Ch06 Quiz

Chapter 06 - The Behavior of Proteins: Enzymes
1. How much faster is a reaction with the fastest enzyme than without a catalyst?
a. About 10 times faster.
b. About 100 times faster.
c. About 1,000 times faster.
d. About 10,000 times faster.
e. About 1020 times faster.
2. The rate of a reaction depends on

a. the free energy change
b. the activation energy
c. the enthalpy change
d. the entropy change
3. The main difference between a catalyzed and an uncatalyzed reaction is that

a. the activation energy of the catalyzed reaction is lower.
b. the catalyzed reaction has a more favorable free energy change.
c. the catalyzed reaction has a more favorable enthalpy change.
d. the catalyzed reaction has a more favorable entropy change.
4. What effect does a catalyst have on the ΔG° of a reaction?

a. A catalyst lowers the ΔG°.
b. A catalyst raises the ΔG°.
c. A catalyst has no effect on the ΔG°.
d. It depend on the specific catalyst.
5. A rate constant is
a. the rate of a reaction at standard temperature and pressure.
b. the rate of a reaction at equilibrium.
c. a proportionality constant relating the rate of a reaction to the concentration(s) of the reactant(s).
d. a kind of transition state.
6. All catalysts work by lowering the activation energy for a reaction.

a. True
b. False
7. Thermodynamically favorable reactions all release energy.

a. True
b. False
8. The kinetic order of a reaction

a. can be determined by inspection from the coefficients of the balanced equation
b. must be determined experimentally
c. always depends on the concentration of enzyme
d. never depends on concentrations of reactants
9. First order kinetics means:

a. The rate of a reaction is independent of the amount of reactant measured.
b. The rate of the reaction varies directly with the amount of reactant measured.
c. The rate of the reaction varies with the square of the amount of the reactant measured.
d. More information is needed to answer this question.
e. None of these is correct.
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10. The substrate will only bind to the enzyme when the shapes fit together rigidly.
a. True
b. False
11. The E-S complex often shows as a slight depression in the energy profile for the reaction.
a. True
b. False
12. Which of the following is implied by induced fit between the enzyme's active site and the substrate?
a. The enzyme is a flexible molecule.
b. An enzyme will work equally well with different substrates.
c. An active site can bind to different substrates.
d. The enzyme is a flexible molecule so different substrates can bind.
e. All of these are correct
13. In the reaction catalyzed by chymotrypsin, a graph in which the rate is plotted against the concentration of
substrate
a. is sigmoidal, characteristic of an allosteric enzyme
b. shows that cooperative kinetics are observed
c. shows that the reaction is zero order
d. is hyperbolic, characteristic of a nonallosteric enzyme
14. The Michaelis-Menten approach to describing the kinetics of an enzyme-catalyzed reaction makes which of the
following assumptions about the conversion of product into substrate?
a. The product binds reversibly to the enzyme in order to be converted into the substrate.
b. The product is not converted to substrate to any appreciable extent.
c. The product is converted to substrate following simple first order kinetics.
d. The product is converted to substrate following simple second order kinetics.
15. According to the steady-state assumption

a. the product concentration does not change significantly
b. the substrate concentration is large and does not change significantly
c. the concentration of enzyme-substrate complex remains constant with time
d. the free enzyme concentration is always in great excess to the concentration of enzyme-substrate complex
16. When the substrate concentration is low, an enzyme reaction

a. will display zero-order kinetics.
b. will display first-order kinetics.
c. will display second-order kinetics.
d. will denature and cease to function.
17. The Michaelis constant is

a. related to the molecular weight of the enzyme
b. a measure of the resistance of the enzyme to denaturation
c. a reflection of the percentage of polar amino acids in the enzyme
d. a rough measure of the affinity of the enzyme for the substrate
18. Which of the following are related for a given enzyme?

a. Vmax, KM, and percentage of α-helix
b. Vmax, kcat, and percentage of β-sheet
c. Vmax, kcat, and turnover number
d. Vmax, KM, and molecular weight
e. None of these are related in any way
19. When an enzyme-catalyzed reaction has two substrates and substrate A must bind before substrate B, the
mechanism is called
a. a ping-pong mechanism
b. a random mechanism
c. an ordered mechanism
d. a suicide mechanism
e. none of these is true
20. A Lineweaver-Burk plot is useful in the analysis of enzymatic reactions because

a. it is easier to see whether points deviate from a straight line than from a curve
b. it is not affected by the presence of inhibitors
c. it can be used whether or not the enzyme displays Michaelis-Menten kinetics
d. all of the above
21. If the y-intercept of a Lineweaver-Burk plot = 1.91 (sec/millimole) and the slope = 75.3 L/sec, Vmax equals:
a. 0.0254 millimoles per second.
b. 0.523 millimoles per second.
c. 5.23 millimoles per second.
d. 39.4 millimoles per second.
e. 75.3 millimoles per second.
22. The Michaelis constant determines the Vmax of an enzymatic reaction.

a. True
b. False
23. In the following graph, which line best represents the Lineweaver-Burk plot obtained in the presence of a
competitive inhibitor?
a. A
b. B
c. C
d. D
e. E
24. "Hindrate" is an inhibitor of triose phosphate isomerase. When it is added to cells at a concentration of 0.1 nM,
the enzyme's KM for the substrate is unchanged, but the apparent Vmax is decreased to 50 nM/sec.
In the following graph, which line best represents the Lineweaver-Burk plot obtained in the presence of hindrate?

a. A
b. B
c. C
d. D
e. E
25. Competitive inhibitors have this effect:

a. Modifying the KM value.
b. Changing the value for Vmax.
c. Interfering with substrate binding.
d. This type of inhibitor both changes the KM and interferes with substrate binding.
e. All of these are correct.
26. Inhibitors can have the following effects on enzyme kinetics:

a. Modifying the KM value.
b. Changing the value for Vmax.
c. Interfering with substrate binding.
d. An inhibitor can change the KM and interfere with substrate binding.
e. All of these are correct.
27. The fundamental difference between competitive and noncompetitive inhibition is

a. the degree of cooperativity of the reaction
b. the size of the active site of the enzyme
c. the manner of binding of substrate to the enzyme
d. the manner of binding of inhibitor to the enzyme
28. For competitive inhibition

a. the value of KM decreases
b. the value of Vmax decreases
c. it is possible to overcome the effect of the inhibitor by increasing the concentration of substrate
d. none of the above
29. A noncompetitive inhibitor

a. binds to the enzyme at a site other than the active site
b. is structurally related to the substrate
c. does not affect the value of Vmax
d. decreases the value of KM
30. What effect is seen on a Lineweaver-Burk graph when a non-competitive inhibitor is added?
a. The y-intercept is changed, but not change the slope of the line.
b. The slope of the line is changed, but not the y-intercept.
c. Both the y-intercept and the slope of the line are changed.
d. Neither the y-intercept not the slope of the line is changed.
31. If an inhibitor changes the slope of the Lineweaver-Burk graph, but not the y-intercept, it is this type of inhibition:
a. Competitive.
b. Non-competitive.
c. Mixed Inhibition (uncompetitive inhibition).
d. You cannot tell from the data given.
e. More than one answer is correct.
32. Which of the following diseases has not been successfully treated using the principles of enzyme inhibition?
a. AIDS.
b. Lactose intolerance
c. Virus infection
d. Neither AIDS nor virus infection.
e. All of these have been successfully treated using enzyme inhibitors.
33. Which of the following is not related to the others?

a. Suicide Substrate
b. Irreversible Inhibitor
c. Trojan Horse substrate
d. Competitive Inhibitor
e. All of these are related
34. The rate of a zero-order reaction depends on the _____.

a. total number of reactants
b. concentration of products
c. concentration of reactants
d. presence of catalysts
35. What type of inhibitor is present in the data given above?

a. Competitive.
b. Non-competitive.
c. Uncompetitive.
d. You cannot tell from the data given.
e. More than one answer is correct.
36. What are the KM and Vmax values for the inhibited and uninhibited reactions for the data above? Upload your
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Chapter 06 - The Behavior of Proteins: Enzymes

2. The rate of a reaction depends on

3. The main difference between a catalyzed and an uncatalyzed reaction is that

4. What effect does a catalyst have on the ΔG° of a reaction?

6. All catalysts work by lowering the activation energy for a reaction.

7. Thermodynamically favorable reactions all release energy.

8. The kinetic order of a reaction

9. First order kinetics means:

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15. According to the steady-state assumption

16. When the substrate concentration is low, an enzyme reaction

17. The Michaelis constant is

18. Which of the following are related for a given enzyme?

20. A Lineweaver-Burk plot is useful in the analysis of enzymatic reactions because

22. The Michaelis constant determines the Vmax of an enzymatic reaction.

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25. Competitive inhibitors have this effect:

26. Inhibitors can have the following effects on enzyme kinetics:

27. The fundamental difference between competitive and noncompetitive inhibition is

28. For competitive inhibition

29. A noncompetitive inhibitor

33. Which of the following is not related to the others?

34. The rate of a zero-order reaction depends on the _____.

35. What type of inhibitor is present in the data given above?

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