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
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
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
19. Enzymes are basically
A. proteins
B. vitamins
C. fat
D. carbohydrates
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