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- Question
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
- Correct Answer
- 0.115
- 1. 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
- 2. Which of these proteases is not a cysteine active site protease?
Options- A. Calpain
- B. Cathepsin D
- C. Papain
- D. None of the above Discuss
- 3. A classical uncompetitive inhibitor is a compound that binds
Options- A. reversibly to the enzyme substrate complex yielding an inactive ESI complex
- B. irreversibly to the enzyme substrate complex yielding an inactive ESI complex
- C. reversibly to the enzyme substrate complex yielding an active ESI complex
- D. irreversibly to the enzyme substrate complex yielding an active ESI complex Discuss
- 4. The conformational change in an enzyme after the substrate is bound that allows the chemical reaction to proceed, can be explained by
Options- A. induced fit
- B. transition
- C. fit and fine
- D. Pasteur Discuss
- 5. Which of the following statements is true for enzymatically catalyzed reaction?
Options- A. The activation energy of the reaction is lowered so that a larger proportion of the substrate qualifies to overcome it
- B. Additional substrate molecules are energized to overcome the activation energy of the reaction
- C. The activation energy of the reaction is increased, thus decreasing the likelihood that any substrate molecules will overcome it
- D. The activation energy of the reaction is lowered so that a fewer substrate molecules can overcome it Discuss
- 6. 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
- 7. Linear inhibition is sometimes called as
Options- A. complete inhibition
- B. incomplete inhibtion
- C. partial inhibition
- D. mixed inhibition Discuss
- 8. 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
- 9. 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 Discuss
- 10. 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
Enzymes and Kinetics problems
Search Results
Correct Answer: structurally similar to the substrate.
Correct Answer: Cathepsin D
Correct Answer: reversibly to the enzyme substrate complex yielding an inactive ESI complex
Correct Answer: induced fit
Correct Answer: The activation energy of the reaction is lowered so that a larger proportion of the substrate qualifies to overcome it
Correct Answer: a temporary association
Correct Answer: complete inhibition
Correct Answer: the complex dissociation step to produce product
Correct Answer: none of the above
Correct Answer: It changes the x-intercept
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