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Matching
A)
B)
C)
D)
E)
F)
G)
H)
I)
J)
K)
L)
M)
N)
O)
P)
isozymes
[A]
the rate constant
Ping Pong
bimolecular
ES complex
random ordered
competitive inhibition
unimolecular
[A]2
competitive inhibition
phosphorylation
small KS
large KS
uncompetitive inhibition
[B]
9. Different enzymes that catalyze the same reaction, although may be found in different tissues,
Multiple Choice
11. A lead compound would be most promising if it had:
A)
B)
C)
D)
E)
KI = 4.7 105 M.
KI = 1.5 108 M.
KI = 1.5 10-8 M.
KI = 4.7 10-5 M.
KM = 4.7 105 M.
Ans: C
Level of Difficulty: Moderate
Section: 12.4.A
Learning objective: Drug Design
12. What is the velocity of a first-order reaction at 37oC when the reactant concentration is 6
10-2 M and the rate constant is 8 103 sec-1?
A)
B)
C)
D)
E)
Ans: D
Level of Difficulty: Moderate
Section: 12.1.A
Learning objective: Reaction Kinetics
13. Reaction that is first order with respect to A and B
A)
B)
C)
D)
E)
Ans: A
Level of Difficulty: Moderate
Section: 12.1.A
Learning objective: Reaction Kinetics
14. For a reaction A + B C, if the concentration of B is much larger than A so that [B] remains
constant during the reaction while [A] is varied, the kinetics will be
A)
B)
C)
D)
E)
sigmoidal.
pseudo-first-order.
unimolecular.
zero-order.
hyperbolic.
Ans: B
Level of Difficulty: Easy
Section: 12.1.A
Learning objective: Reaction Kinetics
15. KM is
A)
B)
C)
D)
E)
Ans: D
Level of Difficulty: Moderate
Section: 12.1.B
Learning objective: Reaction Kinetics
16. In order for an enzymatic reaction obeying the Michaelis-Menten equation to reach 3/4 of its
maximum velocity,
A)
B)
C)
D)
E)
Ans: C
Level of Difficulty: Moderate
Section: 12.1.C
Learning objective: Reaction Kinetics
17. The KM can be considered to be the same as the dissociation constant KS for E + S binding if
A)
B)
C)
D)
E)
Ans: D
Level of Difficulty: Difficult
Section: 12.1.C
Learning objective: Reaction Kinetics
18. Find kcat for a reaction in which Vmax is 4 10-4 molmin-1 and the reaction mixture contains
one microgram of enzyme (the molecular weight of the enzyme is 200,000 D).
A)
B)
C)
D)
E)
2 10-11 min-1
8 107 min-1
8 109 min-1
2 10-14 min-1
4 108 min-1
Ans: B
Level of Difficulty: Difficult
Section: 12.1.C
Learning objective: Reaction Kinetics
A)
B)
C)
D)
E)
Ans: B
Level of Difficulty: Easy
Section: 12.1.C
Learning objective: Reaction Kinetics
20. Find the initial velocity for an enzymatic reaction when Vmax = 6.5 105 molsec1, [S] =
3.0 103 M, KM = 4.5 103 M and the enzyme concentration at time zero is 1.5 10-2 M.
A)
B)
C)
D)
E)
Ans: B
Level of Difficulty: Moderate
Section: 12.1.C
Learning objective: Reaction Kinetics
21. When [S] = KM, 0 = (_____) (Vmax).
A)
B)
C)
D)
E)
[S]
0.75
0.5
KM
kcat
Ans: C
Level of Difficulty: Moderate
Section: 12.1.A
Learning objective: Reaction Kinetics
22. [S] = KM for a simple enzymatic reaction. When [S] is doubled the initial velocity is
A)
B)
C)
D)
E)
2 Vmax
equal to Vmax
(1/3) Vmax
0.5 Vmax
2 KM/[S]
Ans: C
Level of Difficulty: Moderate
Section: 12.1.C
Learning objective: Reaction Kinetics
23. Irreversible enzyme inhibitors
A)
B)
C)
D)
E)
Ans: A
Level of Difficulty: Easy
Section: 12.2.C
Learning objective: Enzyme Inhibition
24. A Lineweaver-Burk plot is also referred to as
I. a sigmoidal plot.
II. a linear plot.
III. a MichaelisMenten plot.
IV. a double reciprocal plot.
A)
B)
C)
D)
E)
II
II, III
IV
II, IV
III, IV
Ans: D
Level of Difficulty: Moderate
Section: 12.1.C
Learning objective: Reaction Kinetics
25. Parallel lines on a Lineweaver-Burk plot indicate
I. an increase in KM.
II. decrease in KM.
III. decrease in Vmax.
IV. uncompetitive inhibition.
A)
B)
C)
D)
E)
I, IV
II, III, IV
I or II, III
I or III, II
I, III, IV
Ans: C
Level of Difficulty: Difficult
Section: 12.2.B
Learning objective: Enzyme Inhibition
26. Fourth-order reactions.
A)
B)
C)
D)
E)
Ans: E
Level of Difficulty: Moderate
Section: 12.1.A
Learning objective: Reaction Kinetics
A)
B)
C)
D)
E)
Ans: E
Level of Difficulty: Easy
Section: 12.1.A
Learning objective: Reaction Kinetics
The following questions (29 and 30) refer to the overall transformation shown in the following
reaction:
Ans: B
Level of Difficulty: Difficult
Section: 12.1.B
Learning objective: Reaction Kinetics
29. For the reaction, the steady state assumption
A)
B)
C)
D)
E)
Ans: E
Level of Difficulty: Difficult
Section: 12.1.B
Learning objective: Reaction Kinetics
30. The Michaelis constant KM is defined as
I. (k1 + k2)/k1
II. Vmax
III. [S] = [ES]
IV. [ES]/2
A)
B)
C)
D)
E)
I
I, II
II
I, IV
II, IV
Ans: A
Level of Difficulty: Easy
Section: 12.1.B
Learning objective: Reaction Kinetics
31. The catalytic efficiency of an enzyme can never exceed
A)
B)
C)
D)
E)
k2.
k1.
k1.
k1 + k2.
(k1 + k2)/k1.
Ans: B
Level of Difficulty: Easy
Section: 12.1.B
Learning objective: Reaction Kinetics
The following questions (33 and 34) refer to the diagram (with boxes where it has been left
incomplete):
A)
B)
C)
D)
E)
Ans: C
Level of Difficulty: Easy
Section: 12.1.D
Learning objective: Reaction Kinetics
33. Which of the following is correct in regards to the diagram above?
A)
B)
C)
D)
E)
Ans: B
Level of Difficulty: Moderate
Section: 12.1.D
Learning objective: Reaction Kinetics
34. A compound that distorts the active site, rendering the enzyme catalytically inactive is
called
A)
B)
C)
D)
E)
a uncompetitive inhibitor
an allosteric effector
an inactivator
a competitive inhibitor
none of the above
Ans: D
Level of Difficulty: Easy
Section: 12.2.B
Learning objective: Enzyme Inhibition
I
II
III
II, III
I, II, III
Ans: E
Level of Difficulty: Easy
Section: 12.2.C
Learning objective: Enzyme Inhibition
36. Enzyme activity in cells is controlled by which of the following?
I. covalent modifications
II. modulation of expression levels
III. feedback inhibition
IV. allosteric effectors
A) I
B) II
C) III
D) III, IV
E) I, II, III, IV
Ans: E
Level of Difficulty: Easy
Section: 12.3
Learning objective: Control of Enzyme Activity
A)
B)
C)
D)
E)
Ans: C
Level of Difficulty: Easy
Section: 12.3.A
Learning objective: Control of Enzyme Activity
38. Protein kinases are involved in
A)
B)
C)
D)
E)
Ans: C
Level of Difficulty: Easy
Section: 12.3.B
Learning objective: Control of Enzyme Activity
39. ________ clinical trials are focused on evaluating the efficacy of new drug candidates, and
usually use _____ test.
A)
B)
C)
D)
E)
Ans: C
Level of Difficulty: Easy
Section: 12.4.C
Learning objective: Drug Design
40. Determine the KM and Vmax from the following graph. (Note: On the x-axis the minor tick
mark spacing is 0.005; on the y-axis the minor tick mark spacing is 0.002)
A)
B)
C)
D)
E)
Ans: D
Level of Difficulty: Moderate
Section: 12.1.C
Learning objective: Reaction Kinetics
41. I propose to design a new drug which will act as an inhibitor for an enzyme. If I have used
all current information about the mechanism of this enzyme to design this inhibitor and I
carefully engineer it with similar chemical properties of the transition state, what type of
inhibitor am I attempting to engineer and how will I know if I have succeeded?
A) A competitive inhibitor, collect kinetic data both in the presence and absence of inhibitor and
watch for a change in Vmax.
B) A competitive inhibitor, collect kinetic data both in the presence and absence of inhibitor and
watch for a change in KM.
C) A uncompetitive inhibitor, collect kinetic data both in the presence and absence of inhibitor
and watch for a change in KM.
D) A uncompetitive inhibitor, collect kinetic data both in the presence and absence of inhibitor
and watch for a change in Vmax.
E) None of the above.
Ans: A
Level of Difficulty: Difficult
Section: 12.2.A
Substrates:
Products:
A)
B)
C)
D)
E)
NAD+
NADH
sequential Ordered
sequential Random
simultaneous addition
Ping Pong
Sequential but the data cannot differentiate between ordered and random.
Ans: B
Level of Difficulty: Very Difficult
Section: 12.2.B
Learning objective: Reaction Kinetics
44. The following data were collected under conditions indicated in the graph below during the
time period of 0-5 seconds. Upon plotting the Lineweaver-Burk plot, the information given in
the table below was determined. Based on this available information which of the following is
FALSE?
x-intercept
y-intercept
slope
A)
B)
C)
D)
E)
Ans: A
Level of Difficulty: Difficult
Section: 12.1.B
Learning objective: Reaction Kinetics
45. In the plot below, can the KM be determined? If so, what is its value?
A)
B)
C)
D)
E)
Yes, it is 30 mM.
Yes, it is 30 mM/sec.
Yes, it is 60 mM/sec
Yes, it is 60 mM
No this data does not follow Michaelis-Menten kinetics
Ans: A
Level of Difficulty: Difficult
Section: 12.1.B
Learning objective: Reaction Kinetics
46. Following several experiments, the data presented on the graph below was obtained. What
A) This data may have been collected both in the absence (solid line) and presence (dashed
line) of a competitive inhibitor.
B) This data may have been collected both in the absence (solid line) and presence (dashed
line) of a mixed (noncompetitive) inhibitor.
C) This data may have been collected both in the absence (solid line) and presence (dashed
line) of mechanism based inhibitor.
D) This data may have been collected both in the absence (solid line) and presence (dashed line)
of an inhibitor which binds the active site.
E) More than one of the above are correct.
Ans: B
Level of Difficulty: Difficult
Section: 12.2.A, B, C
Learning objective: Enzyme Inhibition
47. KM
A)
B)
C)
D)
E)
Ans: A
Level of Difficulty: Easy
Section: 12.1.B
Learning objective: Reaction Kinetics
A)
B)
C)
D)
E)
Ans: B
Level of Difficulty: Difficult
Section: 12.1.B
Learning objective: Reaction Kinetics
49. The breakdown of dopamine is catalyzed by the enzyme monoamine oxidase (MAO). What
is the final concentration of product if the starting dopamine concentration is 0.050 M and the
reaction runs for 5 seconds. (Assume the rate constant for the reaction is 0.249 s1.)
A)
B)
C)
D)
E)
0.050 M
0.014 M
0.018 M
1.2 M
0.025 M
Ans: B
Level of Difficulty: Moderate
Section: 12.1.A
Learning objective: Reaction Kinetics
50. A lab recently developed a new drug which is hypothesized to inhibit the enzyme
cyclooxygenase-2 (COX-2) and reduce inflammation. In their first test they monitored the
reaction of substrate as it is converted to product in the presence of the new drug (data shown
below). If the hypothesis is correct the observed initial rate will be at least 2 times slower than
the normal reaction without the drug. If the normal initial rate is 30 mM/s, does the data below
indicate that the team has designed a successful inhibitor?
A)
B)
C)
D)
E)
Yes.
No.
This cannot be determined with the information given.
The data is dependent on the maximal velocity.
The answer is dependent on the substrate concentration.
Ans: A
Level of Difficulty: Difficult
Section: 12.1.A
Learning objective: Reaction Kinetics
51. From the graph below plotting data that was collected under steady state conditions, velocity
on the y-axis in units of M/s and substrate concentration of the x-axis in units of M, what is the
Vmax?
A)
B)
C)
D)
E)
0.24 M/s
18 M
0.2 M
0.24 M
0.12 M/s
Ans: A
Level of Difficulty: Difficult
Section: 12.1.B
Learning objective: Reaction Kinetics
52. From the graph below plotting data that was collected under steady state conditions,
velocity on the y-axis in units of M/s and substrate concentration of the x-axis in units of M,
what is the KM?
A)
B)
C)
D)
E)
0.24 M/s
18 M
0.2 M
0.24 M
0.12 M/s
Ans: B
A)
B)
C)
D)
E)
Vmax = 1/B
C = 1/ Vmax
D= Vmax
D = 1/ Vmax
A = 1/ Vmax
Ans: D
Level of Difficulty: Moderate
Section: 12.1.B
Learning objective: Reaction Kinetics
54. Based on the figure in the question above (question 54), which of the following expressions
would correctly define KM?
A) A= KM
B) KM = A/2
C) B = KM
D) C = - KM
E) D= 1/ KM
Ans: C
Level of Difficulty: Moderate
Section: 12.1.B
Learning objective: Reaction Kinetics
55. A new drug has been discovered which inhibits the reaction catalyzed by enzyme A. Based
A)
B)
C)
D)
E)
competitive inhibitor
uncompetitive inhibitor
mixed inhibitor
allosteric activator
More information is required to answer the question.
Ans: A
Level of Difficulty: Moderate
Section: 12.2.A
Learning objective: Enzyme Inhibition