Ch08 Test File-Energy, Enzymes, and Metabolism

Test File
to accompany
Life: The Science of Biology, Ninth Edition
Sadava • Hillis • Heller • Berenbaum
Chapter 8: Energy, Enzymes, and Metabolism
TEST FILE QUESTIONS

(By Catherine Ueckert)
Multiple Choice
1. Lactose intolerance is due to the

a. inability to hydrolyze polysaccharides.
b.body’s ability to digest lactose but inability to absorb the resulting products.
c. gaseous side products produced in the small intestine.
d.inability to produce the enzyme lactase.
e. inability to oxidate luciferase.
Answer: d
Textbook Reference: 8.0 Lactase deficiency, p. 148
Bloom’s Category: 2. Understanding
2. Water held back by a dam represents what kind of energy?

a. Hydroelectric
b.Irrigation
c. Potential
d.Kinetic
e. At times, all of the above
Answer: c
Textbook Reference: 8.1 What Physical Principles Underlie Biological Energy
Transformations? p. 149
3. Which of the following represents potential energy?

a. Chemical bonds
b.Concentration gradient
c. Electric charge imbalance
d.Both a and b
e. All of the above
Answer: e
4. What can never be created or destroyed?
a. Entropy
b.Energy
c. Free energy only
d.Thermal energy only
e. Potential energy only
Answer: b
Transformations? pp. 149–150
Bloom’s Category: 1. Remembering
5. The sum total of all the chemical reactions in a living structure is called its
a. energetics.
b.activity.
c. digestive power.
d.entropy.
e. metabolism.
Answer: e
6. How does the second law of thermodynamics apply to organisms?

a. As energy transformations occur, free energy increases and unusable energy
decreases.
b.To maintain order, life requires a constant input of energy.
c. The potential energy of ATP is converted to kinetic energy such as muscle
contractions.
d.Reactions occur only with an input of energy.
e. It does not apply to organisms; the complexity of organisms contradicts the second
law.
Answer: b
7. During photosynthesis, plants use light energy to synthesize glucose from carbon
dioxide. However, plants do not use up energy during photosynthesis; they merely
convert it from light energy to chemical energy. This process is an illustration of
a. increasing entropy.
b.chemical equilibrium.
c. the first law of thermodynamics.
d.the second law of thermodynamics.
e. a spontaneous reaction.
Answer: c
8. The first law of thermodynamics states that the total energy in the universe is
a. decreasing.
b.increasing.
c. constant.
d.being converted to free energy.
e. being converted to matter.
Answer: c
9. In any system, the total energy includes usable and unusable energy. The unusable
energy is a measure of the disorder of the system and is referred to as
a. free energy.
b.entropy.
c. enthalpy.
d.thermodynamics.
e. equilibrium.
Answer: b
10. A change in free energy is related to a change in

a. temperature.
b.entropy.
c. pressure.
d.Both a and b
e. All of the above
Answer: d
11. If ΔG of a chemical reaction is negative and the change in entropy is positive, you
can conclude that the reaction
a. requires energy.
b.is endergonic.
c. is exergonic.
d.will not reach equilibrium.
e. decreases the disorder in the system.
Answer: c
12. A readily reversible reaction, in which reactants and products have almost the same
free energies, is indicated by a
a. slightly negative ΔG.
b.change in free energy.
c. negative ΔG.
d.ΔG near zero.
e. large positive ΔG.
Answer: d
13. The standard free energy change for the hydrolysis of ATP to ADP + Pi is –7.3
kcal/mol. From this information, one can conclude that the
a. reaction will never reach equilibrium.
b.free energy of ADP and phosphate is higher than the free energy of ATP.
c. reaction requires energy.
d.reaction is endergonic.
e. reaction is exergonic.
Answer: e
14. Which of the following statements about the exergonic hydrolysis of maltose to
glucose is true?
a. The reaction requires the input of free energy.
b.The free energy of glucose is larger than the free energy of maltose.
c. The reaction is not spontaneous.
d.The reaction releases free energy.
e. At equilibrium, the concentration of maltose is higher than the concentration of
glucose.
Answer: d
Bloom’s Category: 4. Analyzing
15. Chemical equilibrium

a. is a dynamic state.
b.represents a state of negative energy change.
c. represents a state of positive energy change.
d.cannot exist in nature.
e. is a state in which ΔG = 0.
Answer: e
16. If the enzyme phosphohexoisomerase is added to a 0.3 M solution of fructose 6-

phosphate, and the reaction is allowed to proceed to equilibrium, the final
concentrations are 0.2 M glucose 6-phosphate and 0.1 M fructose 6-phosphate.
These data give an equilibrium constant of 2. What is the equilibrium constant if the
initial concentration of fructose 6-phosphate is 3 M?
a. 2
b.3
c. 5
d.10
e. 20
Answer: a
Bloom’s Category: 3. Applying
17. When ADP gains a phosphate to form ATP,

a. free energy is released by the loss of a phosphate.
b.energy is consumed.
c. the reaction ends.
d.chemical energy is converted to light energy.
e. ribose loses an oxygen to become deoxyribose.
Answer: b
Textbook Reference: 8.2 What Is the Role of ATP in Biochemical Energetics? p. 154
18. Luciferin and luciferase are added to soft drinks because

a. they enhance the taste.
b.they act as preservatives.
c. they detect bacterial contamination by “lighting up.”
d.luciferase speeds up the release of monosaccharides.
e. they hydrolyze disaccharides.
Answer: c
19. ATP can phosphorylate many different molecules. This means that ATP can
a. receive phosphate groups.
b.donate phosphate groups.
c. convert molecules to nucleic acids.
d.store a large amount of energy when hydrolyzed.
e. All of the above
Answer: b
20. Fireflies
a. release a considerable amount of energy as heat.
b.light up to signal danger.
c. use ATP to begin luciferin oxidation.
d.are constantly converting light energy into chemical energy.
e. have a short life cycle due to rapid depletion of ATP.
Answer: c
21. Phosphorylation of ADP to ATP is endergonic, whereas the hydrolysis of ATP to

ADP is exergonic. The two reactions are therefore said to be
a. substrates.
b.endergonic.
c. kinetic.
d.activated.
e. coupled.
Answer: e
22. In glycolysis, the exergonic reaction 1,3-diphosphoglycerate → 3-phosphoglycerate

is coupled to the reaction ADP + Pi → ATP. Which of the following is most likely to
be true about the reaction ADP + Pi → ATP?
a. The reaction never reaches equilibrium.
b.The reaction is spontaneous.
c. There is a large decrease in free energy.
d.The reaction is endergonic.
e. Temperature will not affect the rate constant of the reaction.
Answer: d
23. Which of the following statements about ATP is true?

a. The hydrolysis of ATP is exergonic.
b.ATP consists of adenine bonded to deoxyribose.
c. ATP releases a relatively small amount of energy when hydrolyzed.
d.An active cell requires about 100 molecules of ATP per second.
e. On average, ATP is consumed within one second of its formation.
Answer: e
24. An RNA molecule that has enzyme activity is called

a. RNAse.
b.ribonuclease.
c. an allosteric enzyme.
d.a regulatory enzyme.
e. a ribozyme.
Answer: e
Textbook Reference: 8.3 What Are Enzymes? p. 156
25. The rate of a chemical reaction in a cell is the measure of how

a. often the reaction occurs.
b.quickly the reaction reaches equilibrium.
c. much energy must be added for the reaction to occur.
d.much activation energy is required for the reaction to occur.
e. easily the reaction is inhibited.
Answer: b
26. Knowing the change in free energy (ΔG) of a reaction tells us

a. the equilibrium point of the reaction.
b.the rate of the reaction.
c. how fast equilibrium will be reached.
d.the optimum temperature for the reaction.
e. the activation energy.
Answer: a
27. Which of the following is an example of an exergonic reaction?

a. The beating cilia of a protozoan
b.Cellular respiration
c. Phagocytosis
d.Receptor-mediated endocytosis
e. The Na+–K+ pump
Answer: b
28. Which of the following statements about enzymes is false?

a. An enzyme changes shape when it binds to a substrate.
b.Enzymes lower the activation energy.
c. Enzymes are highly specific.
d.An enzyme may orient substrates, induce strain, or temporarily add chemical
groups.
e. Most enzymes are much smaller than their substrates.
Answer: e
29. What is a transition state?

a. The place where a substrate molecule binds to an enzyme
b.A reactant with high potential energy
c. The combination of a substrate and an enzyme
d.The state at which the bonds of reactants are unstable
e. The active site where reactants are oriented
Answer: d
30. In a chemical reaction, transition-state species have free energies that are
a. lower than either the reactants or the products.
b.higher than either the reactants or the products.
c. lower than the reactants, but higher than the products.
d.higher than the reactants, but lower than the products.
e. lower than the reactants, but the same as the products.
Answer: b
31. Which of the following determines the rate of a reaction?

a. ΔS
b.ΔG
c. ΔH
d.The activation energy
e. The overall change in free energy
Answer: d
32. The hydrolysis of sucrose to glucose and fructose is exergonic. However, if sucrose
is dissolved in water and the solution is kept overnight at room temperature, there is
no detectable conversion to glucose and fructose. Why?
a. The change in free energy of the reaction is positive.
b.The activation energy of the reaction is high.
c. The change in free energy of the reaction is negative.
d.This is a condensation reaction.
e. The free energy of the products is higher than the free energy of the reactants.
Answer: b
33. Trypsin and elastase are both enzymes that catalyze hydrolysis of peptide bonds. But
trypsin only cuts next to lysine and elastase only cuts next to alanine. Why?
a. Trypsin is a protein, and elastase is not.
b.ΔG for the two reactions is different.
c. The shape of the active site for the two enzymes is different.
d.One of the reactions is endergonic, and the other is exergonic.
e. Hydrolysis of lysine bonds requires water; hydrolysis of alanine bonds does not.
Answer: c
34. The statement “enzymes are highly specific” means that certain
a. enzymes are found in certain cells.
b.reactions involving certain substrates are catalyzed by specific enzymes.
c. enzymes require certain concentrations of substrates.
d.reactions with certain activation energies are catalyzed by certain enzymes.
e. concentrations of substrates work with certain enzymes.
Answer: b
35. An active site is

a. the part of the substrate that binds with an enzyme.
b.the part of the enzyme that binds with a substrate.
c. the site where energy is added to an enzyme catalyst.
d.the site where enzymes are found in cells.
e. None of the above
Answer: b
36. In some cases, a substrate–enzyme complex is stabilized by

a. hydrogen bonds.
b.covalent bonds.
c. ionic attractions.
d.hydrophobic interactions.
e. All of the above
Answer: e
37. The molecules that are acted on by an enzyme are called

a. products.
b.substrates.
c. carriers.
d.prosthetics.
e. effectors.
Answer: b
38. The enzyme sucrase increases the rate at which sucrose is broken down into glucose
and fructose. Sucrase works by
a. increasing the amount of free energy of the reaction.
b.lowering the activation energy of the reaction.
c. decreasing the equilibrium constant of the reaction.
d.supplying energy to speed up the reaction.
e. changing the shape of the active site.
Answer: b
39. Which of the following statements about enzymes is true?

a. Enzymes are proteins.
b.Enzymes have a specific amino acid sequence.
c. Enzymes are highly specific.
d.Enzymes lower the energy barrier.
e. All of the above
Answer: e
40. The enzyme -amylase increases the rate at which starch is broken down into
smaller oligosaccharides by _______ of the reaction.
a. decreasing the equilibrium constant
b.increasing the change in free energy
c. decreasing the change in free energy
d.increasing the change in entropy
e. lowering the activation energy
Answer: e
41. The enzyme glyceraldehyde 3-phosphate dehydrogenase catalyzes the reaction

glyceraldehyde 3-phosphate → 1,3-diphosphoglycerate. The binding of the
glyceraldehyde 3-phosphate to the enzyme creates a(n)
a. transition state.
b.activation groove.
c. catalyst.
d.enzyme–substrate complex.
e. energy barrier.
Answer: d
42. The enzyme glucose oxidase binds the six-carbon sugar glucose and catalyzes its
conversion to glucono-1,4-actone. Mannose is also a six-carbon sugar, but glucose
oxidase cannot bind mannose. The specificity of glucose oxidase is based on the
a. free energy of the transition state.
b.activation energy of the reaction.
c. change in free energy of the reaction.
d.three-dimensional shape and structure of the active site.
e. rate constant of the reaction.
Answer: d
43. Binding of substrate to the active site of an enzyme is

a. reversible.
b.irreversible.
c. noncompetitive.
d.coupled.
e. allosteric.
Answer: a
44. Which of the following is an enzyme?

a. Manganese dioxide
b.Hemoglobin
c. Catalase
d.Hydrogen peroxide
e. Malathion
Answer: c
45. The presence of a catalyst affects the

a. amount of activation energy required.
b.overall energy change, or ΔG.
c. energy of the reactants.
d.energy of the products.
e. free energy of the transition state.
Answer: e
Textbook Reference: 8.3 What Are Enzymes? pp. 157–158
46. Enzymes of the acid–base catalysis type contain

a. a metal ion bound to a side chain.
b.a prosthetic group.
c. a coenzyme.
d.acidic or basic amino acid side chains (R groups) in the active site.
e. a covalently activated active site.
Answer: d
Textbook Reference: 8.4 How Do Enzymes Work? p. 158
47. The catalysis mechanism used by lysozyme to break down bacterial cell walls is
a. acid–base catalysis.
b.covalent catalysis.
c. metal cofactor redox catalysis.
d.induced strain.
e. unknown.
Answer: d
48. Enzymes catalyze a reaction by _______ the substrates.

a. orienting
b.inducing strain in
c. adding chemical groups to
d.adding charges to
e. All of the above
Answer: e
49. The ability of an enzyme to change shape when it binds to its substrate is called
a. induced fit.
b.enzyme flex.
c. the lock-and-key paradox.
d.substrate-induced active site shaping.
e. enzyme retrofit.
Answer: a
50. In the presence of alcohol dehydrogenase, the rate of reduction of acetaldehyde to

ethanol increases as the concentration of acetaldehyde is increased. Eventually, the
rate of the reaction reaches a maximum, at which point further increases in the
concentration of acetaldehyde have no effect. Why?
a. All the alcohol dehydrogenase molecules are bound to acetaldehyde molecules.
b.At high concentrations of acetaldehyde, the activation energy of the reaction
increases.
c. At high concentrations of acetaldehyde, the activation energy of the reaction
decreases.
d.The enzyme is no longer specific for acetaldehyde.
e. At high concentrations of acetaldehyde, the change in free energy of the reaction
decreases.
Answer: a
51. Many enzymes require ATP and ADP for a reaction to occur. They temporarily bind
to and then release from the substrate to participate in other reactions. ATP and ADP
are considered
a. a side chain.
b.coenzymes.
c. a coupled reaction.
d.a prosthetic group.
e. cofactors.
Answer: b
52. Enzymatic reactions can become saturated as substrate concentration increases

because
a. enzymes have the maximum possible number of hydrogen atoms attached to them.
b.the concentration of substrate reaches a point at which it cannot increase any
further.
c. substrates are inhibitors of enzymes.
d.the activation energy of the reaction reaches a point at which it cannot be lowered
further.
e. there are a limited number of the enzyme molecules present.
Answer: e
53. Competitive inhibitors of enzymes work by

a. fitting into the active site.
b.fitting into a site other than the active site.
c. altering the shape of the enzyme.
d.changing the enzyme into an inactive form.
e. increasing the activation energy of the enzyme-catalyzed reaction.
Answer: a
Textbook Reference: 8.5 How Are Enzyme Activities Regulated? p. 162
54. Nerve gases such as Sarin and malathion
a. block specific chemical transformations by inactivating specific enzymes.
b.have reversible effects on animals.
c. are proteins with a primary structure.
d.block the energy coupling cycle of ATP.
e. bond covalently to the active site of the enzyme.
Answer: a
55. How do competitive and noncompetitive enzyme inhibitors differ?

a. Competitive inhibitors bind to the active site, whereas noncompetitive inhibitors
change the shape of the active site.
b.Competitive inhibitors have a higher energy of activation than noncompetitive
inhibitors have.
c. They function at different pH values.
d.Noncompetitive enzyme inhibitors contain magnesium, whereas competitive
inhibitors contain iron.
e. Noncompetitive enzyme inhibitors are reversible, whereas competitive inhibitors
are irreversible.
Answer: a
56. The addition of the competitive inhibitor mevinolin slows the reaction HMG-CoA
→ mevalonate, which is catalyzed by the enzyme HMG-CoA reductase. The effects
of mevinolin would be overcome and the rate of the reaction increased by
a. adding more mevalonate.
b.adding more HMG-CoA.
c. lowering the temperature of the reaction.
d.adding a prosthetic group.
e. lowering the rate constant of the reaction.
Answer: b
57. A noncompetitive inhibitor inhibits binding of a substrate to an enzyme by

a. binding to the substrate.
b.binding to the active site.
c. lowering the activation energy.
d.increasing the ΔG of the reaction.
e. changing the shape of the active site.
Answer: e
58. Which type of inhibitor can be overcome completely by the addition of more
substrate?
a. Irreversible
b.Noncompetitive
c. Competitive
d.Prosthetic
e. Isotonic
Answer: c
59. An allosteric inhibitor

a. decreases the concentration of an inactive enzyme.
b.changes the shape of an enzyme.
c. increases the concentration of a product.
d.changes the shape of a substrate.
e. increases the concentration of an enzyme–substrate complex.
Answer: b
60. Allosteric inhibitors act by

a. decreasing the number of enzyme molecules.
b.increasing the number of enzyme molecules.
c. decreasing the amount of the inactive form of the enzyme.
d.decreasing the amount of the active form of the enzyme.
e. increasing the amount of substrate.
Answer: d
61. The inhibition of enzyme activity by noncompetitive inhibitors can be reduced

a. by decreasing the concentration of allosteric enzymes.
b.by decreasing the concentration of substrate.
c. by increasing the concentration of competitive inhibitor.
d.by increasing the concentration of substrate.
e. only when they become unbound.
Answer: e
62. The maximum possible rate of an enzyme reaction that is influenced by a

competitive inhibitor depends on the concentration of
a. inhibitor.
b.substrate.
c. product.
d.enzyme.
e. free energy.
Answer: b
63. Negative feedback in a sequence of chemical reactions involves a chemical that

appears _______ in the sequence and _______ reaction.
a. late; inhibits an earlier
b.early; inhibits a later
c. early; activates a later
d.late; activates an earlier
e. late; inhibits a later
Answer: a
64. Which of the following statements about allosteric regulators is true?

a. The plot for allosteric regulators often has a sigmoid curve.
b.All enzymes are allosterically regulated.
c. Enzymes that are allosterically regulated are made of multiple polypeptide
subunits.
d.Both the active site and the regulatory site are present on the same subunit.
e. Allosteric regulators bind to the active site, blocking enzyme function.
Answer: a
Textbook Reference: 8.5 How Are Enzyme Activities Regulated? pp. 163–164
65. Enzymes are sensitive to

a. temperature.
b.pH.
c. irreversible inhibitors such as DIPF.
d.allosteric effectors.
e. All of the above
Answer: e
66. The process that involves an end product acting as an inhibitor of an earlier step in a
metabolic pathway is called
a. feedback activation.
b.feedback inhibition.
c. positive feedback.
d.concerted activation.
e. competitive inhibition.
Answer: b
67. Enzymes are highly sensitive to pH and temperature because

a. changes in the environment raise their activation energy.
b.changes in temperature and pH readily break their hydrogen bonds.
c. of their three-dimensional structure and side chains.
d.at extreme temperatures and pH levels, coenzymes add chemical groups to the
substrate.
e. extremes of temperature and pH level change the ionization rate.
Answer: c
68. Environmental conditions that affect enzyme function include

a. temperature.
b.pH.
c. CO2 concentration.
d.Both a and b
e. All of the above
Answer: d
69. End products of biosynthetic pathways often act to block the initial step in that
pathway. This phenomenon is called
a. allosteric inhibition.
b.denaturation.
c. branch pathway inhibition.
d.feedback inhibition.
e. binary inhibition.
Answer: d
70. Denatured enzymes are the same as

a. ribozymes.
b.abzymes.
c. isozymes.
d.enzymes that can no longer function.
e. coenzymes.
Answer: d
71. Which of the following is a group of enzymes that are important in allowing
organisms to adapt to changes in their environment?
a. Isozymes
b.Alloenzymes
c. Allosteric enzymes
d.Both a and c
e. All of the above
Answer: d
72. If the temperature of an enzyme-catalyzed reaction is increased from 40°C to 70°C,

the rate of the reaction
a. will increase indefinitely.
b.will decrease immediately.
c. will decrease to zero because the enzyme denatures.
d.will decrease and then increase.
e. cannot be determined without information regarding optimal temperature.
Answer: e
73. When organisms move from one environment to another, they sometimes synthesize
variations of existing enzymes, which are called
a. coenzymes.
b.abzymes.
c. isozymes.
d.effectors.
e. activators.
Answer: c
Fill in the Blank
1. _______ is an enzyme needed to hydrolyze lactose.

Answer: Lactase
Textbook Reference: 8.0 Lactase deficiency, p. 148
2. Cells cannot create energy because _______ cannot be created or destroyed.

Answer: energy
3. The capacity for change is known as _______.
Answer: energy
4. Heat, light, electricity, and motion are all examples of _______ energy.
Answer: kinetic
5. The energy in a system that exists due to position is called _______ energy.
Answer: potential
6. Potential energy can be converted into _______ energy, which does work.
Answer: kinetic
7. The building up of molecules in a living system is known as _______; the breaking

down of molecules in a living system is known as _______.
Answer: anabolism; catabolism
8. The first law of thermodynamics states that _______ is neither created nor
destroyed.
Answer: energy
9. The second law of thermodynamics states that the _______, or disorder, of the
universe is constantly increasing.
Answer: entropy
10. When a drop of ink is added to a beaker of water, the dye molecules become
randomly dispersed throughout the water. This is an example of an increase in
_______.
Answer: entropy
11. If the ΔG of a spontaneous reaction is negative, indicating that the reaction releases
free energy, the reaction is _______.
Answer: exergonic
12. Cells mostly use _______ as an immediate source of energy to drive reactions.
Answer: ATP
13. Enzymes are biological _______.

Answer: catalysts
14. The amount of energy needed to start a reaction is known as the _______ energy.
Answer: activation
15. The enzyme phosphoglucoisomerase catalyzes the conversion of glucose 6-

phosphate to fructose 6-phosphate. The region on phosphoglucoisomerase where
glucose 6-phosphate binds is called the _______.
Answer: active site
16. A change in enzyme shape caused by substrate binding is called _______.

Answer: induced fit
17. Although some enzymes consist entirely of one or more polypeptide chains, others
possess a permanently bound nonprotein portion called a(n) _______.
Answer: prosthetic group
18. Zinc ions that bind to enzymes are called _______.

Answer: cofactors
19. The chemical activities of a living organism are organized into _______ in which
the product of one reaction is the reactant for the next reaction.
Answer: metabolic pathways
20. Variations of enzymes that allow organisms to adapt to changing environments are
termed _______.
Answer: isozymes
21. When an enzyme is heated until its three-dimensional structure is destroyed, the
enzyme is said to be _______.
Answer: denatured
Diagram
1. Which of the following statements about the reaction shown below is true?
a. It is an endergonic reaction.
b.The reactants have less energy than the products.
c. ΔG is negative.
d.The reaction can be reversed without the addition of energy.
e. It is an anabolic reaction.
Answer: c
2.–3. In the diagram below, reactants and products are designated by capital letters;
enzymes are designated by numbers.
2. If enzyme 2 is inactive, which of the following products would be produced from

the metabolic pathway?
a. C
b.D
c. F
d.B
e. G
Answer: d
3. If end product E allosterically inhibits enzyme 1, a buildup of E in the cell will result
in
a. reduced production of G.
b.reduced production of A.
c. increased production of G.
d.increased production of E.
e. increased production of D.
Answer: a
STUDY GUIDE QUESTIONS

(By Jacalyn Newman)
Knowledge and Synthesis

1. ATP is necessary for the conversion of glucose to glucose 6-phosphate. Splitting
ATP into ADP and Pi releases energy into what form used by the cell?
a. Potential
b.Kinetic
c. Entropic
d.Enthalpic
e. Heat
Answer: b. The released energy is available to do work; therefore, it is kinetic
energy. Some energy is lost in the form of entropy, but it will not be used by the cell
to do work.
2. Before ATP is split into ADP and Pi, it holds what type of energy?
a. Potential
b.Kinetic
c. Entropic
d.Enthalpic
e. Physical
Answer: a. Potential energy is energy held within chemical bonds that may be
converted to working kinetic energy.
3. Which of the following statements concerning energy transformations is true?

a. Increases in entropy reduce usable energy.
b.Energy may be created during transformation.
c. Potential energy increases with each transformation.
d.Increases in temperature decrease total amount of energy available.
e. Decreases in entropy reduce usable energy.
Answer: a. Total energy = Free energy + entropy × temperature. Any increase in
entropy is necessarily going to reduce free energy.
4. A reaction has a ΔG of –20 kcal/mol. This reaction is

a. endergonic, and equilibrium is far toward completion.
b.exergonic, and equilibrium is far toward completion.
c. endergonic, and the forward reaction occurs at the same rate as the reverse
reaction.
d.exergonic, and the forward reaction occurs at the same rate as the reverse reaction.
e. of an indeterminate nature according to the information supplied.
Answer: b. A negative ΔG indicates an exergonic reaction with energy being
liberated. A large ΔG indicates that equilibrium lies toward completion.
5. ATP hydrolysis is
a. endergonic.
b.exergonic.
c. chemoautotrophic.
d.anabolic.
e. None of the above
Answer: b. ATP hydrolysis is exergonic, resulting in a ΔG of –7.3 kcal/mol.
6. Enzymes are biological catalysts and function by

a. increasing free energy in a system.
b.lowering activation energy of a reaction.
c. lowering entropy in a system.
d.increasing temperature near a reaction.
e. altering the equilibrium of the reaction.
Answer: b. Enzymes reduce activation energy and speed up reactions.
7. Which of the following contributes to the specificity of enzymes?

a. Each enzyme has a wide range of temperature and pH optima.
b.Each enzyme has an active site that interacts with many substrate.
c. Substrates themselves may alter the active site slightly for optimum catalysis.
d.Enzymes are more active at higher temperatures.
e. All of the above
Answer: d. Enzymes are specific to particular substrates that may actually “adjust”
the fit of the active site. They also function in specific, narrow optimum ranges of
pH and temperature.
8. Coenzymes and cofactors, as well as prosthetic groups, assist enzyme function by

a. stabilizing three-dimensional shape.
b.assisting with the binding of enzyme and substrate.
c. maintaining active sites in an active configuration.
d.reversibly binding to the enzyme to regulate the enzyme’s activity.
e. a, b, and c only
Answer: e. Cofactors, coenzymes, and prosthetic groups assist with the maintenance
of an enzyme’s three-dimensional shape and the conformation of the active
prosthetic groups are permanently bound to the enzyme.
9. Which of the following are characteristics of enzymes?

a. They are consumed by the enzyme-mediated reaction.
b.They are not altered by the enzyme-mediated reaction.
c. They raise activation energy.
d.They can be composed of RNA or proteins.
e. They are only rarely regulated.
Answer: b. Enzymes are not consumed or altered in any way during an enzyme-
mediated reaction, and they function to lower the activation energy of a reaction.
Ribozymes (composed of RNA) are catalysts, but are not true enzymes.
10. Ascorbic acid, found in citrus fruits, acts as an inhibitor to catecholase, the enzyme
responsible for the browning reaction in fruits such as apples, peaches, and pears.
One explanation for the inhibiting function of ascorbic acid could be its similarity, in
terms of size and shape, to catechol, the substrate of the browning reaction. If this
explanation is correct, then this inhibition is most likely an example of _______
inhibition.
a. competitive
b.indirect
c. noncompetitive
d.allosteric
e. feedback
Answer: a
11. Refer to question 10. Suppose further studies indicate that ascorbic acid is not
similar to catechol in size and shape but that the pH of the ascorbic acid solution is
altering the protein folding of catecholase. If this is true, then this inhibition is most
likely an example of
a. competitive inhibition.
b.enzyme denaturation.
c. noncompetitive inhibition.
d.allosteric regulation.
e. feedback inhibition.
Answer: b. Destroying the three-dimensional structure of an enzyme, or denaturing
it, is usually irreversible.
12. Metabolism is organized into pathways that are linked in which of the following
ways?
a. All cellular functions feed into a central pathway.
b.All steps in the pathway are catalyzed by the same enzyme.
c. The product of one step in the pathway functions as the substrate in the next step.
d.Products of the pathway accumulate and are secreted from the cell.
e. Different substrates are acted on by the same enzyme.
Answer: c. Within a given pathway, the products of the preceding step act as
substrates for subsequent steps.
13. Which of the following represents an enzyme-catalyzed reaction? (E = enzyme, P =

product, S = substrate)
a. E + P → E + S
b.E + S → E + P
c. E + S → P
d.E + S → E
e. P + S → E
Answer: b. Substrate is converted to product and the enzyme is unchanged.
14. In the pathway A + B → C + D, enzyme X facilitates the reaction. If compound D

inhibits enzyme X, you would conclude that
a. enzyme X is an allosteric inhibitor of the above reaction.
b.compound D is an allosteric stimulator of the above reaction.
c. compound D is a competitive inhibitor of the above reaction.
d.enzyme X is subject to feedback stimulation.
e. compound D is a coenzyme in the above reaction.
Answer: a. Products of a reaction that inhibit the enzymes via feedback inhibition
are allosteric inhibitors.
15. You are studying a new species never before studied. It lives in acidic pools in
volcanic craters where temperatures often reach 100°C and normally stay above
90°C. You determine that it has a surface enzyme that catalyzes a reaction leading to
its protective coating, and you decide to study this enzyme in the laboratory. Under
what conditions would you most likely find optimal activity of this enzyme?
a. 0°C
b.37°C
c. 55°C
d.95°C
e. 105°C
Answer: d. Enzymes typically work at a maximal rate at a particular temperature or
within a range of temperatures. This optimal temperature tends to be correlated with
the body temperature of the organism.
16. Enzymes alter the

a. ΔG value of the reaction.
b.activation energy of the reaction.
c. equilibrium of the reaction.
d.rate of the reaction.
e. Both a and b
Answer: b. The free energy levels of the reactants and products are not changed by
enzymes. Only the activation energy is altered. See Figure 8.10.
Textbook Reference: 8.3 What Are Enzymes p. 157
17. You fill two containers with identical amounts of reactants A and B and enzymes 1–
4. In the reactions shown below, if product D inhibits enzyme 2 and product F is an
allosteric stimulator of enzyme 1, what will be the final result if you add extra
product D to the second container? (Assume that both containers are given enough
time for the reactions to go to completion.)
a. The concentration of product C will increase and there will be no change in
product F concentration compared to the first container.
b.The concentration of reactants A and B will increase relative to the first container.
c. The concentration of product F will increase in the second container because more
of D is converted back to C.
d.The concentration of products E and F will both increase in the second container,
since D inhibits enzyme 2.
e. The concentration of product F will increase relative to the first container, since
enzyme 2 will have been inhibited from converting as much of C into D.
Answer: e. The addition of more D to the second container will reduce the activity of
Enzyme 2. The pathway from A + B going all the way to F will be the predominant
reaction that takes place, leading to a greater final concentration of F in the second
container. The first container will convert some of C into D, and thus the level of
intermediate E and final product F will be lower than in the second container. (Hint:
Draw a diagram of the experiment.)
18. You are given an unlabeled enzyme and told to add a compound to the container that
will irreversibly bind to the enzyme and increase its function. You ask for
information about the enzyme, but your instructor simply hands you a list of
possible compounds. Based on what you have learned about the enzyme partners
below, which one is the best choice?
a. Coenzyme A
b.Zinc (Zn2+)
c. Flavin
d.ATP
e. NAD
Answer: c. Of the five compounds listed, only one is a prosthetic group, which is
irreversibly bound to its target enzyme.
Textbook Reference: 8.4 How Do Enzymes Work? p. 160, Table 8.1
Application
1. It is estimated that approximately 90 percent of energy that passes between levels in

a food web is “lost” at each level. Explain the first law of thermodynamics and
discuss why this apparent loss of energy does not contradict the law.
Answer: The first law of thermodynamics states that energy cannot be created or
destroyed, but that it may be converted from one form to another. In the transfer
between levels of a food web, approximately 90 percent of the energy is converted
to unusable heat energy. There is a net loss of usable energy during each conversion,
but the total amount of energy (usable and unusable) remains the same.
2. Amylase is a digestive enzyme that breaks down starch and is secreted in the mouth
of humans. Amylase functions well in the mouth but ceases to function once it hits
the acidic stomach environment. Explain why amylase does not function in the
stomach.
Answer: The pH optimum of amylase is approximately 7. At that pH, the protein has
the three-dimensional shape to allow starch to bind to its active site and catalyze its
hydrolysis. When it is at the stomach pH (approximately 2), the protein is denatured,
and its three-dimensional shape and active site are lost; therefore, it can no longer
catalyze the reaction.
3. The ultimate goal of metabolism is to drive ATP synthesis. ATP is considered the
energy currency of the cell. Discuss how ATP couples endergonic and exergonic
reactions and why it is so important in cellular functions.
Answer: The conversion of ATP to ADP and Pi releases approximately 7.3 kcal/mol
of energy. This energy release fuels (endergonic) reactions in the cell. Equilibrium
of the reaction is far to the right and favors the formation of ADP. In the converse,
the formation of ATP from ADP and Pi is energy intensive and can be coupled to
highly exergonic reactions within the cell. Thus, ATP functions as an energy shuttle
between endergonic and exergonic reactions. The small size of the molecule and its
ubiquitousness allow it to be available and move freely within the cell.
4. Figure 8.17 shows the behavior of an allosteric enzyme that has binding sites for a
negative regulator. Describe the behavior of an enzyme with binding sites for a
positive regulator instead of a negative regulator.
Answer: A positive regulator would stabilize the enzyme in its active form. In the
absence of the regulator, the enzyme would alternate between its inactive and active
forms. When it encountered substrate, it would bind it only if it happened to be in its
active form. When bound to the regulator, the enzyme would be fixed in its active
form, and it would bind substrate at a greater rate.
5. Explain how substrate concentration affects the rate of an enzyme-mediated

reaction.
Answer: Increasing substrate concentration will result in an increased rate of
reaction until all available active sites are occupied. At that point, no amount of
substrate increase will increase the rate of reaction (see Figure 8.13).
6. Explain how free energy, total energy, temperature, and entropy are related.
Answer: Total energy = free energy + unusable energy  absolute temperature.
7. Use a graph to explain how temperature affects enzyme activity.

Answer: See Figure 8.21.
8. You decide to purchase a new water heater and start looking at the energy efficiency
ratings. You find one unit that is labeled as 100 percent energy efficient, and the
salesperson says that the more efficient the appliance is, the more money you will
save. However, you don’t trust that the store is providing accurate information, and
you do not buy the product. Was this decision correct?
Answer: The decision was correct. An appliance with 100 percent energy efficiency
is not possible. The second law of thermodynamics indicates that every time energy
is transformed, some is lost in the form of entropy. An appliance with no energy lost
to entropy therefore does not exist.
TEXTBOOK SELF-QUIZ
1. Coenzymes differ from enzymes in that coenzymes are

a. only active outside the cell.
b.polymers of amino acids.
c. smaller molecules, such as vitamins.
d.specific for one reaction.
e. always carriers of high-energy phosphate.
Answer: c
2. Which statement about thermodynamics is true?

a. Free energy is used up in an exergonic reaction.
b.Free energy cannot be used to do work.
c. The total amount of energy can change after a chemical transformation.
d.Free energy can be kinetic but not potential energy.
e. Entropy has a tendency to increase.
Answer: e
3. In a chemical reaction,
a. the rate depends on the value of ΔG.
b.the rate depends on the activation energy.
c. the entropy change depends on the activation energy.
d.the activation energy depends on the value of ΔG.
e. the change in free energy depends on the activation energy.
Answer: b
4. Which statement about enzymes is not true?
a. They usually consist of proteins.
b.They change the rate of the catalyzed reaction.
c. They change the ΔG of the reaction.
d.They are sensitive to heat.
e. They are sensitive to pH.
Answer: c
5. The active site of an enzyme

a. never changes shape.
b.forms no chemical bonds with substrates.
c. determines, by its structure, the specificity of the enzyme.
d.looks like a lump projecting from the surface of the enzyme.
e. changes the ΔG of the reaction.
Answer: c
6. The molecule ATP is

a. a component of most proteins.
b.high in energy because of the presence of adenine.
c. required for many energy-transforming biochemical reactions.
d.a catalyst.
e. used in some exergonic reactions to provide energy.
Answer: c
7. In an enzyme-catalyzed reaction,
a. a substrate does not change.
b.the rate decreases as substrate concentration increases.
c. the enzyme can be permanently changed.
d.strain may be added to a substrate.
e. the rate is not affected by substrate concentration.
Answer: d
8. Which statement about enzyme inhibitors is not true?

a. A competitive inhibitor binds the active site of the enzyme.
b.An allosteric inhibitor binds a site on the active form of the enzyme.
c. A noncompetitive inhibitor binds a site other than the active site.
d.Noncompetitive inhibition cannot be completely overcome by the addition of
more substrate.
e. Competitive inhibition can be completely overcome by the addition of more
substrate.
Answer: b
9. Which statement about the feedback inhibition of enzymes is not true?

a. It is usually exerted through allosteric effects.
b.It is directed at the enzyme that catalyzes the commitment step in a metabolic
pathway.
c. It affects the rate of reaction, not the concentration of enzyme.
d.It acts by permanently modifying the active site.
e. It is an example of reversible inhibition.
Answer: d
10. Which statement about temperature effects is not true?

a. Raising the temperature may reduce the activity of an enzyme.
b.Raising the temperature may increase the activity of an enzyme.
c. Raising the temperature may denature an enzyme.
d.Some enzymes are stable at the boiling point of water.
e. All enzymes have the same optimal temperature.
Answer: e

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What are some of the principles of thermodynamics discussed in the text?

What are some of the principles of thermodynamics discussed in the text?

What is the role of enzymes in metabolic reactions?

What is the role of enzymes in metabolic reactions?

Test File

Chapter 8: Energy, Enzymes, and Metabolism

TEST FILE QUESTIONS

1. Lactose intolerance is due to the

2. Water held back by a dam represents what kind of energy?

3. Which of the following represents potential energy?

6. How does the second law of thermodynamics apply to organisms?

10. A change in free energy is related to a change in

15. Chemical equilibrium

16. If the enzyme phosphohexoisomerase is added to a 0.3 M solution of fructose 6-

17. When ADP gains a phosphate to form ATP,

18. Luciferin and luciferase are added to soft drinks because

21. Phosphorylation of ADP to ATP is endergonic, whereas the hydrolysis of ATP to

22. In glycolysis, the exergonic reaction 1,3-diphosphoglycerate → 3-phosphoglycerate

23. Which of the following statements about ATP is true?

24. An RNA molecule that has enzyme activity is called

25. The rate of a chemical reaction in a cell is the measure of how

26. Knowing the change in free energy (ΔG) of a reaction tells us

27. Which of the following is an example of an exergonic reaction?

28. Which of the following statements about enzymes is false?

29. What is a transition state?

31. Which of the following determines the rate of a reaction?

35. An active site is

36. In some cases, a substrate–enzyme complex is stabilized by

37. The molecules that are acted on by an enzyme are called

39. Which of the following statements about enzymes is true?

41. The enzyme glyceraldehyde 3-phosphate dehydrogenase catalyzes the reaction

43. Binding of substrate to the active site of an enzyme is

44. Which of the following is an enzyme?

45. The presence of a catalyst affects the

46. Enzymes of the acid–base catalysis type contain

48. Enzymes catalyze a reaction by _______ the substrates.

50. In the presence of alcohol dehydrogenase, the rate of reduction of acetaldehyde to

52. Enzymatic reactions can become saturated as substrate concentration increases

53. Competitive inhibitors of enzymes work by

55. How do competitive and noncompetitive enzyme inhibitors differ?

57. A noncompetitive inhibitor inhibits binding of a substrate to an enzyme by

59. An allosteric inhibitor

60. Allosteric inhibitors act by

61. The inhibition of enzyme activity by noncompetitive inhibitors can be reduced

62. The maximum possible rate of an enzyme reaction that is influenced by a

63. Negative feedback in a sequence of chemical reactions involves a chemical that

64. Which of the following statements about allosteric regulators is true?

65. Enzymes are sensitive to

67. Enzymes are highly sensitive to pH and temperature because

68. Environmental conditions that affect enzyme function include

70. Denatured enzymes are the same as

72. If the temperature of an enzyme-catalyzed reaction is increased from 40°C to 70°C,

Fill in the Blank

1. _______ is an enzyme needed to hydrolyze lactose.

2. Cells cannot create energy because _______ cannot be created or destroyed.

7. The building up of molecules in a living system is known as _______; the breaking

13. Enzymes are biological _______.

15. The enzyme phosphoglucoisomerase catalyzes the conversion of glucose 6-