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Biochemical Engineering - Enzymes and Kinetics

Exercise : Enzymes and Kinetics - Section 2
16.
When substrate [S] = KM (Michaelis-Menten constant), the velocity of an enzyme catalyzed reaction is about
0.1 * Vmax
0.2 * Vmax
0.5 * Vmax
0.9 * Vmax
Answer: Option
Explanation:
No answer description is available. Let's discuss.
17.
A classical noncompetitive inhibitor has
no effect on substrate binding
no effect on substrate binding and vice versa
significant effect on substrate binding
significant effect on substrate binding and vice versa
Answer: Option
Explanation:
No answer description is available. Let's discuss.
18.
The active site of an enzyme differs from an antibody-antigen binding site in that the enzyme active site
contains modified amino acids
catalyzes a chemical reaction
is complementary to a specific ligand
contains amino acids without side chains
Answer: Option
Explanation:
No answer description is available. Let's discuss.
19.
Enzymes are basically
proteins
vitamins
fat
carbohydrates
Answer: Option
Explanation:
No answer description is available. Let's discuss.
20.
Which of the following refers to pseudo steady state ?
d(CE)/dt = 0
d(Cp)/dt = 0
d(CES)/dt = 0
d(Cs)/dt = d(CES)/dt
Answer: Option
Explanation:
No answer description is available. Let's discuss.
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