Question 1

For a reaction A + B  →	o→  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

Accepted Answer

A)  sigmoidal.
B)  pseudo-first-order.
C)  unimolecular.
D)  zero-order.
E)  hyperbolic.

Question 2

A Lineweaver-Burk plot is also referred to as
(I) a sigmoidal plot.
(II) a linear plot.
(III) a Michaelis-Menten plot.
(IV) a double reciprocal plot.

Accepted Answer

A)  II
B)  II,III
C)  IV
D)  II,IV
E)  III,IV

Question 3

Based on the figure in the question above (question 54) ,which of the following expressions would correctly define KM?

Accepted Answer

A)  A= KM
B)  KM = A/2
C)  B = KM
D)  C = - KM
E)  D= 1/ KM

Question 4

Irreversible enzyme inhibitors

Accepted Answer

A)  inactivate the enzyme
B)  inhibit competitively
C)  maximize product by minimizing ES →	o→ E+S
D)  behave allosterically
E)  function via Ping Pong mechanism

Question 5

The Michaelis constant KM is defined as
(I) (k-1 + k2) /k1
(II) ½ Vmax
(III) [S] = [ES]
(IV) [ES]/2

Accepted Answer

A)  I
B)  I,II
C)  II
D)  I,IV
E)  II,IV

Question 6

Fourth-order reactions.

Accepted Answer

A)  have three or more sequential rate determining steps.
B)  require a 'Ping Pong' mechanism.
C)  are best analyzed using Lineweaver-Burk plots.
D)  exist only when enzymatically catalyzed.
E)  none of the above.

Question 7

Matching

-A common type of covalent modification of regulatory enzymes involves ______ of serine residues.

Accepted Answer

A)   isozymes
B)   [A] 
C)   the rate constant 
D)   Ping Pong
E)   bimolecularF)  ES complexG)  random ordered H)  competitive inhibitionI)  unimolecularJ)  [A]2K)  Competitive inhibitionL)  phosphorylation M)  small KSN)  large KS O)  uncompetitive inhibitionP)   [B]

Question 8

In order for an enzymatic reaction obeying the Michaelis-Menten equation to reach 3/4 of its maximum velocity,

Accepted Answer

A)  [S] would need to be equal to KM
B)  [S] would need to be ½ KM
C)  [S] would need to be 3KM
D)  [S] would need to be ¾ KM
E)  not enough information is given to make this calculation

Question 9

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)  M 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) KM = [0.006];Vmax = 0.0075/s B) KM = [0.196];Vmax = 0.0075/s C) KM = [165];Vmax = 33/s D) KM = [33];Vmax = 167/s E) KM = [270];Vmax x = 68/s" class="answers-bank-image d-inline" rel="preload" >

Accepted Answer

A)  KM = [0.006];Vmax = 0.0075/s
B)  KM = [0.196];Vmax = 0.0075/s
C)  KM = [165];Vmax = 33/s
D)  KM = [33];Vmax = 167/s
E)  KM = [270];Vmax x = 68/s

Question 10

The following questions refer to the diagram (with boxes where it has been left incomplete) : 
-This diagram refers to a (an)

Accepted Answer

A)  Ping Pong reaction.
B)  ordered bisubstrate reaction.
C)  random bisubstrate reaction.
D)  double order ping pong reaction
E)  X,Y,and Z must be provided in order to answer correctly C

Question 11

KM is

Accepted Answer

A)  a measure of the catalytic efficiency of the enzyme.
B)  equal to half of Vmax
C)  the rate constant for the reaction ES  →	o→  E + P.
D)  the [S] that half-saturates the enzyme.
E)  a ratio of substrate concentration relative to catalytic power.

Question 12

The KM can be considered to be the same as the dissociation constant KS for E + S binding if

Accepted Answer

A)  the concentration of [ES] is unchanged.
B)  ES  →	o→  E + P is fast compared to ES  →	o→  E + S.
C)  k1 >> k2
D)  k2 -1.
E)  this statement cannot be completed because KM can never approximate KS.

Question 13

In the plot below,can the KM be determined? If so,what is its value? M be determined? If so,what is its value?   A) Yes,it is 30 mM. B) Yes,it is 30 mM/sec. C) Yes,it is 60 mM/sec D) Yes,it is 60 mM E) No this data does not follow Michaelis-Menten kinetics" class="answers-bank-image d-inline" rel="preload" >

Accepted Answer

A)  Yes,it is 30 mM.
B)  Yes,it is 30 mM/sec.
C)  Yes,it is 60 mM/sec
D)  Yes,it is 60 mM
E)  No this data does not follow Michaelis-Menten kinetics

Question 14

[S] = KM for a simple enzymatic reaction.When [S] is doubled the initial velocity is

Accepted Answer

A)  2 Vmax
B)  equal to Vmax
C)  (1/3) Vmax
D)  0) 5 Vmax
E)  2 KM/[S]

Question 15

An enzyme is near maximum efficiency when

Accepted Answer

A)  its turnover number is near Vmax.
B)  kcat/KM is near 108 M-1s-1.
C)  k1 -1.
D)  kcat/KM is equal to kcat.
E)  KM is large when k2 exceeds k1. B

Question 16

Matching

-The type of enzyme inhibition in which Vmax is unaffected is ______.

Accepted Answer

A)   isozymes
B)   [A] 
C)   the rate constant 
D)   Ping Pong
E)   bimolecularF)  ES complexG)  random ordered H)  competitive inhibitionI)  unimolecularJ)  [A]2K)  Competitive inhibitionL)  phosphorylation M)  small KSN)  large KS O)  uncompetitive inhibitionP)   [B]

Question 17

From the graph below plotting data that was collected under steady state conditions,velocity on the y-axis in units of μM/s and substrate concentration of the x-axis in units of μM,what is the KM? M?   A) 0) 24 μM/s B) 18 μM C) 0) 2 μM D) 0) 24 μM E) 0) 12 μM/s" class="answers-bank-image d-inline" rel="preload" >

Accepted Answer

A)  0) 24 μM/s
B)  18 μM
C)  0) 2 μM
D)  0) 24 μM
E)  0) 12 μM/s B

Question 18

A new drug has been discovered which inhibits the reaction catalyzed by enzyme A.Based on the information shown below,what is this drug?

Accepted Answer

A)  competitive inhibitor
B)  uncompetitive inhibitor
C)  mixed inhibitor
D)  allosteric activator
E)  More information is required to answer the question.

Question 19

From the graph below plotting data that was collected under steady state conditions,velocity on the y-axis in units of μM/s and substrate concentration of the x-axis in units of μM,what is the Vmax? max?   A) 0) 24 μM/s B) 18 μM C) 0) 2 μM D) 0) 24 μM E) 0) 12 μM/s" class="answers-bank-image d-inline" rel="preload" >

Accepted Answer

A)  0) 24 μM/s
B)  18 μM
C)  0) 2 μM
D)  0) 24 μM
E)  0) 12 μM/s

Question 20

The following questions refer to the overall transformation shown in the following reaction: 1=k−1 B) implies that k−1 and k2 are such that the [ES] = k1[ES] C) [P]>>[E] D) [S] = [P] E) ES breakdown occurs at the same rate as ES formation" class="answers-bank-image d-inline" rel="preload" >
-For the reaction,the steady state assumption

Accepted Answer

A)  implies that k1=k−1
B)  implies that k−1 and k2 are such that the [ES] = k1[ES]
C)  [P]>>[E]
D)  [S] = [P]
E)  ES breakdown occurs at the same rate as ES formation

Exam 12: Enzyme Kinetics, inhibition and Control

For a reaction A + B →\to→ 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

Correct AnswerverifiedShow Answer

A Lineweaver-Burk plot is also referred to as (I) a sigmoidal plot. (II) a linear plot. (III) a Michaelis-Menten plot. (IV) a double reciprocal plot.

Correct AnswerverifiedShow Answer

Based on the figure in the question above (question 54) ,which of the following expressions would correctly define KM?

Correct AnswerverifiedShow Answer

Irreversible enzyme inhibitors

Correct AnswerverifiedShow Answer

The Michaelis constant KM is defined as (I) (k-1 + k2) /k1 (II) ½ Vmax (III) [S] = [ES] (IV) [ES]/2

Correct AnswerverifiedShow Answer

Fourth-order reactions.

Correct AnswerverifiedShow Answer

Matching -A common type of covalent modification of regulatory enzymes involves ______ of serine residues.

Correct AnswerverifiedShow Answer

In order for an enzymatic reaction obeying the Michaelis-Menten equation to reach 3/4 of its maximum velocity,

Correct AnswerverifiedShow Answer

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)

Correct AnswerverifiedShow Answer

The following questions refer to the diagram (with boxes where it has been left incomplete) : -This diagram refers to a (an)

Correct AnswerverifiedC

KM is

Correct AnswerverifiedShow Answer

The KM can be considered to be the same as the dissociation constant KS for E + S binding if

Correct AnswerverifiedShow Answer

In the plot below,can the KM be determined? If so,what is its value?

Correct AnswerverifiedShow Answer

[S] = KM for a simple enzymatic reaction.When [S] is doubled the initial velocity is

Correct AnswerverifiedShow Answer

An enzyme is near maximum efficiency when

Correct AnswerverifiedB

Matching -The type of enzyme inhibition in which Vmax is unaffected is ______.

Correct AnswerverifiedShow Answer

From the graph below plotting data that was collected under steady state conditions,velocity on the y-axis in units of μM/s and substrate concentration of the x-axis in units of μM,what is the KM?

Correct AnswerverifiedB

A new drug has been discovered which inhibits the reaction catalyzed by enzyme A.Based on the information shown below,what is this drug?

Correct AnswerverifiedShow Answer

From the graph below plotting data that was collected under steady state conditions,velocity on the y-axis in units of μM/s and substrate concentration of the x-axis in units of μM,what is the Vmax?

Correct AnswerverifiedShow Answer

The following questions refer to the overall transformation shown in the following reaction: -For the reaction,the steady state assumption

Correct AnswerverifiedShow Answer

For a reaction A + B $\to$ 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

Correct Answer
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Based on the figure in the question above (question 54) ,which of the following expressions would correctly define K_M?

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The Michaelis constant K_M is defined as (I) (k_-1+ k₂) /k₁ (II) ½ V_max (III) [S] = [ES] (IV) [ES]/2

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Determine the K_M and V_max 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)

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C

K_M is

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The K_M can be considered to be the same as the dissociation constant K_S for E + S binding if

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In the plot below,can the K_M be determined? If so,what is its value?

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[S] = K_M for a simple enzymatic reaction.When [S] is doubled the initial velocity is

Correct Answer
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B

Matching -The type of enzyme inhibition in which V_max is unaffected is ______.

Correct Answer
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From the graph below plotting data that was collected under steady state conditions,velocity on the y-axis in units of μM/s and substrate concentration of the x-axis in units of μM,what is the K_M?

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B

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From the graph below plotting data that was collected under steady state conditions,velocity on the y-axis in units of μM/s and substrate concentration of the x-axis in units of μM,what is the V_max?

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