Discussion
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- Question
The active site of an enzyme remains
Options- A. at the center of globular proteins
- B. rigid and does not change shape
- C. complementary to the rest of the molecule
- D. none of the above
- Correct Answer
- none of the above
- 1. The rate-determining step of Michaelis Menten kinetics is
Options- A. the complex formation step
- B. the complex dissociation step to produce product
- C. the product formation step
- D. Both (a)and(c) Discuss
- 2. Linear inhibition is sometimes called as
Options- A. complete inhibition
- B. incomplete inhibtion
- C. partial inhibition
- D. mixed inhibition Discuss
- 3. An enzyme and a reactant molecule maintain relationship as
Options- A. a temporary association
- B. an association stabilized by a covalent bond
- C. one in which the enzyme is changed permanently
- D. non complementary binding Discuss
- 4. An enzyme is assayed at an initial substrate concentration of 2 x 10-5M. In 6 minute, half of the substrate is used. The Km for the substrate is 2 x 10-3M. The value of k in minute is
Options- A. 0.115
- B. 0.42
- C. 0.093
- D. 6.693 Discuss
- 5. A competitive inhibitor of an enzyme is usually
Options- A. a highly reactive compound
- B. a metal ion such as Hg2+ or Pb2+
- C. structurally similar to the substrate.
- D. water insoluble Discuss
- 6. In a Lineweaver-Burk Plot, competitive inhibitor shows which of the following effect?
Options- A. It moves the entire curve to right
- B. It moves the entire curve to left
- C. It changes the x-intercept
- D. It has no effect on the slope Discuss
- 7. The enzyme inhibition can occur by
Options- A. reversible inhibitors
- B. irreversible inhibitors
- C. Both (a) and (b)
- D. None of these Discuss
- 8. Which graphical method is used to determine an enzyme degree of cooperativity?
Options- A. Hill plot
- B. Koshland curve
- C. Michaelis-Menten hyperbola
- D. Can not be determined Discuss
- 9. Which of these enzymes contains a Zinc (Zn) ion?
Options- A. Carboxypeptidase A
- B. Phosphorylase B kinase
- C. Tyrosine hydroxylase
- D. Phosphodiesterase Discuss
- 10. Non-competitive inhibitor of an enzyme catalyzed reaction
Options- A. decreases Vmax
- B. binds to Michaelis complex (ES)
- C. both (a) and (b)
- D. can actually increase reaction velocity in rare cases Discuss
Enzymes and Kinetics problems
Search Results
Correct Answer: the complex dissociation step to produce product
Correct Answer: complete inhibition
Correct Answer: a temporary association
Correct Answer: 0.115
Correct Answer: structurally similar to the substrate.
Correct Answer: It changes the x-intercept
Correct Answer: Both (a) and (b)
Correct Answer: Hill plot
Correct Answer: Carboxypeptidase A
Correct Answer: both (a) and (b)
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