Question 1

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 kineticsF) A) and B)
G) A) and C)

Question 2

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  →\rightarrow→  E + P is fast compared to ES  →\rightarrow→  E + S.
C)  k1 >> k2
D)  k2 -1.
E)  this statement cannot be completed because KM can never approximate KS. F) B) and D)
G) C) and D)

Question 3

The catalytic efficiency of an enzyme can never exceed

Accepted Answer

A)  k2.
B)  k1.
C)  k-1.
D)  k-1 + k2.
E)  (k-1 + k2) /k1.F) A) and E)
G) A) and D)

Question 4

Matching
-The E+S →\rarr→  E+P reaction is ______.

Accepted Answer

A)  isozymes
B)  [A]
C)  the rate constant
D)  Ping Pong
E)  bimolecularF) ES complexG) random orderedH) competitive inhibitionI) unimolecularJ) [A]²K) Competitive inhibitionL) phosphorylationM) small KSN) large KSO) uncompetitive inhibitionP) [B] Q) E) and H)
R) D) and O)

Question 5

Reaction that is first order with respect to A and B

Accepted Answer

A)  is dependent on the concentration of A and B.
B)  is dependent on the concentration of A.
C)  has smaller rate constants than first-order reactions regardless of reactant concentration.
D)  is independent of reactant concentration.
E)  is always faster than first-order reactions due to loss of concentration dependence.F) A) and B)
G) A) and C)

Question 6

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 orderedH) competitive inhibitionI) unimolecularJ) [A]²K) Competitive inhibitionL) phosphorylationM) small KSN) large KSO) uncompetitive inhibitionP) [B]Q) A) and M)
R) A) and O) L

Question 7

At substrate concentrations much lower than the enzyme concentration,

Accepted Answer

A)  the rate of reaction is expected to be inversely proportional to substrate concentration.
B)  the rate of reaction is expected to be directly proportional to substrate concentration.
C)  first order enzyme kinetics are not observed.
D)  the KM is lower.
E)  the rate of reaction is independent of substrate concentration.F) A) and B)
G) D) and E) B

Question 8

For a reaction A + B  →\rightarrow→  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. F) D) and E)
G) A) and E)

Question 9

Protein kinases are involved in

Accepted Answer

A)  the digestion of drugs to potentially toxic byproducts.
B)  the degradation of enzymes to the component amino acids.
C)  the phosphorylation of a wide variety of proteins.
D)  the metabolism of drugs to water soluble, excretable compounds.
E)  all of the aboveF) A) and C)
G) A) and B)

Question 10

Based on the figures below, which of the following expressions would be correct? max = 1/B B) C = 1/ Vmax C) D= Vmax D) D = 1/ Vmax E) A = 1/ Vmax" class="answers-bank-image d-inline" rel="preload" >

Accepted Answer

A)  Vmax = 1/B
B)  C = 1/ Vmax
C)  D= Vmax
D)  D = 1/ Vmax
E)  A = 1/ VmaxF) A) and D)
G) C) and D)

Question 11

Allosteric activators

Accepted Answer

A)  bind via covalent attachment.
B)  stabilize conformations with higher Ks.
C)  stabilize conformations with higher substrate affinity.
D)  all of the above
E)  none of the above.F) C) and D)
G) A) and B)

Question 12

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 calculationF) C) and D)
G) B) and D)

Question 13

Matching
-In uncompetitive inhibition, the inhibitor binds only to the ______.

Accepted Answer

A)  isozymes
B)  [A]
C)  the rate constant
D)  Ping Pong
E)  bimolecularF) ES complexG) random orderedH) competitive inhibitionI) unimolecularJ) [A]²K) Competitive inhibitionL) phosphorylationM) small KSN) large KSO) uncompetitive inhibitionP) [B]Q) A) and L)
R) H) and O) F

Question 14

Matching
-In ______, the inhibitor binds to a site involved in both substrate binding and catalysis.

Accepted Answer

A)  isozymes
B)  [A]
C)  the rate constant
D)  Ping Pong
E)  bimolecularF) ES complexG) random orderedH) competitive inhibitionI) unimolecularJ) [A]²K) Competitive inhibitionL) phosphorylationM) small KSN) large KSO) uncompetitive inhibitionP) [B]Q) G) and L)
R) E) and M)

Question 15

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?

Accepted Answer

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.F) A) and B)
G) None of the above

Question 16

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.F) C) and D)
G) A) and E)

Question 17

Find the initial velocity for an enzymatic reaction when Vmax = 6.5 × 10-5 mol•sec-1, [S] = 3.0 × 10-3 M, KM = 4.5 × 10-3 M and the enzyme concentration at time zero is 1.5 × 10-2  μ\muμ M.

Accepted Answer

A)  3.9 × 10-5 mol•sec-1
B)  2.6 × 10-5 mol•sec-1
C)  1.4 × 10-2 mol•sec-1
D)  8.7 × 10-3 mol•sec-1
E)  Not enough information is given to make this calculation. F) All of the above
G) A) and E)

Question 18

Parallel lines on a Lineweaver-Burk plot indicate
I.an increase in KM.
II.decrease in KM.
III.decrease in Vmax.
IV.uncompetitive inhibition.

Accepted Answer

A)  I, IV
B)  II, III, IV
C)  I or II, III
D)  I or III, II
E)  I, III, IVF) B) and D)
G) C) and E)

Question 19

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.

Accepted Answer

A)  I
B)  II
C)  III
D)  II, III
E)  I, II, IIIF) A) and E)
G) A) and D)

Question 20

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? 
max equals 200 M/s B) The Ks equals 500 M C) The kapp equals 200 per second D) The data was collected prior to reaching steady state. E) The kcat  cannot be determined for this information." class="answers-bank-image d-inline" rel="preload" >

Accepted Answer

A)  The Vmax equals 200 M/s
B)  The Ks equals 500 M
C)  The kapp equals 200 per second
D)  The data was collected prior to reaching steady state.
E)  The kcat  cannot be determined for this information.F) A) and B)
G) A) and D)

Exam 12: Enzyme Kinetics, Inhibition and Control

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

Correct Answer
verified

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

Correct Answer
verified

The catalytic efficiency of an enzyme can never exceed

Correct Answer
verified

Matching -The E+S $\rarr$ E+P reaction is ______.

Correct Answer
verified

Reaction that is first order with respect to A and B

Correct Answer
verified

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

Correct Answer
verified
L

At substrate concentrations much lower than the enzyme concentration,

Correct Answer
verified
B

For a reaction A + B $\rightarrow$ 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
verified

Protein kinases are involved in

Correct Answer
verified

Based on the figures below, which of the following expressions would be correct?

Correct Answer
verified

Allosteric activators

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

Correct Answer
verified

Matching -In uncompetitive inhibition, the inhibitor binds only to the ______.

Correct Answer
verified
F

Matching -In ______, the inhibitor binds to a site involved in both substrate binding and catalysis.

Correct Answer
verified

Correct Answer
verified

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 Answer
verified

Find the initial velocity for an enzymatic reaction when V_max = 6.5 × 10^-5 mol•sec^-1, [S] = 3.0 × 10^-3 M, K_M = 4.5 × 10^-3 M and the enzyme concentration at time zero is 1.5 × 10^-2 $\mu$ M.

Correct Answer
verified

Parallel lines on a Lineweaver-Burk plot indicate I.an increase in K_M. II.decrease in K_M. III.decrease in V_max. IV.uncompetitive inhibition.

Correct Answer
verified

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.

Correct Answer
verified

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?

Correct Answer
verified

Exam 12: Enzyme Kinetics, Inhibition and Control

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

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

The catalytic efficiency of an enzyme can never exceed

Correct AnswerverifiedShow Answer

Matching -The E+S →\rarr→ E+P reaction is ______.

Correct AnswerverifiedShow Answer

Reaction that is first order with respect to A and B

Correct AnswerverifiedShow Answer

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

Correct AnswerverifiedL

At substrate concentrations much lower than the enzyme concentration,

Correct AnswerverifiedB

For a reaction A + B →\rightarrow→ 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

Protein kinases are involved in

Correct AnswerverifiedShow Answer

Based on the figures below, which of the following expressions would be correct?

Correct AnswerverifiedShow Answer

Allosteric activators

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

Matching -In uncompetitive inhibition, the inhibitor binds only to the ______.

Correct AnswerverifiedF

Matching -In ______, the inhibitor binds to a site involved in both substrate binding and catalysis.

Correct AnswerverifiedShow Answer

Correct AnswerverifiedShow Answer

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

Find the initial velocity for an enzymatic reaction when Vmax = 6.5 × 10-5 mol•sec-1, [S] = 3.0 × 10-3 M, KM = 4.5 × 10-3 M and the enzyme concentration at time zero is 1.5 × 10-2 μ\muμ M.

Correct AnswerverifiedShow Answer

Parallel lines on a Lineweaver-Burk plot indicate I.an increase in KM. II.decrease in KM. III.decrease in Vmax. IV.uncompetitive inhibition.

Correct AnswerverifiedShow Answer

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.

Correct AnswerverifiedShow Answer

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?

Correct AnswerverifiedShow Answer

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

Correct Answer
verified

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

Correct Answer
verified

Correct Answer
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Matching -The E+S $\rarr$ E+P reaction is ______.

Correct Answer
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L

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B

For a reaction A + B $\rightarrow$ 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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Correct Answer
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Correct Answer
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Correct Answer
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Correct Answer
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F

Correct Answer
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Find the initial velocity for an enzymatic reaction when V_max = 6.5 × 10^-5 mol•sec^-1, [S] = 3.0 × 10^-3 M, K_M = 4.5 × 10^-3 M and the enzyme concentration at time zero is 1.5 × 10^-2 $\mu$ M.

Correct Answer
verified

Parallel lines on a Lineweaver-Burk plot indicate I.an increase in K_M. II.decrease in K_M. III.decrease in V_max. IV.uncompetitive inhibition.

Correct Answer
verified

Correct Answer
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Correct Answer
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