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Home
‣
Biochemical Engineering
‣
Enzymes and Kinetics
Comments
Question
When substrate [S] = K
M
(Michaelis-Menten constant), the velocity of an enzyme catalyzed reaction is about
Options
A. 0.1 * V
max
B. 0.2 * V
max
C. 0.5 * V
max
D. 0.9 * V
max
Correct Answer
0.5 * V
max
Enzymes and Kinetics problems
Search Results
1. Predominantly uncompetitive inhibition may be called when
Options
A. competitive inhibition is greater than uncompetitive inhibition
B. competitive inhibition is smaller than uncompetitive inhibition
C. competitive inhibition is equal to uncompetitive inhibition
D. none of the above
Show Answer
Scratch Pad
Discuss
Correct Answer: competitive inhibition is greater than uncompetitive inhibition
2. Which category of enzymes belongs to class 5 in the international classification?
Options
A. Hydrolases
B. Isomerases
C. Oxido-reductases
D. Cyclase
Show Answer
Scratch Pad
Discuss
Correct Answer: Isomerases
3. The ratio of the amount of a protein present in a sample, which is used as a measure of purification, is known as
Options
A. specific activity
B. relative activity
C. purity ratio
D. all of these
Show Answer
Scratch Pad
Discuss
Correct Answer: specific activity
4. Which of the following step is assumed to be the slowest step in the Michaelis Menten equation?
Options
A. The substrate consuming step
B. The product releasing step
C. Formation of enzyme substrate complex
D. None of these
Show Answer
Scratch Pad
Discuss
Correct Answer: The product releasing step
5. If a reaction occurs in the absence of inhibitor with rate ?
0
and in the presence of inhibitor with rate ?
i
, the degree of inhibition is defined as
Options
A. (?
0
- ?
i
)/?
0
B. (?
0
+ ?
i
)/?
0
C. (?
0
?
i
)/?
0
D. (?
0
-?
i
)/?
i
Show Answer
Scratch Pad
Discuss
Correct Answer: (?
0
- ?
i
)/?
0
6. A classical noncompetitive inhibitor has
Options
A. no effect on substrate binding
B. no effect on substrate binding and vice versa
C. significant effect on substrate binding
D. significant effect on substrate binding and vice versa
Show Answer
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Discuss
Correct Answer: no effect on substrate binding and vice versa
7. The rate equation in non-competitive inhibition based on Michaelis Menten equation is given by
Options
A. r
max
S
/(
K
m
+
S
)(1+
I
/
K
i
)
B. r
max
E
/(
K
m
(1+
I
/
K
i
)+
S
))
C. V
max
S
/(
K
m
+
S
)(1+
I
/
K
i
)
D. r
max
S
/
K
m
Show Answer
Scratch Pad
Discuss
Correct Answer: r
max
S
/(
K
m
+
S
)(1+
I
/
K
i
)
8. The initial velocity, V
0
, of an enzyme catalyzed reaction reaches V
max
as
Options
A. [S] = K
M
B. [S] = 10 * K
M
C. 1/[S] = 1/K
M
D. 1/[S] ? 0
Show Answer
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Discuss
Correct Answer: 1/[S] ? 0
9. The active site of an enzyme differs from an antibody-antigen binding site in that the enzyme active site
Options
A. contains modified amino acids
B. catalyzes a chemical reaction
C. is complementary to a specific ligand
D. contains amino acids without side chains
Show Answer
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Discuss
Correct Answer: catalyzes a chemical reaction
10. Enzymes are basically
Options
A. proteins
B. vitamins
C. fat
D. carbohydrates
Show Answer
Scratch Pad
Discuss
Correct Answer: proteins
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