Ch 6 Homework Questions

Part 1 (read pages: 118-128)

1. It is estimated that approximately 90 percent of energy that passes between levels in a food web is
“lost” at each level. Explain the first law of thermodynamics and discuss why this apparent loss of energy
does not contradict the law.
Textbook Reference: 6.1 What Physical Principles Underlie Biological Energy Transformations? p. 119

6. Explain how free energy, total energy, temperature, and entropy are related.
Textbook Reference: 6.1 What Physical Principles Underlie Biological Energy Transformations? p. 119

3. The ultimate goal of metabolism is to drive ATP synthesis. ATP is considered the energy currency of
the cell. Discuss how ATP couples endergonic and exergonic reactions and why it is so important in
cellular functions.
Textbook Reference: 6.2 What Is the Role of ATP in Biochemical Energetics? p. 123

1sg. ATP is necessary for the conversion of glucose to glucose 6-phosphate. Splitting ATP into ADP and
Pi releases energy. Explain how the concepts of kinetic energy and potential energy are related to this
process.
Textbook Reference: 6.2 What Is the Role of ATP in Biochemical Energetics? p. 123

5. Explain how substrate concentration affects the rate of an enzyme-mediated reaction.

Textbook Reference: 6.4 How Do Enzymes Work? p. 128

Part 2 (read pages 128-135)

2. Amylase is a digestive enzyme that breaks down starch and is secreted in the mouth of humans.
Amylase functions well in the mouth but ceases to function once it hits the acidic stomach environment.
Explain why amylase does not function in the stomach.
Textbook Reference: 6.5 How Are Enzyme Activities Regulated? p. 131

4. Figure 6.18 shows the behavior of an allosteric enzyme that has binding sites for a negative regulator.
Describe the behavior of an enzyme with binding sites for a positive regulator instead of a negative
regulator.
Textbook Reference: 6.5 How Are Enzyme Activities Regulated? p. 131

7. Use a graph to explain how temperature affects enzyme activity.

Textbook Reference: 6.5 How Are Enzyme Activities Regulated? p. 131
negative regulator. Describe the behavior of an enzyme with binding sites for a positive regulator instead
of a negative regulator.
Textbook Reference: 6.5 How Are Enzyme Activities Regulated? p. 131

15sg. You are studying a new species never before studied. It lives in acidic pools in volcanic craters
where temperatures reach 100°C. You determine that it has a surface enzyme that catalyzes a reaction
leading to its protective coating. You decide to study this enzyme in the laboratory. Under what conditions
would you most likely find optimum activity of this enzyme? Explain your answer.
Textbook Reference: 6.5 How Are Enzyme Activities Regulated? p. 131–133

10sg. Ascorbic acid, found in citrus fruits, acts as an inhibitor to catecholase, the enzyme responsible for
the browning reaction in fruits such as apples, peaches, and pears. One possibility for its function could
be that ascorbic acid is very similar in size and shape to catechol, the substrate of the browning reaction.
What type of inhibition would this be? Explain how it works.
Textbook Reference: 6.5 How Are Enzyme Activities Regulated? pp. 131–132

11sg. Refer to question 10sg. Suppose further studies indicate that ascorbic acid is not similar to catechol
in size and shape but that the pH of the ascorbic acid solution was responsible for the anti-browning
effect. Explain how the pH alone could have this effect.
Textbook Reference: 6.5 How Are Enzyme Activities Regulated? pp. 131–132
1. b. The released energy is available to do work; therefore, it is kinetic energy.

2. a. Potential energy is energy held within chemical bonds that may be converted to working
kinetic energy.

10. a. Competitive inhibitors compete for the active site with the substrate.

11. b. Denaturing an enzyme alters its three-dimensional structure, often irreversibly.

15. d. Enzymes typically have a temperature range over which they work at a maximal rate.
This optimal temperature tends to be correlated with the body temperature of the organism.

Application
1. The first law of thermodynamics states that energy cannot be created or destroyed, but that it
may be converted from one form to another. In the transfer between levels of a food web,
approximately 90 percent of the energy is converted to unusable heat energy. There is a net
loss of usable energy during each conversion, but the total amount of energy (usable and
unusable) remains the same.

2. The pH optimum of amylase is approximately 7. At that pH, the protein has the three-
dimensional shape to allow starch to bind to its active site and catalyze its hydrolysis. When it is
at the stomach pH (approximately 2), the protein is denatured, and its three-dimensional shape
and active site are lost; therefore, it can no longer catalyze the reaction.

3. The conversion of ATP to ADP and Pi releases approximately 7.3 kcal/mol of energy. This
energy release fuels (endergonic) reactions in the cell. Equilibrium of the reaction is far to the
right and favors the formation of ADP. In the converse, the formation of ATP from ADP and Pi is
energy intensive and can be coupled to highly exergonic reactions within the cell. Thus ATP
functions as an energy shuttle between endergonic and exergonic reactions. The small size of
the molecule and its ubiquitousness allow it to be available and move freely within the cell.

4. A positive regulator would stabilize the enzyme in its active form. In the absence of the
regulator, the enzyme would alternate between its inactive and active forms. When it
encountered substrate, it would bind it only if it happened to be in its active form. When bound
to the regulator, the enzyme would be fixed in its active form, and it would bind substrate at a
greater rate.

5. Increasing substrate concentration will result in an increased rate of reaction until all available
active sites are occupied. At that point, no amount of substrate increase will increase the rate of
reaction (see Figure 6.14).

6. Total energy = free energy + unusable energy × absolute temperature.

7. See Figure 6.22.