Discussion
Home ‣ Biochemical Engineering ‣ Enzymes and Kinetics Comments
- Question
A noncompetitive inhibitor of an enzyme-catalyzed reaction
Options- A. increases KM and increases Vmax
- B. increases KM and reduces Vmax
- C. reduces KM and increases Vmax
- D. reduces KM and reduces Vmax
- Correct Answer
- increases KM and reduces Vmax
- 1. The Woolf-Augusteinsson-Hofstee plot of ν versus ν/[S] and the Eadie-Scatchard plot of ν/[S] versus ν do not involve reciprocals of ν therefore are considered to be more reliable when the error in v is
Options- A. non-significant
- B. significant
- C. nothing to do with the reliability
- D. non significant in selected cases Discuss
- 2. Quasi steady state is also known as
Options- A. Michaelis Menten approach
- B. Briggs-Haldane approach
- C. Pseudo steady state
- D. all of the above Discuss
- 3. The plot commonly used for determining the value of Vmax is
Options- A. Lineweaver Burk plot
- B. Langmuir plot
- C. Eadie Hofstee plot
- D. all of these Discuss
- 4. An allosteric inhibitor of an enzyme usually
Options- A. participates in feedback regulation
- B. denatures the enzyme
- C. is a hydrophobic compound
- D. causes the enzyme to work faster Discuss
- 5. In competitive inhibition a factor is obtained from the measurement of
Options- A. Vmax
- B. KM
- C. Y-intercept in Lineweaver-Burk Plot
- D. None of these Discuss
- 6. The reciprocal equation for non competitive inhibition can be arranged to the equation for the
Options- A. Dixon plot
- B. Woolf-Augusteinsson-Hofstee plot
- C. Eadie-Scatchard plot
- D. Hanes-Woolf plot Discuss
Enzymes and Kinetics problems
Search Results
Correct Answer: significant
Correct Answer: Pseudo steady state
Correct Answer: all of these
Correct Answer: participates in feedback regulation
Correct Answer: KM
Correct Answer: Dixon plot
Comments
There are no comments.Programming
Copyright ©CuriousTab. All rights reserved.