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Enzymes and Kinetics problems


  • 1. When an enzyme is functioning at Vmax, the rate of the reaction is limited by

  • Options
  • A. the number of collisions between enzyme and substrate
  • B. the number of substrate molecules in the reaction
  • C. the concentration of the substrate
  • D. the rate at which the enzyme can convert substrate to product
  • Discuss
  • 2. 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
  • Discuss
  • 3. 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
  • Discuss
  • 4. 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
  • Discuss
  • 5. Which category of enzymes belongs to class 5 in the international classification?

  • Options
  • A. Hydrolases
  • B. Isomerases
  • C. Oxido-reductases
  • D. Cyclase
  • Discuss
  • 6. 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
  • Discuss
  • 7. When substrate [S] = KM (Michaelis-Menten constant), the velocity of an enzyme catalyzed reaction is about

  • Options
  • A. 0.1 * Vmax
  • B. 0.2 * Vmax
  • C. 0.5 * Vmax
  • D. 0.9 * Vmax
  • Discuss
  • 8. 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
  • Discuss
  • 9. The rate equation in non-competitive inhibition based on Michaelis Menten equation is given by

  • Options
  • A. rmaxS/(Km + S)(1+I/Ki)
  • B. rmaxE/(Km (1+I/Ki)+S))
  • C. VmaxS/(Km + S)(1+I/Ki)
  • D. rmaxS/Km
  • Discuss
  • 10. The initial velocity, V0, of an enzyme catalyzed reaction reaches Vmax as

  • Options
  • A. [S] = KM
  • B. [S] = 10 * KM
  • C. 1/[S] = 1/KM
  • D. 1/[S] ? 0
  • Discuss

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