickly
ANSWER: b
POINTS: 1
33. According to the steady-state assumption

a. the product concentration does not change significantly
b. the substrate concentration is large and does not change significantly
c. the concentration of enzyme-substrate complex remains constant with time
d. the free enzyme concentration is always in great excess to the concentration of enzyme-substrate complex
ANSWER: c
POINTS: 1


34. Most enzyme reactions display first order kinetics for the individual substrates when the substrate concentration is
low.
a. True
b. False
ANSWER: a
POINTS: 1
35. When the substrate concentration is low, an enzyme reaction

a. will display zero-order kinetics.
b. will display first-order kinetics.
c. will display second-order kinetics.
d. will denature and cease to function.
ANSWER: b
POINTS: 1
36. When an enzyme is saturated with substrates,

a. it will display zero-order kinetics.
b. it will display first-order kinetics.
c. it will display second-order kinetics.
d. it will denature and cease to function.
ANSWER: a
POINTS: 1
37. The Michaelis constant is

a. related to the molecular weight of the enzyme

b. a measure of the resistance of the enzyme to denaturation
c. a reflection of the percentage of polar amino acids in the enzyme
d. a rough measure of the affinity of the enzyme for the substrate
ANSWER: d
POINTS: 1
38. The KM expression is equal to

a. (k1 + k2) / k−1
b. (k−1 + k2) / k1
c. (k1 + k−1) / k2
d. k−1 / k1
ANSWER: b
POINTS: 1
39. Which of the following are related for a given enzyme?

a. Vmax, KM, and percentage of α-helix
b. Vmax, kcat, and percentage of β-sheet
c. Vmax, kcat, and turnover number
d. Vmax, KM, and molecular weight
e. None of these are related in any way
ANSWER: c
POINTS: 1
40. The Michaelis constant is

a. the rate constant for the formation of the substrate-enzyme (E-S) complex.
b. the rate constant for the breakdown of the substrate-enzyme (E-S) complex to form free enzyme and substrate.
c. the rate constant for the breakdown of the substrate-enzyme (E-S) complex to form free enzyme and product.
d. a compilation of several rate constants for the reaction.
ANSWER: d
POINTS: 1
41. 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
ANSWER: e
POINTS: 1
42. The substrate-enzyme (E-S) complex

a. always proceeds to form the products rapidly.
b. always breaks down to form free enzyme and substrate.
c. always breaks down to form free enzyme and product.
d. may break down to form free enzyme and substrate, or free enzyme and product.
ANSWER: d
POINTS: 1
43. When an enzyme-catalyzed reaction has two substrates and substrate A must bind before substrate B, the mechanism
is called
a. a ping-pong mechanism
b. a random mechanism
c. an ordered mechanism
d. a suicide mechanism
e. none of these is true
ANSWER: c
POINTS: 1
44. Which of the following is true concerning a ping-pong mechanism?

a. Either substrate can bind first
b. Either product can leave first
c. One product leaves before the second substrate binds
d. One product leaves before either substrate has bound
e. none of these are true
ANSWER: c
POINTS: 1
45. A Lineweaver-Burk plot is useful in the analysis of enzymatic reactions because

a. it is easier to see whether points deviate from a straight line than from a curve
b. it is not affected by the presence of inhibitors
c. it can be used whether or not the enzyme displays Michaelis-Menten kinetics
d. all of the above
ANSWER: a
POINTS: 1
46. The steady state of an enzyme reaction is the following:

a. The rate observed just after mixing the enzyme and substrate.
b. The rate observed and Vmax.

c. The rate of product formation.
d. The state which exists when E-S complex is forming as fast as it is breaking down.
e. The state which exists when substrate concentration equals KM.
ANSWER: d
POINTS: 1
47. If the y-intercept of a Lineweaver-Burk plot = 1.91 (sec/millimole) and the slope = 75.3 L/sec, Vmax equals:
a. 0.0254 millimoles per second.
b. 0.523 millimoles per second.
c. 5.23 millimoles per second.
d. 39.4 millimoles per second.
e. 75.3 millimoles per second.
ANSWER: b
POINTS: 1
48. If the y-intercept of a Lineweaver-Burk plot = 1.91 (sec/millimole) and the slope = 75.3 L/sec, KM equals:
a. 0.0254 millimolar (mM).
b. 0.523 millimolar (mM).
c. 5.23 millimolar (mM).
d. 39.4 millimolar (mM).
e. 75.3 millimolar (mM).
ANSWER: d
POINTS: 1
49. The Michaelis constant determines the Vmax of an enzymatic reaction.

a. True
b. False
ANSWER: b
POINTS: 1
50. It is important that at physiological conditions, enzymes work at Vmax.

a. True
b. False
ANSWER: b
POINTS: 1
Exhibit 6A
This is a reaction going on in your muscle cells right this very minute:
The enzyme triose phosphate isomerase catalyzes this reaction in the forward direction as part of the glycolytic pathway.
It follows simple Michaelis-Menten kinetics:
Typical cellular concentrations: triose phosphate isomerase = 0.1 nM

dihydroxyacetone phosphate = 5 µM glyceraldehyde-3-phosphate = 2 µM
51. Refer to Exhibit 6A. What is the equilibrium constant for the uncatalyzed reaction?
a. 0.9
b. 1.1
c. 2.5
d. Cannot be determined from the information provided.
ANSWER: a
POINTS: 1
PREFACE NAME: Exhibit 6A

52. Refer to Exhibit 6A. What is the KM of the enzyme?

a. 10 nM
b. 0.1 µM
c. 1 µM
d. 10 µM
ANSWER: d
POINTS: 1
53. Refer to Exhibit 6A. What is the Vmax of the enzyme?

a. 90 nM/s
b. 4500 µM/s
c. 200 µM/s
d. 0.5 M/s
ANSWER: a
POINTS: 1
54. Refer to Exhibit 6A. What is the actual velocity of the forward reaction under physiologic conditions?
a. 2 nM/s
b. 45 nM/s
c. 500 nM/s
d. 30 nM/s
ANSWER: d
POINTS: 1

55. Refer to Exhibit 6A. What is the equilibrium constant for the enzyme-catalyzed reaction?
a. 0.9
b. 1.1
c. 2.5
d. Cannot be determined from the information provided.
ANSWER: a
POINTS: 1
56. Refer to Exhibit 6A. "Restrainin" is an inhibitor of triose phosphate isomerase. When it is added to cells at a
concentration of 0.4 nM, the enzyme's apparent KM for the substrate is altered to 100 µM, but the Vmax is unchanged.
a. This is a competitive inhibitor.
b. This is an uncompetitive inhibitor.
c. This is a noncompetitive inhibitor.
d. This is an irreversible inhibitor.
ANSWER: a
POINTS: 1
TOPICS: Enzyme Inhibition
57. Refer to Exhibit 6A. "Restrainin" is an inhibitor of triose phosphate isomerase. When it is added to cells at a
concentration of 0.4 nM, the enzyme's apparent KM for the substrate is altered to 100 µM, but the Vmax is unchanged.
In the following graph, which line best represents the Lineweaver-Burk plot obtained in the presence of restrainin?

a. A
b. B
c. C
d. D
e. E
ANSWER: c
POINTS: 1
58. Refer to Exhibit 6A. "Hindrate" is an inhibitor of triose phosphate isomerase. When it is added to cells at a
concentration of 0.1 nM, the enzyme's KM for the substrate is unchanged, but the apparent Vmax is altered to 50 nM/sec.
a. This is a competitive inhibitor.
b. This is an uncompetitive inhibitor.
c. This is a noncompetitive inhibitor.
d. This is an irreversible inhibitor.
ANSWER: c
POINTS: 1
59. Refer to Exhibit 6A. "Hindrate" is an inhibitor of triose phosphate isomerase. When it is added to cells at a
concentration of 0.1 nM, the enzyme's KM for the substrate is unchanged, but the apparent Vmax is altered to 50 nM/sec.
In the following graph, which line best represents the Lineweaver-Burk plot obtained in the presence of hindrate?

a. A
b. B
c. C
d. D
e. E
ANSWER: a
POINTS: 1
60. Which of the following statements regarding the Michaelis constant is false?
a. It is similar to the affinity constant between the enzyme and substrate.
b. The dimension for the Michaelis constant is concentration, such as molarity.
c. The Michaelis constant determines the Vmax.
d. It is the substrate concentration necessary to reach 1/2 Vmax.
ANSWER: c
POINTS: 1
61. To study the nature of an enzyme, Vmax is not as good a measurement as the catalytic rate constant kcat because:
a. The Vmax is not a true constant since it depends on the concentration of enzyme
b. The Vmax cannot be measured
c. The Vmax is only valid for allosteric enzymes
d. none of these
ANSWER: a
POINTS: 1
62. The KM of hexokinase for glucose = 0.15 mM and for fructose, KM = 1.5 mM. Which is the preferred substrate?
a. Glucose.
b. Fructose.
c. Neither substrate is preferred over the other.
d. You cannot tell from the data given.
e. None of these answers is correct.
ANSWER: a
POINTS: 1
63. Competitive inhibitors have this effect:

a. Modifying the KM value.
b. Changing the value for Vmax.
c. Interfering with substrate binding.
d. This type of inhibitor both changes the KM and interferes with substrate binding.
ANSWER: d
POINTS: 1
64. 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
ANSWER: b
POINTS: 1
65. Inhibitors can have the following effects on enzyme kinetics:

d. An inhibitor can change the KM and interfere with substrate binding.
ANSWER: e
POINTS: 1
66. The value of Vmax changes in

a. competitive inhibition
b. noncompetitive inhibition
c. both forms of inhibition
d. neither form of inhibition
ANSWER: b
POINTS: 1
67. The fundamental difference between competitive and noncompetitive inhibition is

a. the degree of cooperativity of the reaction
b. the size of the active site of the enzyme
c. the manner of binding of substrate to the enzyme
d. the manner of binding of inhibitor to the enzyme
ANSWER: d
POINTS: 1

68. Which of the following is more likely to inhibit regulatory subunits of an allosteric enzyme?
a. A competitive inhibitor
b. A non-competitive inhibitor
c. An irreversible inhibitor
d. All of these are equally likely to inhibit a regulatory subunit
ANSWER: b
POINTS: 1
69. For competitive inhibition

a. the value of KM decreases
b. the value of Vmax decreases
c. it is possible to overcome the effect of the inhibitor by increasing the concentration of substrate
d. none of the above
ANSWER: c
POINTS: 1
70. Irreversible inhibitors of enzymatic reactions

a. bind to the enzyme only at low temperatures.
b. affect only serine side chains.
c. react with the enzyme to produce a protein that is not enzymatically active and from which the original
enzyme cannot be regenerated.
d. are bound to the enzyme by the lock-and-key mechanism.
ANSWER: c
POINTS: 1

71. A noncompetitive inhibitor

a. binds to the enzyme at a site other than the active site
b. is structurally related to the substrate
c. does not affect the value of Vmax
d. decreases the value of KM
ANSWER: a
POINTS: 1
72. What effect is seen on a Lineweaver-Burk graph when a competitive inhibitor is added?
a. The y-intercept is changed, but not change the slope of the line.
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.
ANSWER: b
POINTS: 1
73. What effect is seen on a Lineweaver-Burk graph when a mixed-type inhibitor is added?
ANSWER: c
POINTS: 1

74. Generally speaking, a competitive inhibitor and the substrate cannot both bind to the enzyme at the same time.
a. True
b. False
ANSWER: a
POINTS: 1
75. What effect is seen on a Lineweaver-Burk graph when a non-competitive inhibitor is added?
ANSWER: a
POINTS: 1
76. Non-competitive inhibitors have this effect:

d. This type of inhibitor both changes the Vmax and interferes with substrate binding.
ANSWER: b
POINTS: 1
77. If an inhibitor changes the slope of the Lineweaver-Burk graph, but not the y-intercept, it is this type of inhibition:
a. Competitive.
b. Non-competitive.
c. Mixed Inhibition (uncompetitive inhibition).
e. More than one answer is correct.

ANSWER: a
POINTS: 1
78. If an inhibitor changes the slope of the Lineweaver-Burk graph, but not the x-intercept, it is this type of inhibition:
a. Competitive.
b. Non-competitive.
c. Mixed Inhibition (uncompetitive inhibition).
e. More than one answer is correct.
ANSWER: b
POINTS: 1
79. Which of the following diseases has not been successfully treated using the principles of enzyme inhibition?
a. AIDS.
b. Lactose intolerance
c. Virus infection
d. Neither AIDS nor virus infection.
e. All of these have been successfully treated using enzyme inhibitors.
ANSWER: b
POINTS: 1
80. Which of the following is true about a mixed type inhibition?

a. A Lineweaver-Burk plot will give parallel lines
b. The KM will change but not the Vmax
c. The lines of a Lineweaver-Burk graph will cross in the top left quadrant
d. None of these is true
ANSWER: c
POINTS: 1
81. Pure noncompetitive inhibition is a limiting case of

a. Competitive inhibition
b. Uncompetitive inhibition
c. Irreversible inhibition
d. Mixed inhibition
e. None of these is true
ANSWER: d
POINTS: 1
82. Which of the following is the most unique about an uncompetitive inhibitor?
a. It affects the KM of the enzyme
b. It affects the Vmax of the enzyme
c. It can be identified by a Lineweaver-Burk plot
d. The inhibitor can bind to ES but not to free E
e. None of these is particularly unique to an uncompetitive inhibitor
ANSWER: d
POINTS: 1
83. Which of the following is not related to the others?

a. Suicide Substrate
b. Irreversible Inhibitor
c. Trojan Horse substrate
d. Competitive Inhibitor
e. All of these are related
ANSWER: d
POINTS: 1
84. Nonenzymatic catalysts enhance the rate of a reaction by factors of _____.

a. 105 to 109
b. 102 to 104
c. 1015 to 1020
d. 1022 to 1024
ANSWER: b
POINTS: 1
TOPICS: Enzyme Kinetics vs. Thermodynamics
DATE CREATED: 11/25/2016 7:19 AM
DATE MODIFIED: 11/25/2016 7:20 AM
85. Identify a true statement about the enzyme creatine kinase (CK).
a. Creatine kinase (CK) is found only in brain and skeletal muscles.
b. After a heart attack, creatine kinase (CK) shows up more rapidly in blood than lactate dehydrogenase (LDH).
c. Creatine kinase (CK) is an isozyme as it can exist in five different forms.
d. A high level of creatine kinase (CK) in brain indicates normal functioning of the brain.
ANSWER: b
POINTS: 1
TOPICS: Enzyme Kinetics vs. Thermodynamics
86. The rate of the reaction of glycogenn with inorganic phosphate, Pi, to form glucose-1-phosphate and glycogenn-1 is
_____.
a. rate = k[Glycogen]1[Pi]1
b. rate = k[Glycogen]0[Pi]1
c. rate = k[Glucose-1-phosphate]1[Pi]1
d. rate = k[Glucose-1-phosphate]0[Pi]1
ANSWER: a
POINTS: 1
TOPICS: Rate of Enzyme-Catalyzed Reactions
87. The rate of a zero-order reaction depends on the _____.

a. total number of reactants
b. concentration of products
c. concentration of reactants
d. presence of catalysts
ANSWER: d
POINTS: 1
TOPICS: Rate of Enzyme-Catalyzed Reactions
88. Explain the mechanism of the lock-and-key model of enzyme-substrate binding.

ANSWER: The lock-and-key model assumes a high degree of similarity between the shape of the substrate and
the geometry of the binding site on the enzyme. The substrate binds to a site whose shape
complements its own shape, like a key in a lock or the correct piece in a three-dimensional jigsaw
puzzle.
POINTS: 1
QUESTION TYPE: Essay

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Biochemistry 9th Edition Campbell Test

2. As catalysts, enzymes are

3. The rate of a reaction depends on

4. Enzymatic activity has an optimum temperature because

a. the component amino acids have varying melting points

5. The main difference between a catalyzed and an uncatalyzed reaction is that

6. Which of the following is not true?

7. What effect does a catalyst have on the ΔG° of a reaction?

c. A catalyst has no effect on the ΔG°.

8. Which of the following is most directly related to the speed of a reaction?

13. Thermodynamically favorable reactions all release energy.

Copyright Cengage Learning. Powered by Cognero. Page 4

15. Which of the following is true about lactate dehydrogenase (LDH)?

17. The kinetic order of a reaction

LEARNING OBJECTIVES: CAFA.BIOC.15.7 - Modified in 8e

19. First order kinetics means:

20. The active site of an enzyme

TOPICS: Enzyme-Substrate Binding

22. In the induced-fit model of substrate binding to enzymes

Copyright Cengage Learning. Powered by Cognero. Page 7

e. All of these are correct.

26. Which of the following is true?

27. Which of the following is true about the enzyme chymotrypsin?

28. The reaction catalyzed by aspartate transcarbamoylase is

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QUESTION TYPE: Multiple Choice

33. According to the steady-state assumption

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DATE CREATED: 12/23/2013 2:14 PM

35. When the substrate concentration is low, an enzyme reaction

36. When an enzyme is saturated with substrates,

37. The Michaelis constant is

a. related to the molecular weight of the enzyme

38. The KM expression is equal to

39. Which of the following are related for a given enzyme?

40. The Michaelis constant is

41. The drug acetazolamide:

42. The substrate-enzyme (E-S) complex

44. Which of the following is true concerning a ping-pong mechanism?

45. A Lineweaver-Burk plot is useful in the analysis of enzymatic reactions because

46. The steady state of an enzyme reaction is the following:

b. The rate observed and Vmax.

49. The Michaelis constant determines the Vmax of an enzymatic reaction.

50. It is important that at physiological conditions, enzymes work at Vmax.

Typical cellular concentrations: triose phosphate isomerase = 0.1 nM

PREFACE NAME: Exhibit 6A

52. Refer to Exhibit 6A. What is the KM of the enzyme?

53. Refer to Exhibit 6A. What is the Vmax of the enzyme?

DATE CREATED: 12/23/2013 2:14 PM

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63. Competitive inhibitors have this effect:

65. Inhibitors can have the following effects on enzyme kinetics:

66. The value of Vmax changes in

67. The fundamental difference between competitive and noncompetitive inhibition is

HAS VARIABLES: False

69. For competitive inhibition

70. Irreversible inhibitors of enzymatic reactions

DATE CREATED: 12/23/2013 2:14 PM

71. A noncompetitive inhibitor

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76. Non-competitive inhibitors have this effect:

e. More than one answer is correct.

80. Which of the following is true about a mixed type inhibition?