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The KM is: equal to the substrate concentration when the reaction rate is half
its maximal value.

2. Which of the following is correct concerning the differences between hemoglobin

and myoglobin? Hemoglobin exhibits cooperative binding of O2 while myoglobin does

3. The number of substrate molecules converted to product in a given unit of time

by a single enzyme molecule at saturation is referred to as the: turnover number.

4. An individual molecular structure within an antigen to which an individual

antibody binds is as a(n): epitope.

5. The formula K'eq = 10^(-?G'/1.36) indicates the relationship between: the

equilibrium constant and standard free energy.

6. What conclusion can be drawn concerning an inhibitor if the Vmax is the same in
the presence and absence of the inhibitor? The inhibitor can be overcome with
sufficiently high concentrations of substrate.

7. 2,3-bisphosphoglycerate: All of the above.(X - preferentially binds to

deoxyhemoglobin and stabilizes it.)

8. During muscle contraction, hydrolysis of ATP results in a change in the:

conformation of myosin.

9. What type(s) of inhibition can be reversed? Competitive, noncompetitive, and


10. Riboflavin is a water-soluble organic substance that is not synthesized by

humans. Metabolically, it is chemically converted into a substance called flavin
adenine dinucleotide, which is required by succinate dehydrogenase. Which of the
following statements is most correct? Flavin adenine Dinucleotide is a coenzyme. (X
- Succinate dehydrogenase is a coenzyme.)

11. What factor(s) influence(s) the binding of oxygen to myoglobin? The partial
pressure of oxygen, pO2

12. Which of the following is true under the following conditions: The enzyme
concentration is 5 nM, the substrate concentration is 5 mM, and the KM is 5 M? The
enzyme is saturated with substrate.

13. Carbon dioxide forms carbamate groups in proteins by reaction with: N-terminal
amino groups.

14. The Gibbs-free energy of activation is: the difference between the substrate
and the transition state.

15. The characteristic that distinguishes an uncompetitive enzyme inhibitor from

other types of inhibitors is: the inhibitor binds only to the ES complex.

16. Sickle-cell anemia is caused by: a substitution of a Val residue for a Glu
residue at the 6 position.

17. A monoclonal antibody differs from a polyclonal antibody in that monoclonal

antibodies: are synthesized by a population of identical, or "cloned," cells.

18. What is the Bohr effect? the regulation of hemoglobin-binding by hydrogen ions
and carbon dioxide
19. The energy that is released by the hydrolysis of ATP by actin is used for:
actin filament assembly.

20. Which of the following parts of the IgG molecule are not involved in binding to
an antigen? Fc

21. Which of these statements about enzyme-catalyzed reactions is false? The

activation energy for the catalyzed reaction is the same as for the uncatalyzed
reaction, but the equilibrium constant is more favorable in the enzyme-catalyzed

22. In a plot of l/V against 1/[S] for an enzyme-catalyzed reaction, the presence
of a competitive inhibitor will alter the: intercept on the l/[S] axis.

23. When substrate concentration is much greater than KM, the rate of catalysis is
almost equal to: Vmax

24. Both water and glucose share an -OH that can serve as a substrate for a
reaction with the terminal phosphate of ATP catalyzed by hexokinase. Glucose,
however, is about a million times more reactive as a substrate than water. The
best explanation is that: the larger glucose binds better to the enzyme; it induces
a conformational change in hexokinase that brings active-site amino acids into
position for catalysis.

25. Which of the following is true? None of the above.

26. The binding of a positive allosteric effector to an allosteric enzyme

typically: decreases the Km for its substrate.

27. A and B interact with Kd = 10^-8 M; A and C interact with Kd = 10^-7 M. What
does this tell you about A, B, and C? The interaction affinity between A and B is
higher than that between A and C.

28. Which of the following is the most accurate statement regarding the enzyme
chymotrypsin? The catalytic mechanism of chymotrypsin involves a catalytic triad
composed of an aspartate, a histidine, and a serine residue.

29. A good transition-state analog: binds to the enzyme more tightly than the

30. The rate of breakdown of the enzyme-substrate complex can be described by the
expression: k-1 [ES] + k2 [ES].