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CH 03
CH 03
1) The chemical energy stored in ATP is converted to mechanical energy that can move
organelles around within the cell. This is an example of __________.
a) being exothermic
b) being endothermic
c) energy transduction
d) polymerization
e) catheterization
Answer: c
Difficulty: Medium
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
2) When energy is being stored for later use or for use at a distant site, the most frequent form of
storage is _____________________.
a) as mechanical energy
b) within the chemical bonds of molecules
c) as kinetic energy
d) as electrostatic energy
Answer: b
Difficulty: Medium
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
3) What is an essential difference between thermodynamics and bioenergetics?
a) Bioenergetics studies energy transformations taking place within living organisms while
thermodynamics studies energy changes within a broader system, up to the size of the universe.
b) Bioenergetics studies energy transformations taking place within living organisms while
thermodynamics studies molecular reactions occurring in isolation.
c) Thermodynamics studies energy transformations taking place within living organisms while
bioenergetics studies energy changes within a broader system, up to the size of the universe.
d) Bioenergetics studies energy transformations taking place within living organisms while
thermodynamics studies only the energy changes of the non-living world.
Answer: a
Difficulty: Medium
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
Answer: d
Difficulty: Easy
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
5) You are observing a reaction and discover that the reaction vessel is warm to the touch. The
reaction also results in an increase in entropy. Which statement correctly confirms whether or not
the reaction is spontaneous and explains why?
a) The reaction is exothermic (-H) as demonstrated by the warm reaction vessel and entropy is
increased (+S). The reaction has a negative G and is, therefore, spontaneous.
b) The reaction is exothermic (+H) as demonstrated by the warm reaction vessel and entropy is
increased (+S). The reaction therefore has a negative G and is, therefore, spontaneous.
c) The reaction is exothermic (+H) as demonstrated by the warm reaction vessel and entropy is
increased (-S). The reaction has a positive G and is, therefore, spontaneous.
d) The reaction is endothermic (-H) as demonstrated by the warm reaction vessel and entropy is
increased (-S). The reaction has a positive G and is, therefore, spontaneous.
Answer: a
Difficulty: Hard
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
6) A reaction vessel is cold to the touch and the reaction results in an increase in order of the
products inside the reaction vessel. Which statement correctly confirms whether or not the
reaction is spontaneous and explains why?
a) The reaction is exothermic (-H) as demonstrated by the cold reaction vessel and entropy is
increased (+S). The reaction has a negative G and is, therefore, spontaneous.
b) The reaction is endothermic (+H) as demonstrated by the cold reaction vessel and entropy is
decreased (-S). The reaction therefore has a positive G and is, therefore nonspontaneous.
c) The reaction is exothermic (+H) as demonstrated by the cold reaction vessel and entropy is
increased (-S). The reaction has a positive G and is, therefore, spontaneous.
d) The reaction is endothermic (-H) as demonstrated by the cold reaction vessel and entropy is
increased (+S). The reaction has a positive G and is, therefore, nonspontaneous.
Answer: b
Difficulty: Hard
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
Answer: b
Difficulty: Medium
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
8) Which choice below correctly rationalized whether this pair of reactions is coupled?
a) The equations above do not represent coupled reactions because the overall G is positive.
b) The equations above do not represent coupled reactions because the overall G is negative.
c) The equations represent coupled reactions because the overall G is positive.
d) The equations represent coupled reactions because the overall G is negative.
Answer: a
Difficulty: Medium
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
a) entropic
b) endothermic
c) exothermic
d) unreactive
Answer: c
Difficulty: Easy
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
10) The statement that events in the universe proceed from a state of higher energy to one of
lower energy describes the_____________________.
Answer: b
Difficulty: Easy
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
11) Which scenario does NOT describe an increase in entropy within the system described?
Answer: d
Difficulty: Easy
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
12) Entropy is associated with the _________ movement of particles of matter, which because
they are ________ cannot accomplish a directed work process.
a) rapid, directed
b) random, random
c) rapid, random
d) slow, rapid
e) random, slow
Answer: b
Difficulty: Easy
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
Answer: b
Difficulty: Easy
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
14) Given the equation G = H - TS, which set of conditions would result in a reaction that is
unambiguously nonspontaneous?
Answer: a
Difficulty: Hard
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
15) Which reaction below might be a suitable coupled reaction for the reaction A + B —> C + D
(G = -8.7 kcal/mole)?
Answer: c
Difficulty: Hard
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
Answer: c
Difficulty: Easy
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
17) You mix reagents (A, B, C, D) so that each is present at an initial concentration of 0.5M.
The equilibrium constant for the reaction Keq is 4. Which choice represents the final
a) [ 0.67][0.67]
[ 0.33][0.33]
b) [ 0.5][0.5]
[ 0.25][0.25
]
c) [ 0.4][0.4]
[ 0.5][0.5]
d) [ 0.4][0.4]
[ 0.1][0.1]
Answer: a
Difficulty: Hard
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
18) After allowing the reaction to proceed, you find that the the final concentrations of each
a) 18
b) 1.8
c) 0.18
d) .001
Answer: c
Difficulty: Medium
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
19) After allowing the reaction to proceed, you find that the the final concentrations of each
Answer: d
Difficulty: Medium
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
20) A pharmacist is looking for a drug which will prevent an enzyme from working by binding to
it as an inhibitor. Which of the inhibitors listed as choices will prove most effective, given
equality in other considerations such as solubility, toxicity and stability?
a) Substance X, Kd = 2.7
b) Substance Y, Kd = 23
c) Substance Z, Kd = 0.05
d) Substance P, Kd = 0.001
Answer: d
Difficulty: Medium
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1: Bioenergetics
Answer: a
Difficulty: Medium
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
a) raising the activation energy of a reaction and thus speeding up the reaction
b) lowering the activation energy of a reaction and thus speeding up the reaction
c) raising the G of a reaction and thus speeding up the reaction
d) lowering the G of a reaction and thus speeding up the reaction
e) changing the free energy of the products and thus speeding up the reaction
Answer: b
Difficulty: Easy
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
23) What kind of interaction is NOT involved in the binding of a substrate to a normally
functioning enzyme?
a) hydrogen bonds
b) a transient covalent bond
c) ionic bonds
d) a permanent covalent bond
e) hydrophobic interactions
Answer: d
Difficulty: Easy
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
24) What molecule type other than protein has been observed to have catalytic activity?
a) carbohydrates
b) lipids
c) RNA
d) DNA
Answer: c
Difficulty: Easy
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
25) Who was the first scientist to determine the structure and composition of an enzyme?
a) von Liebig
b) Pasteur
c) Sumner
d) Büchner
Answer: c
Difficulty: Easy
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
26) In the absence of an enzyme, a monosaccharide like galactose or glucose, will likely
decompose in roughly ___________.
a) 30 seconds
b) 3 weeks
c) 30 days
d) 30,000 years
Answer: d
Difficulty: Easy
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
27) Energy rich monosaccharides and other biological monomers which are seen to exist stably
in purified form are said to be:
Answer: d
Difficulty: Medium
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
28) You are a researcher trying to design an enzyme inhibitor for a particular enzyme. Which
molecule should your inhibitor most closely resemble for the most effective inhibition to take
place?
Answer: c
Difficulty: Medium
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
29) The environment within an enzyme’s active site tends to have ______________
characteristics.
a) acidic
b) hydrophilic
c) basic
d) hydrophobic
Answer: c
Difficulty: Easy
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
30) Doubling the concentration of enzyme will ______ the Vmax and _____ the KM.
Answer: a
Difficulty: Hard
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
31) What kind of inhibitor binds very tightly to an enzyme often forming a covalent bond with
an amino acid in the active site?
a) irreversible
b) reversible
c) uncompetitive
d) reversible and uncompetitive
e) None of these are correct.
Answer: a
Difficulty: Medium
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
Answer: b
Difficulty: Easy
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
33) You are observing an enzyme driven reaction. You add chemical X, which inhibits the
reaction. If you add more substrate, the reaction rate approaches the Vmax of the uninhibited
reaction. Furthermore, the structure of X is similar to the natural substrate. What kind of inhibitor
is X?
a) irreversible
b) reversible
c) competitive
d) reversible and uncompetitive
e) None of these are correct.
Answer: c
Difficulty: Medium
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
Answer: e
Difficulty: Medium
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
35) The existence of ________ motion in proteins suggests that enzymes are capable - even in
the absence of substrate - of many of the same movements that can be detected during their
catalytic cycle.
a) extrinsic
b) intrinsic
c) instant
d) built-in
e) intrinsic and built-in
Answer: e
Difficulty: Medium
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
36) In the reaction A + B <—> C + D, how might the reaction take place in the cell if the G is
very positive?
a) The reaction would probably take place by coupling it to a reaction with a larger -G so that
when the G values are added up the sum is negative.
b) ) The reaction would probably take place by coupling it to a reaction with a smaller -G so
that when the G values are added up the sum is positive.
c) ) The reaction would probably take place by coupling it to a reaction with a larger G so that
when the G values are added up the sum is positive.
d) ) The reaction would probably take place by coupling it to a reaction with the same positive
G so that when the G values are added up the energy levels balance.
Answer: a
Difficulty: Medium
Learning Objective: LO 3.1: Explain the importance of the laws of thermodynamics to biological
systems.
Section Reference: Section 3.1 Bioenergetics
37) What is the effect of a competitive inhibitor on an enzyme-mediated reaction?
Answer: e
Difficulty: Medium
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
38) Penicillin fits into the active site of transpeptidases and acts as what kind of inhibitor?
Answer: c
Difficulty: Medium
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
a) macrolides
b) lincosamides
c) tetracyclines
d) quinolones
Answer: d
Difficulty: Medium
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
40) Strategies to combat antimicrobial drug resistance include all of the following EXCEPT:
Answer: b
Difficulty: Medium
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
41) If an antibiotic were found to bind to a site on an essential bacterial enzyme other than the
active site, what would its most likely mode of action be?
a) competitive inhibitor
b) noncompetitive inhibitor
c) inhibitor of protein synthesis
d) lowering activation energy
Answer: b
Difficulty: Easy
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
42) An enzyme has a KM of 20 µM and a Vmax of 50 mmoles of product/minute/µg of enzyme.
After exposure to an inhibitor and analysis on a Lineweaver-Burk plot the following values are
obtained: -1/ KM = - 0.05 liters/µmole and 1/ Vmax = 0.04 (mmoles of product/minute/µg of
enzyme)-1. What kind of inhibitor was used in the experiment and what data interpretation
supports this conclusion?
a) noncompetitive inhibitor because the KM has remained the same and the Vmax has decreased
b) competitive inhibitor because the KM has remained the same and the Vmax has decreased
c) noncompetitive inhibitor because the KM has increased and the Vmax has decreased
d) competitive inhibitor because the KM has increased and the Vmax has decreased
Answer: a
Difficulty: Medium
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
a) noncompetitive inhibitor because the KM has remained the same and the Vmax has decreased
b) competitive inhibitor because the KM has remained the same and the Vmax has decreased
c) noncompetitive inhibitor because the KM has increased and the Vmax has decreased
d) competitive inhibitor because the KM has increased and the Vmax remains the same
Answer: d
Difficulty: Medium
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
44) Metabolic pathways that provide building blocks from which other molecules can be
synthesized and that provide the chemical energy required for many cell activities are known as
______ reactions.
a) anabolic
b) catabolic
c) allosteric
d) anabolic and catabolic
Answer: b
Difficulty: Easy
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
45) A reaction involving the gain of one or more electrons is _________ reaction.
a) an oxidation
b) a reduction
c) an inclusion
d) an elimination
Answer: b
Difficulty: Easy
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
46) Glycolysis occurs in the ________; the Krebs (TCA) cycle occurs in the ______ of
eukaryotes and the ______ of prokaryotes.
Answer: c
Difficulty: Medium
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
47) What kind of enzyme adds phosphate groups to enzymes for the purpose of activating or
deactivating them?
a) phosphatases
b) protein kinases
c) flippases
d) glycosyltransferases
e) carboxypeptidase
Answer: b
Difficulty: Easy
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
48) The hydrolysis of one glucose molecule has the potential to produce _______ ATP molecules
in cells evolved to optimally catabolize it.
a) 5
b) 10
c) 36
d) 120
Answer: c
Difficulty: Easy
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
49) Although the glycolytic pathway is considered catabolic in purpose, some of the reactions
within the pathway could be considered anabolic. Select the enzyme in glycolysis which
catalyses an anabolic reaction.
a) hexokinase
b) phosphoglucose isomerase
c) aldolase
d) phosphoglycerate kinase
Answer: a
Difficulty: Hard
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
50) Although the glycolytic pathway is considered catabolic in purpose, some of the reactions
within the pathway could be considered anabolic. Select the enzyme in glycolysis which
catalyses an anabolic reaction.
a) phosphofructokinase
b) phosphoglucose isomerase
c) aldolase
d) phosphoglycerate kinase
Answer: a
Difficulty: Hard
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
Answer: c
Difficulty: Medium
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
a) Glucose 6-phosphate
b) 3-phosphoglycerate
c) pyruvate
d) dihydroxyacetone phosphate
Answer: a
Difficulty: Medium
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
53) Given the ability of NADH to transfer energy from the high energy electrons it carries, it is a
molecule most analogous to:
a) glucose
b) ADP
c) ATP
d) pyruvate
Answer: c
Difficulty: Medium
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
Answer: c
Difficulty: Easy
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
55) In glycolysis, fructose 1,6-biphosphate is split into two different molecules with distinct
structures. Which enzyme is responsible for converting one of those molecules to be the same
as the other?
a) hexokinase
b) phosphofructokinase
c) triose phosphate isomerase
d) enolase
Answer: c
Difficulty: Medium
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
56) You are studying metabolic pathways and discover that two pathways intersect so that the
enzyme basinase participates in both of the intersecting pathways, in one case using substrate K
and in the other using substrate M. When presented with substrate K in amounts significantly
larger than M, basinase converts K to L which leads eventually to the production of the end
product R. The activity of the second pathway is depressed simultaneously. In the presence of
large amounts of substrate M and lower amounts of substrate K, the second pathway is activated
and culminates in the production of that pathway's end product Y. The activity of the first
pathway is depressed simultaneously. What are the alternative substrates K and M acting like?
a) noncompetitive inhibitors
b) competitive inhibitors
c) irreversible inhibitors
d) noncompetitive and irreversible inhibitors
Answer: b
Difficulty: Medium
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2: Enzymes as Biological Catalysts
J 4
L
5
Q P O N M 7
9 8
10
a) Positions 1, 2, 8
b) Positions 4, 5, 7
c) Positions 1, 2, 3
d) Positions 8, 9, 10
Answer: c
Difficulty: Medium
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
a) a kinase
b) a dehydrogenase
c) an isomerase
d) a hydrolase
Answer: b
Difficulty: Easy
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
59) What is the activity of dehydrogenase enzymes destined to provide in a cell capable of
respiration?
Answer: a
Difficulty: Medium
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
Answer: c
Difficulty: Hard
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
61) In cells relying exclusively upon glycolysis and substrate-level phosphorylation for ATP
production, why is the production of reduced intermediates from pyruvate so essential?
a) Reduction of pyruvate also allows for the reduction of NADH, providing NAD+ which is an
essential substrate for the activity of glyceraldehyde phosphate dehydrogenase.
b) Reduction of pyruvate allows for the oxidation of NADH, providing NAD+ which is an
essential substrate for the activity of glyceraldehyde phosphate dehydrogenase.
c) Reduction of pyruvate also allows for the reduction of NADH, providing NAD+ which is an
essential substrate for the activity of triose phosphate isomerase.
d) Reduction of pyruvate allows for the oxidation of NADH, providing NAD+ which is an
essential substrate for the activity of triose phosphate isomerase.
Answer: b
Difficulty: Hard
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
62) Plants can regulate proteins, chlorophylls and other factors required for photosynthesis via a
light/dark independent regulatory mechanism known as a _______________________.
a) regulating oscillator
b) circadian oscillator
c) diurnal oscillator
d) entraining oscillator
Answer: b
Difficulty: Easy
Learning Objective: LO 3.4: Explain how the light/dark cycle regulates plant metabolism
Section Reference: Section 3.4: Green Cells: Regulation of Metabolism by the Light/Dark Cycle
63) Advantages derived from the use of a circadian oscillator regulatory mechanism include:
a) less down regulation of proteins needed for photosynthesis during hours of total darkness
b) reduced synthesis of essential photosynthesis proteins on cloudy days
c) reduced synthesis of essential photosynthesis proteins at dawn and dusk
d) prediction of need for photosynthesis-related molecules to maximize photosynthesis during
daylight hours
Answer: d
Difficulty: Medium
Learning Objective: LO 3.4: Explain how the light/dark cycle regulates plant metabolism
Section Reference: Section 3.4: Green Cells: Regulation of Metabolism by the Light/Dark Cycle
64) What is responsible for the periodicity that controls the production of essential
photosynthetic enzymes and factors through the circadian oscillator?
a) carbohydrate availability
b) lipid levels within the cell
c) a protein network synchronized through light sensitivity
d) an RNA network synchronized through light sensitivity
Answer: c
Difficulty: Easy
Learning Objective: LO 3.4: Explain how the light/dark cycle regulates plant metabolism
Section Reference: Section 3.4: Green Cells: Regulation of Metabolism by the Light/Dark Cycle
65) Other than controlling the synthesis of photosynthesis-related proteins and other factors,
which process has been observed in plants to be regulated by the circadian oscillator?
a) flower production
b) pollen release
c) leaf curling
d) root production
Answer: c
Difficulty: Easy
Learning Objective: LO 3.4: Explain how the light/dark cycle regulates plant metabolism
Section Reference: Section 3.4: Green Cells: Regulation of Metabolism by the Light/Dark Cycle
66) If you were comparing circadian oscillator structures between plant species, where might you
predict that there would be the greatest differences?
Answer: a
Difficulty: Hard
Learning Objective: LO 3.4: Explain how the light/dark cycle regulates plant metabolism
Section Reference: Section 3.4: Green Cells: Regulation of Metabolism by the Light/Dark Cycle
67) Tumor imaging can exploit soft tissue differences between normal and malignant cells by
using all of the following EXCEPT:
a) X-rays
b) CAT scans
c) infrared light
d) positron emission
Answer: c
Difficulty: Easy
Learning Objective: LO 3.5: Describe how their increased metabolic rate can be used to image
tumors.
Section Reference: Section 3.5: Engineering Linkage: Using Metabolism to Image Tumors
Answer: b
Difficulty: Medium
Learning Objective: LO 3.5: Describe how their increased metabolic rate can be used to image
tumors.
Section Reference: Section 3.5: Engineering Linkage: Using Metabolism to Image Tumors
69) 2-[18F] fluoro-2-deoxy-D-glucose (FDG) accumulates within tumor cells engaging in higher
than normal glycolytic activity. Which reactive functional group is missing in FDG, permitting
its accumulation in tumor cells and their detection through PET scans?
a) a methyl group
b) a fluoride atom
c) a phosphate group
d) a hydroxyl group
Answer: d
Difficulty: Easy
Learning Objective: LO 3.5: Describe how their increased metabolic rate can be used to image
tumors.
Section Reference: Section 3.5: Engineering Linkage: Using Metabolism to Image Tumors
a) X-rays
b) photons
c) positrons
d) electrons
Answer: c
Difficulty: Medium
Learning Objective: LO 3.5: Describe how their increased metabolic rate can be used to image
tumors.
Section Reference: Section 3.5: Engineering Linkage: Using Metabolism to Image Tumors
a) an X-ray
b) a photon
c) a positron
d) an electron
Answer: b
Difficulty: Medium
Learning Objective: LO 3.5: Describe how their increased metabolic rate can be used to image
tumors.
Section Reference: Section 3.5: Engineering Linkage: Using Metabolism to Image Tumors
72) When using 2-[18F] fluoro-2-deoxy-D-glucose (FDG) uptake by tumor cells to detect
cancerous masses, fluorescein 18 decays releasing __________. This in turn reacts with
__________ and releases pairs of _________________ which are ultimately detected by the
diagnostic scanner.
Answer: b
Difficulty: Medium
Learning Objective: LO 3.5: Describe how their increased metabolic rate can be used to image
tumors.
Section Reference: Section 3.5: Engineering Linkage: Using Metabolism to Image Tumors
73) Using an imaging technique such as positron emission tomography (PET) to detect cancer
has all the advantages described EXCEPT:
a) the image will be clearer than one derived from X-rays or CAT scans
b) PET data can quantify the level of metabolic activity possessed by the tumor cells which may
be useful in determining the rate of tumor growth
c) PET data can predict the next area likely to be invaded by the tumor as it expands or the
region to which stray tumor cells may move (metastasize).
d) PET data can determine the size and shape of the tumor
Answer: c
Difficulty: Hard
Learning Objective: LO 3.5: Describe how their increased metabolic rate can be used to image
tumors.
Section Reference: Section 3.5: Engineering Linkage: Using Metabolism to Image Tumors
Question Type: Multiple Select
74) Why has the pharmaceutical industry drastically cut resources devoted to the development of
new antibiotics? (Select all correct choices)
a) The pharmaceutical industry views the period of time antibiotics need to be taken as too long,
making it difficult to keep supply and demand in balance.
b) The pharmaceutical industry views the period of time antibiotics need to be taken as too short,
making it difficult to maintain profitability.
c) Pharmaceutical companies view the inevitability of microbial resistance acquisition as a
barrier to profitability since drugs that take a long time to produce will have a short market life.
d) Pharmaceutical companies view the holding back of drugs of last resort, such as vancomycin,
as sufficient to shore up the problem of drug resistance acquisition.
Answer: b, c, d
Difficulty: Medium
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
75) You isolate the enzyme that synthesizes folic acid in bacteria and conduct some enzyme
kinetics experiments. You find, not surprisingly, that sulfa drugs inhibit the enzyme's activity.
What happens to the Vmax and KM of this enzyme when it is treated with sulfa drugs? (Select all
the correct statements relating to this experiment)
a) sulfa drugs are competitive inhibitors of the folic acid synthesis pathway
b) Vmax will stay the same and KM of this enzyme will decrease
c) Vmax will decrease and KM of this enzyme will stay the same
d) Vmax will increase and KM of this enzyme will increase
e) Vmax will stay the same and KM of this enzyme will increase
Answer: a, e
Difficulty: Easy
Learning Objective: LO 3.2: Explain how enzyme specificity may lower a reaction's activation
energy.
Section Reference: Section 3.2 Enzymes as Biological Catalysts
76) If people are kept on diets containing about 25% fewer calories than would be required to
maintain their initial body weight, what happens? (Select all correct responses)
Answer: b, c
Difficulty: Easy
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
77) If mice are maintained on very strict diets with reduced caloric intake, what happens to their
life span as compared to littermates fed diets with normal caloric content and why? (Select all
correct responses)
Answer: a, c, d
Difficulty: Medium
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
78) Evidence suggests that lower levels of insulin in the blood may be important in promoting
longevity. Which animal models have been used to gather this evidence? (Select all that apply)
a) mice
b) nematodes
c) humans
d) fruit flies
Answer: c, d
Difficulty: Medium
Learning Objective: LO 3.3: Describe the differences between catabolic and anabolic pathways
in biochemical reactions, including their intermediate steps.
Section Reference: Section 3.3: Metabolism
79) Which statements accurately describe the metabolism and detection of tumor cells? (Select
all that are correct choices)
Answer: a, b, c
Difficulty: Medium
Learning Objective: LO 3.5: Describe how their increased metabolic rate can be used to image
tumors.
Section Reference: Section 3.5: Engineering Linkage: Using Metabolism to Image Tumors
80) Which statements regarding the diagnosis and detection of brain tumors are INCORRECT?
(Select all incorrect choices)
a) PET scanners will directly detect positrons emitted from fluorescein 18 incorporated into 2-
deoxy- D-glucose
b) PET scanners will indirectly detect positrons emitted from fluorescein 18 incorporated into 2-
deoxy- D-glucose
c) Tumor localization within the skull relies on tracking a pair of positrons back to the point
where they diverged in position
d) Tumor localization within the skull relies on tracking a pair of photons back to the point where
they diverged in position
Answer: a, c
Difficulty: Medium
Learning Objective: LO 3.5: Describe how their increased metabolic rate can be used to image
tumors.
Section Reference: Section 3.5: Engineering Linkage: Using Metabolism to Image Tumors