Chapter 12: Enzyme Kinetics, Inhibition and Control

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]

1. The E+S E+P reaction is ______.

Ans: E
Level of Difficulty: Easy
Section: 12.1.A
Learning objective: Reaction Kinetics
2. Assume a first order reaction, the rate of the reaction 2AB is dependent on ______.
Ans: B
Level of Difficulty: Easy
Section: 12.1.A
Learning objective: Reaction Kinetics
3. If AB is a zero-order reaction, the rate is dependent on ______.
Ans: C
Level of Difficulty: Easy
Section: 12.1.B
Learning objective: Reaction Kinetics
4. A two-substrate enzymatic reaction in which one product is produced before the second

substrate binds to the enzyme has a __ping pong____ mechanism.

Ans: D
Level of Difficulty: Easy
Section: 12.1.D
Learning objective: Reaction Kinetics
5. The type of enzyme inhibition in which Vmax is unaffected is ___competitive___.
Ans: K
Level of Difficulty: Moderate
Section: 12.2.A
Learning objective: Enzyme Inhibition
6. In uncompetitive inhibition, the inhibitor binds only to the __ES____.
Ans: F
Level of Difficulty: Moderate
Section: 12.2.B
Learning objective: Enzyme Inhibition
7. A common type of covalent modification of regulatory enzymes involves ______ of serine
residues.
Ans: L
Level of Difficulty: Moderate
Section: 12.3.B
Learning objective: Control of Enzyme Activity
8. A lead compound for a new drug should bind to its target protein with a very ______.
Ans: M
Level of Difficulty: Moderate
Section: 12.4.A
Learning objective: Drug Design

9. Different enzymes that catalyze the same reaction, although may be found in different tissues,

are known as ______.

Ans: A
Level of Difficulty: Easy
Section: 12.3.B
Learning objective: Control of Enzyme Activity
10. In ______, the inhibitor binds to a site involved in both substrate binding and catalysis.
Ans: H
Level of Difficulty: Easy
Section: 12.2.C
Learning objective: Enzyme Inhibition

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)

1.33 105 M-1sec-1

1.33 105 Msec
7.5 10-2 Msec
4.8 102 Msec-1
Not enough data are given to make this calculation

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)

is dependent on the concentration of A and B.

is dependent on the concentration of A.
has smaller rate constants than first-order reactions regardless of reactant concentration.
is independent of reactant concentration.
is always faster than first-order reactions due to loss of concentration dependence.

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)

a measure of the catalytic efficiency of the enzyme.

equal to half of Vmax
the rate constant for the reaction ES E + P.
the [S] that half-saturates the enzyme.
a ratio of substrate concentration relative to catalytic power.

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)

[S] would need to be equal to KM

[S] would need to be KM
[S] would need to be 3KM
[S] would need to be KM
not enough information is given to make this calculation

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)

the concentration of [ES] is unchanged.

ES E + P is fast compared to ES E + S.
k1 >> k2
k2 << k-1.
this statement cannot be completed because KM can never approximate KS.

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

19. An enzyme is near maximum efficiency when

A)
B)
C)
D)
E)

its turnover number is near Vmax.

kcat/KM is near 108 M-1s-1.
k1 << k-1.
kcat/KM is equal to kcat.
KM is large when k2 exceeds k1.

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)

3.9 105 molsec1

2.6 105 molsec1
1.4 102 molsec1
8.7 103 molsec1
Not enough information is given to make this calculation.

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)

inactivate the enzyme

inhibit competitively
maximize product by minimizing ESE+S
behave allosterically
function via Ping Pong mechanism

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)

have three or more sequential rate determining steps.

require a Ping Pong mechanism.
are best analyzed using Lineweaver-Burk plots.
exist only when enzymatically catalyzed.
none of the above.

Ans: E
Level of Difficulty: Moderate
Section: 12.1.A
Learning objective: Reaction Kinetics

27. Pseudo-first-order reaction kinetics would be observed for the reaction A + B C

A)
B)
C)
D)
E)

if [A] or [B] > [C].

if [C]>[A] and [C]>[B].
if [A] or [B] = 0.
if [C] = 0.
none of the above

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:

28. Which of the following is (are) true?

A)
B)
C)
D)
E)

The [ES] will remain constant if k2>k1 and k1< k2.

The reaction is zero order with respect to [S] if [S]>>[E]
It describes a double displacement reaction
All of the above are true.
None of the above is true.

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)

implies that k1=k1

implies that k1 and k2 are such that the [ES] = k1[ES]
[P]>>[E]
[S] = [P]
ES breakdown occurs at the same rate as ES formation

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):

32. This diagram refers to a (an)

A)
B)
C)
D)
E)

Ping Pong reaction.

ordered bisubstrate reaction.
random bisubstrate reaction.
double order ping pong reaction
X, Y, and Z must be provided in order to answer correctly

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)

X=A, Y=B, Z=P

X=B, Y=A, Z=Q
X=E, Y=A, Z=E
X=E, Y=B, Z=Q
X=E, Y=B, Z=P

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

35. Compounds that function as mixed inhibitors

I. interfere with substrate binding to the enzyme.

II. bind to the enzyme reversibly.
III. can bind to the enzyme/substrate complex.
A)
B)
C)
D)
E)

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

37. Allosteric activators

A)
B)
C)
D)
E)

bind via covalent attachment.

stabilize conformations with higher Ks.
stabilize conformations with higher substrate affinity.
all of the above
none of the above.

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)

the digestion of drugs to potentially toxic byproducts.

the degradation of enzymes to the component amino acids.
the phosphorylation of a wide variety of proteins.
the metabolism of drugs to water soluble, excretable compounds.
all of the above

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)

Phase 1; single blind

Phase 1; double blind
Phase 2; single blind
Phase 2; double blind
Phase 3; double blind

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)

KM = [0.006]; Vmax = 0.0075/s

KM = [0.196]; Vmax = 0.0075/s
KM = [165]; Vmax = 33/s
KM = [33]; Vmax = 167/s
KM = [270]; Vmax x = 68/s

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

Learning objective: Enzyme Inhibition

42. An extremely efficient enzyme called efficase catalyzes the conversion of A to B. A
researcher decides to mutate the enzyme in order to try to improve its performance. Following
active site mutations, a significant reduction in the value of KM and Vmax was observed. Which of
the following may have occurred?
A) The affinity of the enzyme for the substrate was increased to a point which did not favor
propagation (continuation) of the reaction.
B) The decrease in Vmax was not related to the decrease in KM.
C) If the reaction was first-order, the change in KM cannot have affected Vmax.
D) The stability of E+S (E+A as written above) was increased, thereby increasing the KM.
E) The reverse reaction (breakdown of EA to E+A) was favored, slowing the Vmax.
Ans: E
Level of Difficulty: Very Difficult
Section: 12.1.B
Learning objective: Reaction Kinetics
43. Enzyme E is responsible for conversion of substrate X to product U. As a result of this
conversion electrons are transported to a coenzyme (FAD) within Enzyme E. In order for the
reaction to be completed, a second substrate NAD+ must also bind Enzyme E and collect stored
electrons (which converts it to product, NADH). The graph below shows the data while varying
X, with fixed concentrations of NAD+. What type of multi-substrate mechanism does enzyme E
utilize?

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)

- 0.002 (Units on the x-axis are 1/M)

0.005 (Units on the y-axis are 1/s)
2.50

The Vmax equals 200 M/s

The Ks equals 500 M
The kapp equals 200 per second
The data was collected prior to reaching steady state.
The kcat cannot be determined for this information.

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

can you determine from this graph?

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)

is the concentration of substrate where the enzyme achieves Vmax.

is equal to Ks.
measures the stability of the product
is high if the enzyme has high affinity for the substrate.
All of the above are correct.

Ans: A
Level of Difficulty: Easy
Section: 12.1.B
Learning objective: Reaction Kinetics

48. At substrate concentrations much lower than the enzyme concentration,

A)
B)
C)
D)
E)

the rate of reaction is expected to be inversely proportional to substrate concentration.

the rate of reaction is expected to be directly proportional to substrate concentration.
first order enzyme kinetics are not observed.
the KM is lower.
the rate of reaction is independent of substrate concentration.

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

Level of Difficulty: Difficult

Section: 12.1.B
Learning objective: Reaction Kinetics
53. Based on the figures below, which of the following expressions would be correct?

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

on the information shown below, what is this drug?

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