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