Question 1

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 
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 2

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. 
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 3

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?

Accepted Answer

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

Question 4

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 
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 5

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)  bimolecular
F) ES complex
G) random ordered 
H) competitive inhibition
I) unimolecular
J) [A]2
K) Competitive inhibition
L) phosphorylation 
M) small KS
N) large KS 
O) uncompetitive inhibition
P)  [B] 
A)  isozymes 
B)  [A] 
C)  the rate constant 
D)  Ping Pong 
E)  bimolecular
F) ES complex
G) random ordered 
H) competitive inhibition
I) unimolecular
J) [A]2
K) Competitive inhibition
L) phosphorylation 
M) small KS
N) large KS 
O) uncompetitive inhibition
P)  [B]

Question 6

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

Accepted Answer

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

Question 7

Irreversible enzyme inhibitors

Accepted Answer

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

Question 8

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

Question 9

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?

Accepted Answer

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

Question 10

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

Question 11

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

Question 12

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)

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 
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 13

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

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 
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

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)  bimolecular
F) ES complex
G) random ordered 
H) competitive inhibition
I) unimolecular
J) [A]2
K) Competitive inhibition
L) phosphorylation 
M) small KS
N) large KS 
O) uncompetitive inhibition
P)  [B] 
A)  isozymes 
B)  [A] 
C)  the rate constant 
D)  Ping Pong 
E)  bimolecular
F) ES complex
G) random ordered 
H) competitive inhibition
I) unimolecular
J) [A]2
K) Competitive inhibition
L) phosphorylation 
M) small KS
N) large KS 
O) uncompetitive inhibition
P)  [B]

Question 15

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. 
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 16

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

Question 17

The following questions refer to the overall transformation shown in the following reaction:  
-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 
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

Question 18

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

Question 19

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

Question 20

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

Exam 12: Enzyme Kinetics, inhibition and Control

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

An enzyme is near maximum efficiency when

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?

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

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

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

Irreversible enzyme inhibitors

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

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?

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

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.

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)

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

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

Fourth-order reactions.

KM is

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

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

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

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

Introduction to the Chemistry of Life

Water

Nucleotides, nucleic Acids, and Genetic Information

Amino Acids

Proteins: Primary Structure

Proteins: Three-Dimensional Structure

Protein Function Part I: Myoglobin and Hemoglobin

Carbohydrates

Lipids and Biological Membranes

Membrane Transport

Enzyme Catalysis

Biochemical Signaling

Introduction to Metabolism

Glucose Catabolism

Glycogen Metabolism and Gluconeogenesis

Citric Acid Cycle

Electron Transport and Oxidative Phosphorylation

Photosynthesis

Lipid Metabolism

Amino Acid Metabolism

Mammalian Fuel Metabolism: Integration and Regulation

Nucleotide Metabolism

Nucleic Acid Structure

DNA Replication, repair and Recombination

Transcription and Rna Processing

Protein Synthesis

Regulation of Gene Expression

Filters

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?

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

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

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?

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

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)

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

K_M is

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

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

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