Multiple Choice Questions: Energy and Metabolism

Chapter 06 - Energy and Metabolism
Chapter 06
Energy and Metabolism
Multiple Choice Questions

1. Why do we have storage macromolecules, such as fats, in our bodies?

A. We can break down these macromolecules to provide energy for the endergonic reactions
in our bodies.
B. Human cells can directly capture the energy of sunlight through photosynthesis and store it
as macromolecules such as fats.
C. Macromolecules, such as fats, are a convenient way to store kinetic energy.
D. Breaking down macromolecules, such as fats, is an endergonic process.
Blooms Level: 2. Understand

Gradable: automatic
LO: 06.01.02 Identify the source of energy for the biosphere.
Section: 06.01
Topic: The Flow of Energy in Living Systems

2. Energy is defined as

A. heat.
B. the capacity to do work.
C. change.
D. movement.
Blooms Level: 1. Remember

Gradable: automatic
LO: 06.01.01 Differentiate between kinetic and potential energy.
Section: 06.01

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McGraw-Hill Education.
3. The amount of energy available to do work is called

A. activation energy
B. free energy
C. kinetic energy
D. potential energy

Gradable: automatic
LO: 06.02.02 Relate free energy changes to the outcome of chemical reactions.
Section: 06.02
Topic: The Laws of Thermodynamics and Free Energy

4. The energy needed to destabilize existing chemical bonds and start a chemical reaction is
called
A. activation energy
B. free energy
C. kinetic energy
D. potential energy

Gradable: automatic
LO: 06.02.03 Contrast the course of a reaction with and without an enzyme catalyst.
Section: 06.02

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5. Based on the graph, what are the optimal temperatures for the human enzyme and
hotsprings prokaryote enzyme?

A. The optimal temperature for the human enzyme is 30 degrees C. The optimal temperature
for the hotsprings prokaryote enzyme is 60 degrees C.
B. The optimal temperature for the human enzyme is 40 degrees C. The optimal temperature
C. The optimal temperature for the human enzyme is 46 degrees C. The optimal temperature
D. The optimal temperature for the human enzyme is 35 degrees C. The optimal temperature
Fat molecules have many bonds, and breaking those bonds provides energy, as discussed in
the text. Therefore, these macromolecules are a convenient way of storing energy, and stored
energy is considered potential energy. Human cells cannot perform photosynthesis. Breaking
down macromolecules is an exergonic process.
Blooms Level: 3. Apply

Gradable: automatic
LO: 06.04.03 List the factors that influence the rate of enzyme-catalyzed reactions.
Section: 06.04
Topic: Enzymes: Biological Catalysts

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6. A drug binds to the active site of an enzyme. If it is bound to the active site of the enzyme,
it prevents substrate binding. This drug would be considered a
A. noncompetitive inhibitor.
B. allosteric inhibitor.
C. allosteric activator.
D. competitive inhibitor.

Gradable: automatic
Section: 06.04

7. A particular reaction has a negative delta G. However, this reaction takes many years to
proceed in the absence of enzyme. Why is this the case?
A. This reaction does not obey the second law of thermodynamics
B. This reaction does not proceed spontaneously
C. The initial free energy of the reactants is much less than the final free energy of the
products
D. A certain amount of activation energy is required for the reaction to proceed
Reactions with a negative delta G proceed spontaneously, but not instantaneously. They need
a certain amount of activation energy to proceed.

Gradable: automatic
Section: 06.02

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8. A molecule that closely resembles the shape of a substrate for an enzyme would most
likely serve as a
A. noncompetitive inhibitor.
B. allosteric inhibitor.
C. competitive inhibitor.
D. allosteric activator.
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Clarify Question
What is the key concept addressed by the question?

· The question asks for you to identify the most likely function of a molecule that
closely resembles the shape of the substrate.
What type of thinking is required?
· You are being asked to take what you already know aboutenzymes and molecular
shape and apply your understanding to determine which function is most likely.
Gather Content
What do you already know about enzymes and inhibition? What other information is
related to the question?
· To solve this problem you’ll need to apply what you know about the different ways
thatenzyme inhibition can occur and molecular shape and determine the most likely role for a
molecule with similar shape to the substrate. Recall that enzyme function can be inhibited
competitively, noncompetitively, and allosterically. Why is the shape of substrate molecules
important, and what possible role could a molecule that mimics the substrate’s shape play in
enzyme function?
Choose Answer
Do you have all the information needed to answer the question?

· At this point you should have everything you need to answer the question. Remember
that enzyme function can be competitively, noncompetitively, and allosterically inhibited.
What are the key differences between these methods?
· Let’s consider noncompetitive inhibition first. Noncompetitive means molecules are
not trying to outcompete substrate molecules for the enzyme’s active site. As such, the shape
of noncompetitive inhibitors is unlikely to closely match the shape of the substrate molecule.
· Likewise, allosteric inhibitors, which are noncompetitive by definition, bind at a site
remote from the active site to inhibit enzyme function. Again, the shape of allosteric inhibitor
is unlikely to closely resemble the shape of a substrate molecule because it doesn’t need to
function as a mimic.
· That leaves competitive inhibition as the only viable option, but why does that make
sense? In order to compete for the active site of an enzyme, an inhibitor needs to be able to fit
into the same space as a substrate molecule. This means the inhibitor must closely resemble
the substrate’s shape in order to inhibit enzyme function.
Reflect on Process
Did your problem-solving process lead you to the correct answer? If not, where did the
process break down or lead you astray? How can you revise your approach to produce a
more desirable result?
· Answering this question correctly depended on your ability to use your understanding
of enzymes and inhibitionto determine what the most likely function would be for a molecule
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closely resembling the substrate.

· If you got an incorrect answer, did yourecallthe ways in whichenzymes can be
inhibited? Did you remember that noncompetitive and allosteric inhibition don’t involve the
active site, and therefore their shape would have no need to resemble the substrate’s shape?
Were you able to rationalize competitive inhibition considering the shape of the inhibitor
needed to resemble the substrate?

Gradable: automatic
Section: 06.04

9. Oxidation and reduction reactions are chemical processes that result in a gain or loss of:
A. atoms.
B. neutrons.
C. electrons.
D. molecules.
E. protons.

Gradable: automatic
LO: 06.01.03 Contrast oxidation and reduction reactions.
Section: 06.01

10. The synthesis of sugar molecules through the process of photosynthesis requires energy
absorbed from sunlight. Bearing this in mind, what kind of reaction is photosynthesis?
A. exergonic
B. endergonic
C. catabolic
D. feedback
Because this process requires energy input, it is an endergonic reaction.

Gradable: automatic
Section: 06.02

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11. A particular chemical reaction is exergonic. What can you say about the relationship
between the reactants and the products in this exergonic reaction?
A. The reactants have more free energy than the products
B. The reactants are likely more disordered and the products are likely more ordered
C. The reactants cannot spontaneously react to generate the products
D. The reactants likely have lower enthalpy than the products
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Clarify Question

· The question asks for you to determine the relationship between reactants and
products in an exergonic reaction.
· You are being asked to take what you already know about enzymes and free energy
and apply your understanding to determine the energy characteristics of an exergonic
reaction.
Gather Content
What do you already know about the energy associated with reactants and products in
reactions? What other information is related to the question?
· To solve this problem you’ll need to apply what you know about the free energy
associated with reactants and products and determine how it is associated with exergonic and
endergonic reactions. What free energy characteristics determine whether or not a reaction is
exergonic (spontaneous) or endergonic (nonspontaneous)?
Choose Answer

· Recall that the change in free energy in enzyme-based reactions is classified as
exergonic or endergonic. Exergonic reactions have a negative delta G and are spontaneous,
whereas endergonic reactions have a positive delta G and are nonspontaneous. Remember
also that nonspontaneous reactions can be made to work if there is sufficient investment of
energy (e.g. coupled reactions).
· The only way to be able to meet the criteria for an exergonic reaction is to choose an
answer that will create a negative delta G. In practical terms, that means the free energy of the
reactants must be higher than the free energy of the products. All other answer choices are
implausible because they violate that basic energy assumption.
Reflect on Process
of reactions and free energy to determine the energy characteristics for an exergonic reaction.
· If you got an incorrect answer, did you remember that reactions can be classified as
exergonic and endergonic based on whether or not their change in free energy is positive or
negative? Did you remember that exergonic reactions have a negative delta G and endergonic
reactions have a positive delta G? Were you able to infer from this information that the
reactant must have more free energy than the products in order to obtain a negative delta G?
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Gradable: automatic
Section: 06.02

12. Kinases are enzymes that can phosphorylate (transfer phosphate groups
onto) macromolecules such as proteins. A particular kinase, Kinase 1 is known to promote cell
division. It promotes cell division by phosphorylating Protein X. Phosphorylation of Protein
X activates Protein X. Once activated, Protein X stimulates the production of other proteins
such as Protein Y and Z that directly promote cell division. In order to function, Kinase 1
requires the presence of Metal A. However, in the presence of Protein A, Kinase 1 is
nonfunctional. From the description, what is considered the substrate of Kinase 1?
A. Protein X
B. Protein Y
C. Protein Z
D. Metal A
E. Protein A
Since kinases function to phosphorylate macromolecules, and Kinase 1 phosphorylates

Protein X, Protein X is considered a substrate of Kinase 1.

Gradable: automatic
LO: 06.04.02 Explain how enzymes bind to their substrates.
Section: 06.04

6-12
13. Kinases are enzymes that can phosphorylate (transfer phosphate groups
onto) macromolecules such as proteins. A particular kinase, Kinase 1 is known to promote
cell division. It promotes cell division by phosphorylating Protein X. Phosphorylation of
Protein X activates Protein X. Once activated, Protein X stimulates the production of other
proteins such as Protein Y and Z that directly promote cell division. In order to function,
Kinase 1 requires the presence of Metal A. However, in the presence of Protein A, Kinase 1 is
nonfunctional. From the description, what is considered a cofactor of Kinase 1?
A. Protein X
B. Protein Y
C. Protein Z
D. Metal A
E. Protein A
Metal A is required for Kinase 1 to function, and thus is a cofactor for this kinase.

Gradable: automatic
Section: 06.04

14. Hexokinase is an enzyme that binds specifically to glucose and converts it into glucose 6-
phosphate. The activity of hexokinase is suppressed by glucose 6-phosphate, which binds to
hexokinase at a location that is distinct from the active site. This is an example of.
A. feedback inhibition.
B. competitive inhibition.
C. cofactor binding.
D. allosteric activation.
In this case, the product of the reaction, glucose 6-phosphate, is feeding back to inhibit the
enzyme that catalyzes the reaction, hexokinase. As a result, this is an example of feedback
inhibition.

Gradable: automatic
Section: 06.04

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15. The organic non-protein components that aid in enzyme functioning are called
A. reactants.
B. cofactors.
C. coenzymes.
D. substrates.
E. products.

Gradable: automatic
Section: 06.04

16. The inorganic non-protein components that participate in enzyme catalysis are known as
A. coenzymes.
B. cofactors.
C. products.
D. substrates.
E. reactants.

Gradable: automatic
Section: 06.04

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17. Many metabolic pathways are ultimately concerned with ATP; either with the generation
of ATP, or with the requirement of ATP for that pathway to function. Why is ATP so
important to metabolism?
A. Hydrolysis of ATP is used to drive exergonic reactions
B. Hydrolysis of the bond between adenine and ribose in ATP is commonly used to release
energy that can be used to drive other cellular reactions
C. The phosphate groups of ATP are held together by unstable bonds that can be broken to
release energy
D. ATP is a protein that serves as the energy currency of cells
ATP does serve as the energy currency of cells, by storing energy in its triphosphate group.
By cleaving the unstable bonds holding the phosphates together in the ATP molecule, energy
can be released to drive endergonic reactions. ATP can also be used as a building block for
RNA molecules. It is not a protein.

Gradable: automatic
LO: 06.03.02 Distinguish which bonds in ATP are high energy.
Section: 06.03
Topic: ATP: The Energy Currency of Cells

18. The chemistry of living systems representing all chemical reactions is called
A. catabolism.
B. anabolism.
C. metabolism.
D. enzymology.
E. thermodynamics.

Gradable: automatic
LO: 06.05.01 Explain the kinds of reactions that make up metabolism.
Section: 06.05
Topic: Metabolism: The Chemical Description of Cell Function

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19. A calorie is the commonly used unit of chemical energy. It is also the unit of
A. light.
B. magnetism.
C. sound.
D. heat.
E. radioactivity.

Gradable: automatic
Section: 06.01

20. The term oxidation is derived from the name of the element oxygen. This is reasonable,
because oxygen
A. attracts electrons very strongly.
B. can be oxidized by accepting electrons.
C. contains more electrons than are needed.
D. passes electrons to many other types of molecules.

Gradable: automatic
Section: 06.01

21. When an atom or molecule gains one or more electrons, it is said to be:
A. energized.
B. oxidized.
C. polarized.
D. reduced.

Gradable: automatic
Section: 06.01

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22. The ultimate source of energy for humans comes from what source?
A. The sun
B. Plants
C. Water
D. Air
E. Animals

Gradable: automatic
LO: 06.01.02 Identify the source of energy for the biosphere.
Section: 06.01

23. Glucose is broken down through cellular respiration, which involves a large number of
chemical reactions. At the end of the cellular respiration process, a large number of ATP
molecules are generated, but yet, not all of the possible energy that is contained in a molecule
of glucose can be harnessed through these chemical reactions to generate ATP. In other
words, during cellular respiration, not all of the energy that is contained in a molecule of
glucose is converted into the energy stored in ATP. What happens to the remaining energy?
A. It is destroyed
B. It is used to drive exergonic reactions
C. It is donated to molecules in the cellular respiration process to reduce them
D. It is lost as heat
It is lost as heat. In fact, this is one of the ways we maintain our body temperature.

Gradable: automatic
LO: 06.02.01 Explain the laws of thermodynamics.
Section: 06.02

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24. The Law of Thermodynamics that states that energy cannot be created or destroyed is:
A. The First Law of Thermodynamics
B. The Second Law of Thermodynamics
C. The Third Law of Thermodynamics
D. The Fourth Law of Thermodynamics

Gradable: automatic
Section: 06.02

25. The Law of Thermodynamics that states that increases in entropy are favored is:
A. The First Law of Thermodynamics
B. The Second Law of Thermodynamics
C. The Third Law of Thermodynamics
D. The Fourth Law of Thermodynamics

Gradable: automatic
Section: 06.02

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26. A current problem in modern medicine is the development of drug resistance mutations.
This occurs when a mutation arises in a disease-causing microbe making it resistant to a drug
and thus rendering the drug useless in treating a specific disease. Many useful drugs are
competitive inhibitors of specific enzymes, and the drug-resistance mutations prevent the
binding of the drug. These types of mutations, in addition to preventing competitive inhibitor
binding, can also sometimes reduce the activity of the enzyme. Why is that the case? rev:
01_20_2015_QC_CS-4567
A. Binding to the competitive inhibitor is essential for the function of the enzyme
B. These mutations most likely affect an allosteric site on the enzyme
C. These mutations lower the activation energy of the reaction catalyzed by the enzyme
D. These mutations most likely change the shape of the active site of the enzyme
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Clarify Question

· The question asks you ascertain how drug resistance development in bacteria is related
to reduced enzyme activity.
· You are being asked to break down, or analyze, a possible means by which drug
resistance in bacteria might work to reduce enzyme activity.
Gather Content
What do you already know about enzymes and how their activity is regulated? How does
this drug affect enzyme activity under normal circumstances? What other information is
· Remember that the activity of an enzyme is directly related to its structure and
function. Recall that there are several structural elements of an enzyme that affect its function;
these include the active site and the allosteric site. These structural elements as well as
inhibitors influence an enzyme’s ability to facilitate reactions. The question also indicates that
the drug acts as a competitive inhibitor of the enzyme. Considering the structure and function
of enyzmes, which most directly affected by bacterial drug resistance that reduces enzyme
activity?
Choose Answer
Do you have all necessary information to analyze how drug resistance would reduce
enzyme activity?
· The first major clue in this question is that the drug is a competitive inhibitor of the
enzyme, and that microbial changes in the enzyme’s structure render the drug ineffective.
Recall that competitive inhibitors mimic the shape of a substrate, which binds to the active
site. This information implies that the shape of the drug was a close match to the substrate in
order to be competitive inhibitor in the first place.
· A second major clue is the mutation in the bacterium that also renders the drug
ineffective.
· These two lines of evidence imply that the active site of the enzyme must be directly
involved, since neither the allosteric site nor the activation energy of the enzyme would be
affected.
Reflect on Process
· This question asked you to analyze possible reasons for why a previously-effective
drug that works as a competitive inhibitor is rendered ineffective by bacterial mutation.
· If you got the answer correct, well done! If you got an incorrect answer, were you able
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to break down the structural elements of the enzyme into the active and allosteric sites? Were
you able to correlate the two lines of evidence of the drug being a competitive inhibitor and
the bacterial mutation eliminating drug effectiveness? Were you able to infer from this
evidence that the active site was the most likely aspect of the enzyme to be affected?
Blooms Level: 4. Analyze

Gradable: automatic
Section: 06.04
Topic: Metabolism

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27. Tacrolimus (FK-506) is a drug that inhibits an enzyme called calcineurin. Calcineurin is
a protein phosphatase. This is an enzyme that dephosphorylates (removes phosphate groups)
from proteins. When added to cells, tacrolimus can inhibit the dephosphorylation of a protein
called NFAT, but it cannot prevent the dephosphorylation of a protein called CDK1. What is
the most likely explanation for this finding?
A. Calcineurin requires an additional cofactor to dephosphorylate NFAT
B. NFAT is a substrate of calcineurin, but CDK1 is not
C. Tacrolimus is a competitive inhibitor of calcineurin for NFAT and CDK11
D. Tacrolimus changes the optimum pH for calcineurin
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Clarify Question

· The question asks you determine the likely explanation for why the drug tacrolimus
works in cells to inhibit the enzyme calcineurin, prevent dephosphorylation of NFAT, and
maintain phosphorylation of CDK1.
· You are being asked to break down, or analyze, a possible means by which the drug
tacrolimus works on calcineurin phosphatase enzyme.
Gather Content
What do you already know about phosphates and enzymestructure? What other
information is related to the question?
· Since calcineurin is an enzyme, that means it works to convert substrates to products –
just like any other enzyme. In the case of this enzyme, calcineurin dephosphorylates other
proteins. The trick to answering this question correctly is to try and decipher how NFAT and
CDK1 relate to calcineurin.
· Let’s consider the options. How would calcineurin function if NFAT were a cofactor?
A substrate? How might tacrolimus work if it were a competitive inhibitor of calcineurin? Is it
possible for tacrolimus to change the operating pH of calcineurin? If you take it one step at a
time, what is the likely role of calcineurin on NFAT and CDK1?
Choose Answer
6-24
Do you have all necessary information to analyze how tacrolimus works on NFAT and
CDK1?
· It is unlikely that tacrolimus would affect calcineurin’spH.Enyzmes operate in very
specific pH ranges and if tacrolimus affected pH, other enzymes besides calcineurin would
also be affected.
· The question mentions nothing about any cofactors needed for calcineurin to
dephosphorylate NFAT.
· If tacrolimus were a competitive inhibitor of calcineurin, it would interact with the
enzyme as a substrate but prevent calcineurin’sdephosphorylation activity, leading to greater
phosphorylation of NFAT and CDK1. The question indicates that tacrolimus acts to prevent
dephosphorylation of NFAT but not CDK1, so that answer is not plausible.
· That leaves NFAT as a substrate of calcineurin, which makes sense when you consider
that adding tacrolimus prevents NFAT being dephosphorylated by calcineurin. CDK1 is
unaffected, as indicated in the question.
Reflect on Process
6-25
· This question asked you to determine the likely explanation for relationships between
calcineurin, NFAT, and CDK1 proteins based on tacrolimus treatment.
· If you got the answer correct, good job! If you got an incorrect answer, were you able
to decipher that tacrolimus resulted in less calcineurin activity and therefore less NFAT
dephosphorylation? Were you able to correlate the activity of calcineurin and NFAT together?
Were you infer that their relationship would only be possible if NFAT were a substrate for
calcineurin?

Gradable: automatic
LO: 06.04.01 Discuss the specificity of enzymes.
Section: 06.04

28. RNA molecules that also act as enzymes are given the name
A. ribozymes
B. cofactors
C. coenzymes
D. allosteric enzymes

Gradable: automatic
Section: 06.04

29. In an enzyme-catalyzed reaction, the reactant is called the

A. coenzyme
B. catalyst
C. substrate
D. product

Gradable: automatic
Section: 06.04

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30. When the substrate is bound to the enzyme, the shape of the enzyme may change slightly,
leading to
A. an induced fit
B. a great range of possible catalytic activities
C. a greater supply of activation energy
D. more permanent binding through intimate total contact
E. more possible products of the reaction

Gradable: automatic
Section: 06.04

31. In order to reuse an enzyme after the conclusion of an enzyme catalyzed reaction, what
must occur?
A. the enzyme has to be resynthesized
B. the enzyme has to separate itself from the product
C. changes into an active form
D. the enzyme has to decrease entropy

Gradable: automatic
Section: 06.04

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32. You are working with a specific enzyme-catalyzed reaction in the lab. You are a very
careful experimentalist, and as a result, at the beginning of each of your experiments, you
measure the temperature in the lab. On days 1 through 5, the temperature in the lab was 20oC.
Today is day 6 of your experiment, and the temperature in the lab is 30oC. How do you
predict that this will alter the rate of your enzyme-catalyzed reaction?
A. It will decrease the rate
B. It will increase the rate
C. It could possibly increase or decrease the rate
D. it will not affect the rate
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Clarify Question

· The question asks you predict what effect temperature change will have on the rate of
an enzyme-catalyzed reaction.
· You are being asked to weigh and judge, or evaluate, which prediction is most
plausible from a given change in environmental temperature.
Gather Content
What do you already know about enzyme rates and temperature? What other information
is related to the question?
· Remember that temperature affects protein structure and function, and as such can
influence enzyme rate of reaction because enzymes are proteins. The real question here is to
predict how a 10 degree temperature change might affect enzyme reaction rate.
Choose Answer
Do you have all necessary information to make a judgment?

· Recall that enzyme protein structure and function operates best within a relatively
narrow window. Therefore, enzyme reaction rates will fluctuate, depending on the degree of
temperature change.
· The enzyme rates could increase if the 10 degree temperature increase brings the
enzyme closer to its optimal temperature. Conversely, enzyme reaction rates could decrease if
the optimal temperature is closer to the 20 degree room temperature. Without more
information, it is impossible to predict how exactly the enzyme rates will change, so the most
acceptable prediction is to say that enzyme reaction rates could increase or decrease.
Reflect on Process
· This question asked you to evaluate by predicting the effects of environmental
temperature on enzyme reaction rates.
· If you got the answer correct, good job! If you got an incorrect answer, did you
remember that enzymes are proteins, and that temperature affects protein structure and
function? Did you recall that enzymes operate best at an optimal temperature? Were you able
to determine that enzyme rate could increase or decrease due to the 10 degree environmental
temperature change?
6-29
Blooms Level: 5. Evaluate

Gradable: automatic
Section: 06.04

33. Metabolic reactions fall under two general categories: anabolic and catabolic. What type
of chemical reactions are these two classes of metabolic reactions?
A. Anabolic reactions are exergonic reactions, whereas catabolic reactions are endergonic.
B. Both anabolic and catabolic reactions are exergonic.
C. Both anabolic and catabolic reactions are endergonic.
D. Anabolic reactions are endergonic reactions, whereas catabolic reactions are exergonic.

Gradable: automatic
LO: 06.05.01 Explain the kinds of reactions that make up metabolism.
Section: 06.05

34. Under standard conditions, ATP can release for every molecule converted to ADP
A. less than 1 cal of energy.
B. 1 to 2 cal of energy.
C. 7.3 Kcal of energy.
D. different amounts of energy depending on the cell.

Gradable: automatic
LO: 06.03.01 Describe the role of ATP in short-term energy storage.
Section: 06.03

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35. Glucose is converted into glucose 6-phosphate by hexokinase. Glucose 6-phosphate then
serves as the substrate for the enzyme phosphoglucose isomerase, which converts this reactant
into fructose 6-phosphate. Fructose 6-phosphate serves as the substrate for
phosphofructokinase, which converts fructose 6-phosphate into fructose 1,6-bisphosphate.
Based on the information provided, this is an example of what?
A. Feedback inhibition
B. Allosteric regulation
C. A metabolic pathway
D. Enzyme inhibition

Gradable: automatic
LO: 06.05.02 Discuss what is meant by a metabolic pathway.
Section: 06.05

36. In an experiment described in a chemistry lab book, the directions state that after mixing
two chemicals (A and B) and waiting 5 minutes that A will be oxidized. This means that:
A. chemical A has lost electrons to chemical B.
B. chemical A has gained electrons from chemical B.
C. chemical A has gained energy in the form of heat from chemical B.
D. chemical A has lost energy in the form of heat to chemical B.
E. chemical A has reacted with oxygen.

Gradable: automatic
Section: 06.01

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37. In a chemical reaction, glyceraldehyde-3-phosphate + NAD+ yields 1,3-

bisphosphoglycerate + NADH. In this reaction, what happened to NAD+?
A. It was oxidized to form NADH
B. It was reduced to form NADH
C. It was activated to form NADH
D. it served as an enzyme to catalyze the reaction, and at the end of the reaction formed
NADH
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Clarify Question

· The question asks you to determine what happens to NAD+ during a chemical
reaction.
· You are being asked to break down, or analyze, the chemical reaction to determine
what happens to NAD+.
Gather Content
What do you already know about oxidation and reduction chemical reactions? What other
· Remember that many chemical processes participate in oxidation and reduction
(redox) reactions. Oxidation reactions occur when electrons are liberated from a molecule
whereas reduction reactions occur when electrons are added to a molecule. Reduction is
frequently associated with addition of hydrogen atoms as well.
· As you may remember, redox reactions are quite common in biochemical pathways
such as the reactions described in the question. Given what you know about the participants in
redox reactions, what happens to NAD+ when it becomes NADH?
Choose Answer
Do you have all the information needed to determine the correct answer?
· Redox reactions involve one molecule becoming oxidized and another molecule
becoming reduced via the removal and addition of electrons, respectively.
· NAD+ is a molecular acceptor of electrons, and is therefore an oxidized molecule.
The question indicates that NADH is a product of the reaction. So what is the relationship
between NAD+ and NADH?
· When NAD+ accepts electrons, it becomes reduced. The reduced form of NAD+ is
therefore NADH.
Reflect on Process
· This question asked you to determine what happens to NAD+ in the reaction.
· If you got the answer correct, good work! If you got an incorrect answer, did you
remember how redox reactionsoccur? Were you able to identify which molecules participated
in redox reactions? Were you able to discover what happened to NAD+ when it became
NADH?
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Gradable: automatic
Section: 06.01

6-34
38. In a chemical reaction, 1,3-bisphosphoglycerate + ADP yields 3-phosphoglycerate plus

ATP. What is the delta G for this reaction?
A. Greater than zero.
B. Less than zero.
C. Equal to zero.
D. Cannot be determined
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Clarify Question

· The question asks for you to determine the free energy characteristics for a chemical
reaction.
· You are being asked to take what you already know about enzymes and free energy
and apply your understanding to determine the energy characteristics of the enzyme-based
reaction.
Gather Content
What do you already know about free energy in enzymatic reactions? What other
· To solve this problem you’ll need to apply what you know about free energy and how
it is associated with different types of enzyme reactions. What free energy characteristics
determine whether a reaction will occur or not?
· What clues does the question give you about delta G? Does the reaction require the
breakdown of ATP or produce ATP? What types of reaction require ATP hydrolysis in order to
run?
Choose Answer

· Recall that the change in free energy in an enzyme-based reaction is classified as
exergonic or endergonic. Exergonic reactions have a negative delta G and are spontaneous,
whereas endergonic reactions have a positive delta G and are nonspontaneous. Remember
also that nonspontaneous reactions can be made to work if there is sufficient investment of
energy (e.g. coupled reactions).
· Since the question says nothing about the need to invest energy such as ATP, that is
one clue that the reaction is exergonic and has a negative delta G. Another clue is the reaction
shows that ADP is converted to ATP rather than the other way around. The lack of ATP
hydrolysis and coupling to an endergonic reaction indicates that the reaction must not have a
positive delta G, which would indicate an endergonic reaction. Clearly, an energy conversion
of some kind has occurred, so delta G definitely does change. The only suitable option left
would be a negative delta G, which is corroborated by both the clues and the process of
elimination.
Reflect on Process
of enzymes and free energy to determine what the free energy change would be for the
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reaction.
· If you got an incorrect answer, did you remember that enzyme reactions can be
classified as exergonic and endergonic based on whether or not their change in free energy is
positive or negative? Did you remember that exergonic reactions have a negative delta G and
endergonic reactions have a positive delta G? Were you able to see that ADP eventually
formed ATP and infer that the reaction would have to be exergonic and therefore have a
negative delta G?

Gradable: automatic
Section: 06.02

6-38
39. For a particular chemical reaction, the enthalpy of the reactants is -400 kJ. The enthalpy
of the products is -390 kJ. The entropy of the reactants is 0.2 kJ/K. The entropy of the
products is 0.3 kJ/K. The temperature of the reaction is 25 degrees Celsius. What can you
conclude about this reaction?
A. It is exergonic
B. It is endergonic
C. it is a redox reaction
D. It is being catalyzed by an enzyme
6-39
Clarify Question

· The question asks you to draw a conclusion about a reaction given different energy
parameters of reactants and products.
· You are being asked to dissect, or analyze, several energy parameters of a reaction in
order to arrive at a conclusion.
Gather Content
What do you already know aboutenergy of reactants and products in a reaction? What
other information is related to the question?
· Remember that the total energy (enthalpy or H) in a chemical system is equal to the
amount of free energy (G) minus the amount of disorder (entropy) at a particular temperature
(T, in Kelvin). Thus, H = G – TS.
· Recall also that delta G equals the difference in energy level from the beginning to the
end of the reaction, such that delta G = delta H – T(delta S). Consider also that reactions that
have a negative delta G are considered to be exergonic (spontaneous), whereas positive delta
G reactions are endergonic (nonspontaneous).
· How is the overall delta G of a reaction determine once you have values for total
energy (enthalpy) and wasted energy (entropy)?
Choose Answer
Do you have all the information needed to make a determination about the change in free
energy?
· Recall that delta G refers to the amount of energy that changes from the beginning to
the end of the reaction, and is equal to the total change in enthalpy (delta H) minus the
product of temperature (T, in Kelvin) and disorder (S).
· Let’s unpack this solution by first comparing the total energy between products and
reactants. If you compare the enthalpy (total energy) of the products and reactants, you will
find the change in enthalpy is -390kJ –(-400kJ), which equals 10kJ.
· Next let’s determine the disorder component, which is the product of entropy and
temperature in Kelvin. Change in entropy is 0.3kJ/K – 0.2kJ/K and equals 0.1 kJ/K. The
temperature in Kelvin is 25 degrees Celsius + 273K and equals 298K.
· Finally, the change in free energy is determined by change in enthalpy minus the
disorder component. Thus, delta G = (10-(298*0.1)), which equals (10-29.8), which produces
a final answer of -19.8. Since the change in free energy is negative for this reaction, it is
exergonic. Note that it cannot be concluded from the description whether this is a redox
reaction, or whether it is being catalyzed by an enzyme.
Reflect on Process
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· This question asked you to analyze energy characteristics for a reaction to determine
whether it is exergonic, endergonic, redox, or enzyme-catalyzed.
· If you got the answer correct, well done! This was a more challenging problem to
solve.If you got an incorrect answer, did you recall how delta G is different between
exergonic and endergonic reactions? Were you able to calculate the change in free energy
based on the information provided? Based on that information, were you able to show the
reaction had a negative delta Gand based on that must be exergonic?

Gradable: automatic
Section: 06.02

40. Does ADP contain the capacity to provide energy for the cell?
A. No. ADP does not contain any bonds that can be broken to provide energy for the cell.
B. Yes. ADP has the same capacity to provide energy for the cell as ATP.
C. Yes. Cleaving the bond between the ribose sugar and the two phosphate groups can
provide energy for the cell.
D. Yes. Cleaving the bond between the terminal phosphate and the phosphate attached to the
ribose sugar can provide energy for the cell.

Gradable: automatic
LO: 06.03.02 Distinguish which bonds in ATP are high energy.
Section: 06.03

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41. AMP-activated protein kinase (AMPK) is an enzyme that is activated by high levels of
AMP in cells. If levels of AMP are high in cells, that means that levels of ATP are low. Once
active, AMPK activates catabolic pathways and inhibits anabolic pathways in the cell. Why
do you think that is the case? Choose the answer that best explains the role of AMPK.
A. High levels of AMP indicate that there is a high amount of energy stored in the cell, thus
activating catabolic pathways and inhibiting anabolic pathways are mechanisms to use stored
energy.
B. By inhibiting anabolic pathways, AMPK provides a mechanism to generate heat for the
cell, which is important if AMP levels are high in the cell.
C. By activating catabolic pathways, AMPK provides a mechanism to activate exergonic
pathways, which is important if AMP levels are high in the cell.
D. Activating catabolic pathways and inhibiting anabolic pathways will ultimately lead to
higher consumption of ATP, which is important if AMP levels are high in the cell.
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Clarify Question

· The question asks you to determine the role of AMPK in balancing catabolic and
anabolic pathways in cells.
· You are being asked to dissect, or analyze, a scenario to ascertain the role of AMPK in
cells.
Gather Content
What do you already know about AMP, ADP, and ATP in cells? What other information is
· Remember that ATP is the energy currency of the cell. High levels of ATP indicate the
cell is fully powered and has the energy reserves it needs to conduct cellular work. Recall also
that ADP and AMP are lower-level and lowest-level energy molecules, respectively.
· If the cell is in an energy deficit, which molecule will be most prevalent: ATP, ADP, or
AMP?
Choose Answer
Do you have all the information needed to make a determination about the change in free
energy?
· If AMP levels are high in the cell, this indicates that energy levels in the cell are low.
This in turn means that the cell would have lower levels of ATP, the high-energy currency of
the cell.
· Recall that AMP can be converted to ADP and then to ATP by adding inorganic
phosphate. When energy levels are low (AMP), the cell needs to generate more high energy
molecules (ATP). This requires the cell to turn on energy-generating exergonic pathways and
turn offendergonic pathways that require energy. Since reactions that break chemical bonds in
molecules are required to capture stored energy and generate ATP, and reactions that require
energy to build molecules are less needed, AMPK will most likely activate catabolic pathways
and inhibit anabolic pathways.
Reflect on Process
· This question asked you to analyze the most likely role of AMPK in cells when AMP
levels are high and ATP levels are low.
· If you got the answer correct, congratulations! If you got an incorrect answer, were
you able to correlate AMP levels with low energy and ATP levels with high energy in the cell?
Were you able to determine that catabolic reactions are required to generate ATP and anabolic
reactions require ATP? Were you able to connect the two ideas together to determine
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that high AMP levels would lead to increased catabolic (exergonic) and decreased anabolic
(endergonic) reactions?

Gradable: automatic
LO: 06.03.01 Describe the role of ATP in short-term energy storage.
Section: 06.03

42. You are studying an enzyme-catalyzed reaction that induces a particular cellular activity
in the lab. If you wanted to slow down that particular cellular activity by controlling the
enzyme, what could you do?
A. Decrease the temperature of the incubator where the cells are growing
B. Increase the pH of the media the cells are growing in to the optimum pH
C. Add cofactors to the media the cells are growing in
D. Add an allosteric activator to the cells
Decreasing the temperature could work to slow down the reaction. All of these other choices
would either increase or maintain the rate of the reaction.

Gradable: automatic
Section: 06.04

6-46
43. A new antibiotic has been developed that inhibits the activity of an enzyme by
competitive inhibition. What effect will this have on the activation energy of the enzyme-
catalyzed reaction?
A. The activation energy required for the reaction in the presence of the antibiotic would be
greater than the activation energy required in the absence of the antibiotic
B. The activation energy required for the reaction in the presence of the antibiotic would be
less than the activation energy required in the absence of the antibiotic
C. The activation energy required for the reaction in the presence of the antibiotic will be the
same as the activation energy required in the absence of the antibiotic
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Clarify Question

· The question asks you ascertain how an antibiotic that competitively inhibits an
enzyme will affect the enzyme’s activation energy.
· You are being asked to break down, or analyze, how a competitive inhibitor antibiotic
will influence an enzyme’s activation energy.
Gather Content
What do you already know about enzymes and activation energy? What factors influence
activation energy? What other information is related to the question?
· Remember that the activity of an enzyme is directly related to its structure and
function. Recall that there are several structural elements of an enzyme that affect its function;
these include the active site, which can be regulated by competitive inhibitors.
· The question indicates that the antibiotic acts as a competitive inhibitor of the enzyme.
Considering the structure and function of enyzmes and how competitive inhibitors work, how
might the activation energy of the reaction be affected?
Choose Answer
Do you have all necessary information to analyze how the antibiotic might influence
activation energy?
· Recall that competitive inhibitors bind to the active site of the enzyme, which
precludes the substrate binding to the same location. Thus, it will take more substrate to out-
compete the competitive inhibitor, but with enough substrate this can be done and the enzyme
will achieve the same maximum rate eventually, with or without the competitive inhibitor.
· Regardless of how fast the enzyme can process the reaction (meaning with or without
the competitive inhibitor), the actual energy costs associated with the reaction do not change.
As a result, the competitive inhibitor antibiotic should have no effect on the activation energy
required for the enzyme-catalyzed reaction.
Reflect on Process
· This question asked you to analyze the effect of a competitive inhibitor antibiotic on
the activation energy for an enzyme-catalyzed reaction.
· If you got the answer correct, good job! If you got an incorrect answer, did you
remember that competitive inhibitors bind to the active site? Did you recall how competitive
inhibitors affect overall reaction rate as substrate concentration changes? Were you able to
determine that activation energy, the actual cost of the reaction, doesn’t change regardless of
the presence or absence of a competitive inhibitor?
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Gradable: automatic
Section: 06.02

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44. A new antibiotic has been developed. It acts as a noncompetitive inhibitor. How will this
antibiotic affect delta G for the enzyme-catalyzed reaction?
A. Delta G will increase
B. Delta G will decrease
C. Delta G will be unaffected
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Clarify Question

· The question asks you ascertain how an antibiotic that noncompetitively inhibits an
enzyme will affect the reaction’s change in free energy.
· You are being asked to break down, or analyze, how a noncompetitive inhibitor
antibiotic will influence an enzyme-catalyzed change in free energy.
Gather Content
What do you already know about enzymes and free energy? What other information is
· Remember that an enzyme helps to accelerate the rate of a reaction by making the
reaction more likely to occur. Recall that noncompetitive inhibitors bind not to the active site,
but to an enzyme’s secondary site which changes the protein’s three-dimensional
confirmation, changes the shape of the active site, and thereby reduces the overall speed of the
reaction.
· Considering the structure and function of enyzmes and how noncompetitive inhibitors
work, how might the free energy of the reaction be affected?
Choose Answer
Do you have all necessary information to analyze how the noncompetitive inhibitor might
influence free energy?
· Recall that noncompetitive inhibitors bind to a secondary site on the enzyme, which
changes the shape of the enzyme and precludes the substrate from binding to the active site.
Thus, no amount of substrate will allow the enzyme to reach its top speed because the shape
of the active site has been changed.
· Regardless of how fast the enzyme can process the reaction (meaning with or without
the noncompetitive inhibitor), the actual difference in free energy between the reactants and
the products will not change. Whether or not a reaction is exergonic or endergonic is a
function of whether or not the reaction has a positive or negative delta G. The presence of an
enzyme, or a noncompetitive inhibitor, has no effect on the difference in free energy. As a
result, the noncompetitive inhibitor antibiotic should have no effect on the free energy
required for the enzyme-catalyzed reaction.
Reflect on Process
· This question asked you to analyze the effect of a noncompetitive inhibitor antibiotic
on the free energy for an enzyme-catalyzed reaction.
· If you got the answer correct, well done! If you got an incorrect answer, did you
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remember that noncompetitive inhibitors bind to a secondary site on an enzyme? Did you
recall how noncompetitive inhibitors affect overall reaction rate as substrate concentration
changes? Were you able to determine that free energy, or the difference in free energy from
reactants to products, doesn’t change regardless of the presence or absence of a
noncompetitive inhibitor?

Gradable: automatic
Section: 06.02

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45. Glycolysis is a metabolic process that is done by all cells. However, not all cells make
use of another metabolic process called the Krebs cycle. What does this tell you about the
evolution of these processes?
A. As a metabolic process, glycolysis likely evolved prior to the Krebs cycle
B. As a metabolic process, the Krebs cycle likely evolved prior to glycolysis
C. Both the Krebs cycle and glycolysis likely evolved at the same time
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Clarify Question

· The question asks you to determine why glycolysis is used by all cells but the Krebs
cycle is not.
· You are being asked to break down, or analyze, why glycolysis is used by all cells but
only some use the Kreb’s cycle.
Gather Content
What do you already know about evolution and time? What other information is related to
the question?
· Remember that evolution is a series of changes that occur over time. Evolution is
shaped by several factors, including natural selection that confers greater biological fitness for
a pre-existing genetic makeup within a given environment.
· Recall also that the greater numbers of species that share a trait, the older the trait or
the more important the trait may be. Given this context and considering that all organisms use
glycolysis but not all use the Kreb’s cycle, what conclusions can you draw?
Choose Answer
Do you have all necessary information to determine the relative importance of glycolysis
and the Kreb’s cycle?
· Glycolysis is used by all cells to metabolize energy. Since it is such a widely shared
trait across different life forms, it is because it is fundamentally important to survival and
because it has been around for a long time in evolutionary history; certainly longer than the
Kreb’s cycle, which is not used by all cells..
Reflect on Process
· This question asked you to analyze the relative importance of glycolysis vs the Kreb’s
cycle in evolutionary history.
· If you got the answer correct, excellent! If you got an incorrect answer, did you
remember how evolution occurs? Were you able to infer how biologically relevant glycolysis
is based on its prevalence across life forms in nature? Were you able to compare its
importance to the Kreb’s cycle based on this information?
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Gradable: automatic
LO: 06.05.03 Recognize that metabolism is a product of evolution.
Section: 06.05

46. Enzyme 1 converts substrate A into product B. Is this an example of a metabolic
pathway?
A. Yes. This is a metabolic pathway that includes feedback inhibition.
B. No. This only describes one chemical reaction. A metabolic pathway includes multiple
chemical reactions.
C. Yes. This is a simple metabolic pathway.
D. No. A metabolic pathway must include an inhibitory step.

Gradable: automatic
LO: 06.05.02 Discuss what is meant by a metabolic pathway.
Section: 06.05

47. It is summer, and you are excited about going to your local amusement park, and
specifically about riding the new roller coaster that was just built. You imagine waiting at the
top of the stairs for the roller coaster to pull into the station, climbing into the car, strapping
yourself into the seatbelt, and pulling down the harness. You can imagine the cars slowly
chugging up to the top of the first hill, coming down on the other side, and the excitement you
expect to feel as you go along for the ride. Of all of the things that you have imagined, which
is an example of potential energy?
A. Waiting at the top of the stairs for the roller coaster to pull into the station
B. Climbing into the car
C. Pulling down the harness
D. The roller coaster car going up the first hill

Gradable: automatic
Section: 06.01

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48. Phosphofructokinase (PFK) is an enzyme that converts fructose 6-phosphate to fructose

1,6-bisphosphate, by adding a phosphate group. This is the first committed step of the
metabolic pathway of glycolysis, and thus it is very tightly regulated. AMP binds to PFK at a
site distinct from the binding site for fructose 6-phosphate, and stimulates the formation of
fructose 1,6-bisphosphate. ATP binds to PFK at a site distinct from the binding site for
fructose 6-phosphate, and inhibits the formation of fructose 1,6-bisphosphate. There are other
regulators of this enzyme as well. What is the role of AMP in this example?
A. Competitive inhibitor
B. Noncompetitive inhibitor
C. Allosteric inhibitor
D. Allosteric activator
E. Catalyst
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Clarify Question

· The question asks you to determine the role of AMP in regulating PFK enzyme in the
glycolysis metabolic pathway.
· You are being asked to dissect, or analyze, how AMP works to regulate the activity of
the PFK enzyme based on the scenario.
Gather Content
What do you already know about enzymes, feedback inhibition, and glycolysis? What
other information is related to the question?
· Remember that several enzymes can function together in a biochemical pathway, and
the efficient regulation of that pathway frequently involves feedback inhibition, which occurs
when the final product regulates an earlier step in the pathway.
· In glycolysis, PFK is a critical rate-setting enzyme that can be regulated to work faster
or slower, depending on environmental conditions. What molecules are likely to help increase
PFK activity when the cell needs more energy and decrease PFK activity when it needs less
energy via glycolysis?
Choose Answer
Do you have all the information needed to determine how AMP helps to regulate PFK
activity?
· Recall that biochemical pathways are a series of enzyme-regulated chemical reactions.
Control of a key enzyme in the pathway helps to regulate the entire pathway.
· In order to regulate a key enzyme like PFK, you need that enzyme to be able to sense
when there is too little or too much energy available. Carefully managing the cell’s resources
by tailoring energy metabolism is key to efficiency and survival.
· Consider that ATP is an important high-energy molecule used by the cell to power its
processes. If a cell has enough ATP, is it useful and efficient for that cell to make more when it
already has enough? When enough ATP is present, it will bind to PFK and down-regulate its
activity so that more ATP isn’t made until it is needed.
· Conversely, when energy levels are too low in the cell, you want to move molecules
through glycolysis in order to make more ATP. But how does the cell sense when energy
levels are low? It needs a sensory molecule, which in this case is AMP. AMP is a low-level
energy molecule, and acts as an effective sensor for PFK and glycolysis. So how does it
work? AMP can bind to an allosteric site on PFK, which activates PFK and increases the rate
of glycolysis, which results in greater ATP production.
Reflect on Process
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· This question asked you to analyze a possible role for AMP in regulating PFK and
glycolysis.
· If you got the answer correct, fantastic! If you got an incorrect answer, did you
remember how biochemical pathways work? Were you able to determine how PFK is
regulated based on key role in glycolysis? Were you able to infer how AMP works as a sensor
and activates PFK?

Gradable: automatic
Section: 06.04

49. You eat a bowl of beans as part of your dinner. As you digest the beans, the proteins that
are present get broken down to their component amino acids. As your body destroys the
macromolecules that were present in the beans, is the energy present in those molecules
destroyed?
A. Yes. By breaking down these macromolecules, some of the energy they contained is
destroyed.
B. No. While the vast majority of the energy contained in these macromolecules is converted
to heat, it is not actually destroyed.
C. No. The energy contained within these macromolecules is converted into other forms of
chemical energy and kinetic energy, though some is lost as heat.
D. No. Breaking down molecules does not lead to the release of energy.

Gradable: automatic
Section: 06.02

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50. While standing at the top of the stairs, you have a potential energy of 40 Joules. If you
walk all the way down the stairs, what would your potential energy be at the bottom of the
stairs?
A. 0 Joules
B. 20 Joules
C. 40 Joules
D. 80 Joules
6-62
Clarify Question

· The question asks for you to identify the how muchpotential energy exists after
walking down stairs.
· You are being asked to take what you already know about different states of energy
and apply your understanding to determine how much potential energy you would have at the
bottom of stairs.
Gather Content
What do you already know about potential and kinetic energy? What other information is
· To solve this problem you’ll need to apply what you know about different states of
energy and use this to determine how much potential energy exists after walking down stairs
to the bottom.
· Remember that potential energy is stored energy and kinetic energy is from things in
motion. How are potential and kinetic energy related to each other?
Choose Answer

· At this point you should have everything you need to answer the question. Of the
available options, which are involved with motion and which with rest? Hopefully it is clear
that any answer with a number has some level of potential energy associated with it.
· When the person was at the top of the stairs they had maximum potential energy. As
they walked down the stairs this potential energy became converted into kinetic energy.
Ultimately, when they arrived at the bottom of the stairs, all the potential energy has been
converted, and since they aren’t moving, has no potential energy left.
Reflect on Process
of potential and kinetic energy. If you got an incorrect answer, did you remember that energy
has potential and kinetic forms? Did you remember that potential energy is stored energy, and
kinetic energy is energy of motion? Were you able to apply that understanding to determine
that walking to the bottom of stairs converted all your potential energy and so would have 0
Joules?
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Gradable: automatic
Section: 06.01

6-64
51. If you were able to increase the kinetic energy of the molecules inside your body, how
would this affect your body temperature?
A. It would increase
B. It would decrease
C. It would remain the same
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Clarify Question

· The question asks for you to determine how increased kinetic energy in your body
might affect your body temperature.
· You are being asked to take what you already know about potential and kinetic energy
and apply your understanding to determine how increased kinetic energy might affect body
temperature.
Gather Content
What do you already know about potential and kinetic energy? What other information is
· To solve this problem you’ll need to apply what you know about kinetic energy and
use this to infer what might happen to body temperature.
· Remember that kinetic energy is energy associated with things in motion. What effect
does temperature how on objects in motion?
Choose Answer

· Objects in motion are affected by temperature. Think about it; when something is
frozen, it is immobile, and its kinetic energy is very low or absent. The opposite would also be
true; if you could increase the kinetic energy of your body, the molecules that make up your
body would be in motion, and more intensely moving. This would increase the number of
contact events between molecules, which would elevate the cellular temperature and thus your
body temperature.
Reflect on Process
of kinetic energy and relate it to temperature. If you got an incorrect answer, did you
remember that kinetic energy is energy associated with objects in motion? Did you remember
that objects in motion frequently generate friction, and friction generates heat? Were you able
to apply that understanding to predict that body temperature would increase as kinetic energy
increases?
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Gradable: automatic
Section: 06.01

52. You return home to find that your baby brother has scattered his toy trains and trucks all
over the floor of your room. As you begin to pick up the toys and put them away, you realize
that even though he is just a baby, he has clearly mastered:
A. the first law of thermodynamics.
B. the second law of thermodynamics.
C. potential energy.
D. free energy.

Gradable: automatic
Section: 06.02

53. If the DG of a reaction was -31.45 kJoules, you would know that:
A. the products have more free energy than the reactants.
B. the reaction requires an energy input of 31.45 kJoules to proceed.
C. the reaction most likely leads to development of a more ordered system.
D. the reaction is spontaneous.

Gradable: automatic
Section: 06.02

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54. In the hypothetical biochemical pathway, P ® Q + R ® S ® T, which step is likely to have

evolved first?
A. P ® Q
B. Q + R
C. R ® S
D. S ® T
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Clarify Question

· The question asks you to determine which step in a biochemical pathway would be
likely to have evolved first.
· You are being asked to break down, or analyze, the steps in a biochemical pathway to
determine the most suitable targets for early evolution.
Gather Content
What do you already know about evolution? What other information is related to the
question?
· Remember that evolution is a series of changes that occur over time. Evolution is
shaped by several factors, including natural selection that confers greater biological fitness for
a pre-existing genetic makeup within a given environment.
· A trait that evolved could convey greater biological fitness to some members of a
population as compared to others without that trait for a given environment. The same can be
said of molecules in a biochemical pathway. Inherited genetic changes that lead to molecular
variation which in turn affects pathway productivity could provide enhanced function for the
cells that contain them. That said, which steps in the biochemical pathway are most likely to
be foundational to function and evolved first?
Choose Answer
Do you have all necessary information to break down the biochemical pathway?
· There are 5 components in the biochemical pathway, starting with P and eventually
leading to T. Of these 5 components, which is most likely to have the key outcome and
function? That would most likely be product T, which is the function end product and most
likely to be used directly in cellular structure and/or function.
· Working backwards from there, the steps that are most directly connected to product T
represent the core chemistry in the pathway, which in this case is S -> T. All the other steps in
the pathway are essentially preparation to get to the functional end point of product T. Being
the most central to the pathway’s function, the S -> T reaction is likely to have evolved first.
Reflect on Process
· This question asked you to determine which steps in a biochemical pathway are most
likely to have evolved first.
· If you got the answer correct, excellent! If you got an incorrect answer, did you
remember how evolution occurs? Were you able to break down the steps in a biochemical
pathway and determine which is most important? Were you able to infer the evolutionary
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significance of this step?

Gradable: automatic
LO: 06.05.03 Recognize that metabolism is a product of evolution.
Section: 06.05

6-71
55. While conducting an experiment, you realize that a competitive inhibitor was interfering
with your reaction. How could you overcome this problem?
A. Add a non-competitive inhibitor to the reaction.
B. Add a cofactor to the reaction.
C. Increase the concentration of the correct substrate in the reaction.
D. Add an allosteric activator to the reaction.
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Clarify Question

· The question asks for you to overcome a problem where a competitive inhibitor is
interfering with a reaction.
· You are being asked to take what you already know about enzymes and competitive
inhibition and apply your understanding to determine how to rectify the problem.
Gather Content
What do you already know about enzymes and competitive inhibition? What other
· To solve this problem you’ll need to apply what you know about how competitive
inhibition regulates enzyme function. Recall that enzyme function can be inhibited
competitively, noncompetitively, and allosterically. How does competitive inhibition compare
to the other types of inhibition, and keeping that mechanism in mind, what could you do to
overcome the inhibition?
Choose Answer

· The question indicates that a competitive inhibitor is messing up your reaction. If you
added a noncompetitive inhibitor, you would like still end up with decreased enzyme
functionality because it changes the enzyme structure and prevents substrate binding
altogether. An allosteric inhibitor would essentially function in the same way as a
noncompetitive inhibitor, and likewise not help your reaction.
· A cofactor might conceivably help overcome the latent inhibition, but only if the
cofactor outcompeted the inhibitor for the active site.
· That leaves increasing substrate concentration as the best solution. Recall that with
competitive inhibition, the inhibitor directly competes with the substrate for the enzyme’s
active site. Both inhibitor and substrate try to occupy the same physical space within the
structure of the enzyme. Increasing substrate concentration would serve up more reactants to
the active site per unit time than the inhibitor, effectively washing out the effects of the
inhibitor.
Reflect on Process
of enzymes and competitive inhibition to determine what would be the most likely solution to
restore your reaction.
· If you got an incorrect answer, did you recall how competitive inhibition works? Did
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you contrast that with noncompetitive and allosteric inhibition, which don’t involve the active
site and therefore wouldn’t solve the problem at all? Were you able to decipher that the best
solution was to simply outcompete the competitive inhibitor by increasing substrate?

Gradable: automatic
Section: 06.04

56. A ribozyme catalyzes a reaction on itself and actually changes shape. This is an example
of.
A. intra-enzyme reactions.
B. inter-enzyme reactions.
C. intramolecular catalysis.
D. intermolecular catalysis.

Gradable: automatic
Section: 06.04

6-75

Multiple Choice Questions: Energy and Metabolism

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Chapter 06 - Energy and Metabolism

Multiple Choice Questions

1. Why do we have storage macromolecules, such as fats, in our bodies?

Blooms Level: 2. Understand

2. Energy is defined as

Blooms Level: 1. Remember

3. The amount of energy available to do work is called

Blooms Level: 1. Remember

Blooms Level: 1. Remember

Blooms Level: 3. Apply

Blooms Level: 1. Remember

Blooms Level: 2. Understand

What is the key concept addressed by the question?

Do you have all the information needed to answer the question?

closely resembling the substrate.

Blooms Level: 3. Apply

Blooms Level: 1. Remember

Because this process requires energy input, it is an endergonic reaction.

Blooms Level: 2. Understand

What is the key concept addressed by the question?

Do you have all the information needed to answer the question?

Blooms Level: 3. Apply

Since kinases function to phosphorylate macromolecules, and Kinase 1 phosphorylates

Blooms Level: 2. Understand

Blooms Level: 2. Understand

Blooms Level: 2. Understand

Blooms Level: 1. Remember

Blooms Level: 1. Remember

Blooms Level: 2. Understand

Blooms Level: 1. Remember

Blooms Level: 1. Remember

Blooms Level: 2. Understand

Blooms Level: 1. Remember

Blooms Level: 1. Remember

Blooms Level: 2. Understand

Blooms Level: 1. Remember

Blooms Level: 1. Remember

What is the key concept addressed by the question?

Blooms Level: 4. Analyze

What is the key concept addressed by the question?

Blooms Level: 4. Analyze

Blooms Level: 1. Remember

29. In an enzyme-catalyzed reaction, the reactant is called the

Blooms Level: 2. Understand

Blooms Level: 1. Remember

Blooms Level: 2. Understand

What is the key concept addressed by the question?

Do you have all necessary information to make a judgment?

Blooms Level: 5. Evaluate

Blooms Level: 2. Understand

Blooms Level: 1. Remember

Blooms Level: 2. Understand

Blooms Level: 2. Understand

37. In a chemical reaction, glyceraldehyde-3-phosphate + NAD+ yields 1,3-

What is the key concept addressed by the question?

Blooms Level: 4. Analyze

38. In a chemical reaction, 1,3-bisphosphoglycerate + ADP yields 3-phosphoglycerate plus