Enzymes and Kinetics – Section 2

16. When substrate [S] = KM (Michaelis-Menten constant), the velocity of an enzyme-catalyzed reaction is about

A. 0.1 * Vmax
B. 0.2 * Vmax
C. 0.5 * Vmax
D. 0.9 * Vmax

Correct Answer: C. 0.5 * Vmax

17. A classical noncompetitive inhibitor has

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

Correct Answer: B. no effect on substrate binding and vice versa

18. The active site of an enzyme differs from an antibody-antigen binding site in that the enzyme active site

A. contains modified amino acids
B. catalyzes a chemical reaction
C. is complementary to a specific ligand
D. contains amino acids without side chains

Correct Answer: B. catalyzes a chemical reaction

19. Enzymes are basically

A. proteins
B. vitamins
C. fat
D. carbohydrates

Correct Answer: A. proteins

20. Which of the following refers to pseudo steady-state?

A. d(CE)/dt = 0
B. d(Cp)/dt = 0
C. d(CES)/dt = 0
D. d(Cs)/dt = d(CES)/dt

Correct Answer: C. d(CES)/dt = 0

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