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Chapter 14: Rates of Enzymatic Reactions

Matching
A)
B)
C)
D)
E)
F)
G)
H)
I)
J)
K)
L)
M)

isozymes
substrate binding
rate constant
Ping Pong
bimolecular
ES complex
large KD
mixed inhibition
unimolecular
[A]2
competitive inhibition
phosphorylation
small KD

1. The 2AB reaction is ______.


Ans: E
Level of Difficulty: Easy
Section: 14-1. Chemical Kinetics
2. The rate of the reaction 2AB is dependent on ______.
Ans: J
Level of Difficulty: Easy
Section: 14-1. Chemical Kinetics
3. A zero-order reaction's rate is dependent on the ______.
Ans: C
Level of Difficulty: Easy
Section: 14-1. Chemical Kinetics
4. A two-substrate enzymatic reaction in which one product is produced before the second
substrate binds to the enzyme has a ______ mechanism.

Ans: D
Level of Difficulty: Easy
Section: 14-5. Bisubstrate Reactions
5. The type of enzyme inhibition in which Vmax is unaffected is ______.
Ans: K
Level of Difficulty: Moderate
Section: 14-3. Inhibition
6. In uncompetitive inhibition, the inhibitor binds only to the ______.
Ans: F
Level of Difficulty: Moderate
Section: 14-3. Inhibition
7. In ______, the inhibitor binds to a site involved in both substrate binding and catalysis.
Ans: H
Level of Difficulty: Easy
Section: 14-3. Inhibition

Multiple Choice
8. What is the velocity of a first-order reaction when the reactant concentration is 6 x 10-2 M and
the rate constant is 8 x 103 sec-1?
A) 1.33 x 105 M-1sec-1
B) 1.33 x 105 Msec
C) 7.5 x 10-2 Msec
D) 4.8 x 102 Msec-1
E) not enough data are given to make this calculation
Ans: D
Level of Difficulty: Moderate
Section: 14-1. Chemical Kinetics
9. Second-order reactions:
A) occur when two reactants collide.
B) are quite rare.
C) have smaller rate constants than first-order reactions.
D) are termolecular.
E) are always faster than first-order reactions.

Ans: A
Level of Difficulty: Easy
Section: 14-1. Chemical Kinetics
10. 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) sigmoidal
B) pseudo-first-order
C) unimolecular
D) zero-order
E) enzymatic
Ans: B
Level of Difficulty: Easy
Section: 14-1. Chemical Kinetics
11. KM is:
A) a measure of the catalytic efficiency of the enzyme.
B) the rate at which the enzyme dissociates from the substrate.
C) the rate constant for the reaction ES E + P.
D) the [S] that half-saturates the enzyme.
E) the rate at which the enzyme binds the substrate.
Ans: D
Level of Difficulty: Easy
Section: 14-2. Enzyme Kinetics
12. In order for an enzymatic reaction obeying the Michaelis-Menten equation to reach 3/4 of its
maximum velocity,
A) [S] would need to be 2KM
B) not enough information is given to make this calculation
C) [S] would need to be 50% greater than KM
D) [S] would need to be 3KM
E) [S] would need to be 3/4KM
Ans: D
Level of Difficulty: Moderate
Section: 14-2. Enzyme Kinetics
13. The KM can be considered to be the same as the dissociation constant KS for E + S binding if:
A) this statement cannot be completed because KM can never approximate KS.

B)
C)
D)
E)

ES E + P is fast compared to ES E + S.
the turnover number is very large.
k2 << k-1.
kcat/KM is near the diffusion-controlled limit.

Ans: D
Level of Difficulty: Difficult
Section: 14-2. Enzyme Kinetics
14. Find kcat for a reaction in which Vmax is 4 x 10-4 molmin-1 and the reaction mixture contains
one microgram of enzyme (the molecular weight of the enzyme is 200,000 D).
A) 2 x 10-11 min-1
B) 8 x 107 min-1
C) 8 x 109 min-1
D) 2 x 10-14 min-1
E) 4 x 108 min-1
Ans: B
Level of Difficulty: Difficult
Section: 14-2. Enzyme Kinetics
15. An enzyme is considered to have evolved to its most efficient form if
A) kcat is a large number
B) kcat/KM is near the diffusion-controlled limit
C) KM is a large number
D) kcat/KM is a very small number
E) KM is a small number
Ans: B
Level of Difficulty: Easy
Section: 14-2. Enzyme Kinetics
16. Find the initial velocity for an enzymatic reaction when Vmax = 6.5 x 105 molsec1, [S] = 3.0
x 103 M, and KM = 4.5 x 103 M.
A) not enough information is given to make this calculation
B) 2.6 x 105 molsec1
C) 1.4 x 102 molsec1
D) 8.7 x 103 molsec1
E) 3.9 x 105 molsec1
Ans: B
Level of Difficulty: Moderate
Section: 14-2. Enzyme Kinetics

17. When [S] = KM, 0 = _____Vmax.


A) 2
B) 1
C) 0.67
D) 0.5
E) 0.1
Ans: D
Level of Difficulty: Easy
Section: 14-2. Enzyme Kinetics
18. [S] = KM for a simple enzymatic reaction. When [S] is doubled, the rate becomes
_____ Vmax.
A) 2
B) 1
C) 0.67
D) 0.5
E) 0.1
Ans: C
Level of Difficulty: Easy
Section: 14-2. Enzyme Kinetics
19. Irreversible enzyme inhibitors are also called:
A) inactivators.
B) covalent substrates.
C) product inhibitors.
D) allosteric effectors.
E) Ping Pong inhibitors.
Ans: A
Level of Difficulty: Easy
Section: 14-3. Inhibition
20. A Lineweaver-Burk plot is also called:
A) a sigmoidal plot
B) a linear plot
C) a doubledisplacement plot
D) a MichaelisMenten plot
E) a double reciprocal plot
Ans: E
Level of Difficulty: Easy

Section: 14-2. Enzyme Kinetics


21. Parallel lines on a Lineweaver-Burk plot are diagnostic of:
A) competitive inhibition.
B) non-competitive inhibition.
C) allosteric activation.
D) allosteric inhibition.
E) none of the above.
Ans: B
Level of Difficulty: Easy
Section: 14-3. Inhibition
22. Fourth-order reactions:
A) have three or more sequential rate determining steps.
B) require a Ping Pong mechanism.
C) are best analyzed using Lineweaver-Burk plots.
D) are unknown.
E) none of the above.
Ans: D
Level of Difficulty: Moderate
Section: 14-1. Chemical Kinetics
23. If the half-life of a given reaction is constant (not dependant upon the initial conditions), the
reaction must be:
A) zeroth order
B) first order
C) second order
D) diffusion controlled
E) enzyme catalyzed
Ans: B
Level of Difficulty: Easy
Section: 14-1. Chemical Kinetics
24. Pseudo-first-order reaction kinetics would be observed for the reaction A + B C:
A) if [A]=[B]
B) if [C]>[A] and [C]>[B]
C) if [A] or [B] = 0
D) if [C] = 0
E) none of the above

Ans: E
Level of Difficulty: Easy
Section: 14-1. Chemical Kinetics
The following questions refer to the overall transformation:

25. The overall transformation


A) is composed of two elementary reactions.
B) can be zeroth order in [S] if [S]>>[E]
C) may be described by the Michaelis-Menten equation if certain assumptions are made
D) all of the above
E) none of the above
Ans: D
Level of Difficulty: Easy
Section: 14-2. Enzyme Kinetics
26. For the reaction, the steady state assumption assumes that
A) [S] = [P]
B) [ES] is constant
C) [P]>>[E]
D) [P] is constant
E) k1>>k2
Ans: B
Level of Difficulty: Easy
Section: 14-2. Enzyme Kinetics
27. The Michaelis constant KM is defined as
A) (k1 + k2)/k1
B) (k1 + k1)/k2
C) ([P] + [E])/[ES]
D) [ES]
E) none of the above
Ans: A
Level of Difficulty: Easy
Section: 14-2. Enzyme Kinetics
28. The most efficient enzymes have kcat/KM values that approach

A)
B)
C)
D)
E)

k2
k1
k1
k1 + k2
1012 Ms1

Ans: B
Level of Difficulty: Easy
Section: 14-2. Enzyme Kinetics
The following questions refer to the diagram (with boxes where it has been left incomplete):

29. This diagram refers to a:


A) Ping Pong reaction.
B) ordered bisubstrate reaction.
C) random bisubstrate reaction.
D) double displacement reaction.
E) not enough information is provided.
Ans: C
Level of Difficulty: Easy
Section: 14-5. Bisubstrate Reactions
30. Which reactant/product should be in the box labeled with a Z?
A) A
B) B
C) P
D) Q
E) E
Ans: D
Level of Difficulty: Easy
Section: 14-5. Bisubstrate Reactions

31. A compound that reduces the concentration of enzyme available for substrate binding is
called:
A) a transition-state analog
B) a non-competitive inhibitor
C) an allosteric effector
D) an enzyme inactivator
E) a competitive inhibitor
Ans: E
Level of Difficulty: Easy
Section: 14-3. Inhibition
32. Compounds that function as mixed inhibitors
A) interfere with substrate binding to the enzyme
B) bind to the enzyme reversibly
C) can bind to the enzyme/substrate complex
D) all of the above
E) none of the above
Ans: D
Level of Difficulty: Easy
Section: 14-3. Inhibition