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APBIO Reading Guide Answers Chapter 8
APBIO Reading Guide Answers Chapter 8
Define metabolism.
The totality of an organisms chemical reactions, consisting of catabolic and anabolic pathways,
which manage the material and energy resources of the organism.
2.
There are two types of reactions in metabolic pathways: anabolic and catabolic.
a. Which reactions release energy? catabolic
b. Which reactions consume energy? anabolic
c. Which reactions build up larger molecules? catabolic
d. Which reactions break down molecules? catabolic
e. Which reactions are considered uphill? anabolic
f. What type of reaction is photosynthesis? catabolic
g. What type of reaction is cellular respiration? catabolic
h. Which reactions require enzymes to catalyze reactions? catabolic, anabolic
3.
4.
Which type of energy does water behind a dam have? A mole of glucose?
Water behind a dam has potential energy. A mole of glucose also has potential energy, though more
specifically, glucose has chemical energy, a term used by biologists to refer to the potential energy
available for release in a chemical reaction.
5.
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Concept 8.2 The free-energy change of a reaction tells us whether the reaction occurs spontaneously
6.
7.
8.
9.
Is photosynthesis endergonic or exergonic? What is the energy source that drives it?
Photosynthesis is an endergonic reaction. Plants get the required energy686 kcal to make a mole of
glucosefrom the environment by capturing light and converting its energy into chemical energy.
10.
Concept 8.3 ATP powers cellular work by coupling exergonic reactions to endergonic reactions
11.
List the three main kinds of work that a cell does. Give an example of each.
a. Chemical work, the pushing of endergonic reactions that would not occur spontaneously, such as the
synthesis of polymers from monomers
b. Transport work, the pumping of substances across membranes against the direction of spontaneous
movement; possible examples include the sodium-potassium pump and proton pump
c. Mechanical work, such as the beating of cilia, the contraction of muscle cells, and the movement of
chromosomes during cellular reproduction
12.
Here is a molecule of ATP. Label it. Use an arrow to show which bond is likely to break.
See page 149 of your text for the labeled figure.
a. By what process will that bond break?
Hydrolysis
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b. Explain the name ATP by listing all the molecules that make it up.
ATP contains the sugar ribose, with the nitrogenous base adenine and a chain of three phosphate
groups bonded to it, forming adenosine triphosphate.
13.
When the terminal phosphate bond is broken, a molecule of inorganic phosphate Pi is formed, and
energy is released.
For this reaction: ATP ADP + Pi, G = 7.3 kcal/mol (30.5 kJ/mol)
Is this reaction endergonic or exergonic? Exergonic
FYI: An essay question on the 2009 AP Biology exam asked students to identify the molecules that make
up ATP. What are they again?
Sugar ribose, with the nitrogenous base adenine and a chain of three phosphate groups
14.
15.
In many cellular reactions, a phosphate group is transferred from ATP to some other molecule in
order to make the second molecule less stable. The second molecule is
said to be phosphorylated intermediate.
16.
Look for this amazing bit of trivia on page 151: If you could not regenerate ATP by
phosphorylating ADP, how much ATP would you need to consume each day?
If ATP could not be regenerated by the phosphorylation of ADP, humans would use up nearly their
body weight in ATP each day.
What is a catalyst?
A chemical agent that selectively increases the rate of a reaction without being consumed by the
reaction.
18.
19.
Label the x-axis of this graph Progress of the Reaction and the y-axis Free Energy.
Label EA on this sketch, both with and without an enzyme.
See page 152 of your text for the labeled figure.
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Label this figure while you define each of the following terms:
See page 155 of your text for the labeled figure.
enzyme: A macromolecule serving as a catalyst, a chemical agent that increases the rate of a reaction
without being consumed by the reaction. Most enzymes are proteins.
substrate: The reactant on which an enzyme works.
active site: The specific region of an enzyme that binds the substrate and that forms the pocket in
which catalysis occurs.
products: A material resulting from a chemical reaction.
21.
What is meant by induced fit? How is it shown in the figure in question 20?
Caused by entry of the substrate, the change in shape of the active site of an enzyme so that it binds
more snugly to the substrate. In Figure 8.14 on page 154, when the substrate enters the active site, it
forms weak bonds with the enzyme, inducing a change in the shape of the protein. This change
allows additional weak bonds to form, causing the active site to enfold the substrate and hold it in
place.
22.
23.
Enzymes use a variety of mechanisms to lower activation energy. Describe four of these mechanisms.
a. In reactions involving two or more reactants, the active site provides a template on which the
substrates can come together in the proper orientation for a reaction to occur between them.
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b. As the active site of an enzyme clutches the bound substrate, the enzyme may stretch the substrate
molecules toward their transition-state form, stressing and bending critical chemical bonds that must
be broken during the reaction.
c. The active site may also provide a microenvironment that is more conducive to a particular type of
reaction than the solution itself would be without the enzyme.
d. Direct participation of the active site in the chemical reaction is another mechanism of catalysis.
24.
Many factors can affect the rate of enzyme action. Explain each factor listed here.
a. initial concentration of substrate: The more substrate molecules that are available, the more
frequently they access the active sites of the enzyme molecules.
b. pH: With some exceptions, the optimal pH values for most enzymes fall in the range of pH 68.
c. temperature: Up to a point, the rate of an enzymatic reaction increases with increasing temperature,
partly because substrates collide with active sites more frequently when molecules move rapidly.
Above that temperature, however, the speed of the enzymatic reaction drops sharply.
25.
Recall that enzymes are globular proteins. Why can extremes of pH or very high temperatures affect
enzyme activity?
Three-dimensional structures of proteins are sensitive to their environment. As a consequence, each
enzyme works better under some conditions than other conditions, because these optimal conditions
favor the most active shape for their enzyme molecule.
26.
27.
28.
Compare and contrast competitive inhibitors and noncompetitive inhibitors. Label each type of
inhibitor in this figure.
See page 156 of your text for the labeled figure.
Competitive inhibitors are substances that reduce the activity of an enzyme by entering the active site
in place of the substrate, whose structure it mimics.
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Noncompetitive inhibitors are substances that reduce the activity of an enzyme by binding to a
location remote from the active site, changing the enzymes shape so that the active site no longer
effectively catalyzes the conversion of substrate to product.
Concept 8.5 Regulation of enzyme activity helps control metabolism
29.
30.
How is allosteric regulation somewhat like noncompetitive inhibition? How might it be different?
It is like noncompetitive inhibition in that it may inhibit enzyme activity, but different in that it may
also stimulate enzyme activity.
31.
32.
Although it is not an enzyme, hemoglobin shows cooperativity in binding O2. Explain how
hemoglobin works at the gills of a fish.
Hemoglobin is made up of four subunits, each of which has an oxygen-binding site. The binding of
an oxygen molecule to one binding site increases the affinity for oxygen of the remaining binding
sites. Thus, where oxygen is at high levels, such as in the lungs or gills, hemoglobins affinity for
oxygen increases as more binding sites are filled.
33.
Study this figure from your book (Figure 8.21) and answer the questions that follow.
See page 160 of your text for the labeled figured.
a. What is the substrate molecule to initiate this metabolic pathway?
Threonine
b. What is the inhibitor molecule?
Isoleucine
c. What type of inhibitor is it?
Noncompetitive inhibitor
d. When does it have the most significant regulatory effect?
When it binds to an allosteric site
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2. c
3. b
4. a
5.c
6. e
7. e
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