1.

What thermodynamic parameters always area compatible with a spontaneous chemical

reaction?
a. Positive free energy change
b. Negative free energy change
c. Negative redox potential
d. Positive enthalpy change
e. Negative entropy change
2. Give the chemical reaction, A + B <-> C + D, Go = -1.3 kcal/mol. What can we conclude about
this chemical reaction
a. This reaction will proceed spontaneously to the right
b. The more negative the G, the faster the reaction will produce C.
c. At equilibrium, if [A] = [C], then [B] < [D].
d. Under physiological conditions, the reaction will proceed in the reverse direction
3. The conversion of Glucose 1-P (Glc 1-P) to Fructose 1,6-diphosphate (Frc 1,6dip) occurs in
three steps. What is the standard free energy change for the overall reaction.
a. Frc 1,6diP <-> Frc 6-P + Pi Go = -3.8 kcal/mol
b. Glc 6-P <-> Frc 6-P Go = +0.4 kcal/mol
c. Glc 6-P <-> Glc 1-P Go = +1.7 kcal/mol
d. Glc 1-P + Pi <-> Frc 1,6diP Go = ?

4. What is the standard redox potential for the reduction of pyruvate by NADH?
a. Pyruvate + 2e- => lactate Eo = -0.19V
b. NAD+ + 2e- => NADH Eo = -0.32V

5. At equilibrium of the above reaction, if the concentration of NAD+ and NADH are equal, will
pyruvate or lactate be present at higher concentration?
6. Enzymes may be expected to change which of the following reaction parameters or metrics?
a. G
b. E
c. Go
d. G*
7. Consider the reaction A + B C + D with a G of +12.7 kcal/mol and mediated by enzyme
XYZ. Which are the products and which are the reactants?
a. A and B are the reactants, a G of +12.7 indicates a thermos push toward C and D
b. C and D are the reactants, but the thermos push is away from the products A and B
c. Either A + B or C + D may considered to be reactants, as enzymes catalyze both the
forward and reverse of the reaction depending on local conditions
d. None of the above are correct
8. When an enzyme breaks a bond and adds a molecule of water, the enzyme is referred to as a:
a. Transferase
b. Hydrolase
c. Ligase
 d. Oxidoreductase
9. The active site of an enzyme is best described as often composed of:
a. Adjacent amino acids in the primary structure that are in critically conserved portions of
the same subunit
b. Adjacent amino acids in the primary structure, but not in the same subunit
c. Non-adjacent amino acids that approach each other in the tertiary or quaternary
structure
d. Non-adjacent amino acids that approach each other in the secondary structure
10. Heme is a ___________of the protein hemoglobin, while NADH is a ___________for the
enzyme lactate dehydrogenase.
a. Cofactor/Prosthetic group
b. Vitamin/Cofactor
c. Prosthetic group/Cofactor
d. Ribozyme/Isoform
11. Formation of the peptide bond during the process of protein synthesis (translation) is:
a. Catalyzed by ribonucleic acid (RNA)
b. An example of an isozyme
c. Activity that is entirely protein-based
d. An example of isomerase activity
12. The concepts of enzyme breathing, flexibility and the existence of a transition state are all
related to which of the following:
a. Enzymes show saturation kinetics
b. Enzymes are like using a key to unlock a door and pass through
c. Enzymes have a top speed known as Vmax
d. The model of induced fit
13. Lactate dehydrogenase catalyzes the following reaction: lactate + NAD+ pyruvate +
NADH

In a reaction tube containing LDH with a Vmax = 50 micromol/min, Km = 2 mmol/L and

[lactate] = 1 mmol/L, what is the rate of pyruvate formation?

14. All of the following statements regarding enzymes are correct EXCEPT:
a. Enzymes enhance reactions by making the G for the reaction more negative.
b. Enzymes enhance reactions by lowering the activation energy for the reaction.
c. Most enzymes are proteins
d. Enzyme activity varies with the pH of the solution.
15. True or False? ______The rate of a chemical reaction is given by the concentration of the
products multiplied by a rate constant, k.
16. Ture or False? ______In a Lineweaver-Burk plot, the slope of the line is equal to Km/Vmax and
the y-intercept is equal to 1/Vmax.
17. According to the M-M equation, when Km is equal to [S], the initial rate of the reaction would
be:
a. 10% of max
b. 25% of max
c. 50% of max
d. 100% of max (Vmax)
18. Choose the best statement regarding Vmax for an enzyme.
a. Vmax is a measure of an enzymes affinity for its substrate.
b. Vmax is also known as the turnover number.
c. An enzyme with multiple substrates will have the same Vmax for all substrates.
d. Vmax is the rate when all enzyme molecules are in the ES complex
19. Isozymes
a. Are enzymes that use the same cofactor
b. Are enzymes that catalyze the same reaction
c. Show the same Km for a substance
d. Show the same Vmax for a chemical reaction
20. Regarding enzyme inhibition
a. Non-competitive inhibition can be reversed by adding more substrate
b. A competitive inhibitor will lower the apparent Km for a substrate
c. The transition state should show greater affinity than the substrate
d. Competitive inhibitors is irreversible
21. How is specificity of location and peptide bond selection of chymotrypsin achieved?

22. How does chymotrypsin stabilize the transition state?

23. How does the transition state relate to the original substrate structure?

24. What is meant by a tetrahedral state?

25. Define and give the function of the chymotrypsin hydrophobic pocket, the substrate pocket,
the catalytic triad and the oxyanion hole.
26. What type of protease is chymotrypsin?

27. What are several of the acceleration mechanisms used?

28. What is a Ping Pong Bi Bi reaction?

29. What general biochemical mechanistic events occur (in order, please) during the reaction
mechanism of chymotrypsin.

30. What is resonance and how does it contribute to this reaction?

31. How does hydrogen bonding contribute to this reaction?

32. What important step occurs at the very end of the reaction cycle, in order to regenerate the
enzyme to begin another reaction cycle?

33. What happens structurally to a protein substrate acted upon by chymotrypsin?

34. What type of acceleration mechanism is exemplified by a Sn2 attack as described for an
aspartate protease enzyme?
35. If a mutation occurred in the hydrophobic (specificity) pocket of chymotrypsin that changed
one of the amino acids to aspartate, what effect do you predict this would have on the
specificity of chymotrypsin? With regard to a pre-selected peptide bond site hydrolyzed by the
normal form of chymotrypsin, would the effect seen in the mutated form of the enzyme be
seen primarily in the Km or the Vmax? What would be expected regarding Kcat? How would
you predict that catalytic efficiency would change?

36. Which of the following statements best describes the catalytic mechanism of HIV protease?
a. HIV protease requires a Zn2+ cofactor
b. The active site contains a catalytic triad of Ser, His and Asp side chains
c. HIV protease differs from chymotrypsin only in the specificity pocket
d. Two aspartate residues act together to enhance the nucleophilicity of a water molecule
37. What are the four major mechanisms that cells use to regulate the activity of existing
enzymes? Give a brief definition and one example of each mechanism.

38. Regarding allosteric modulation of enzyme activity

a. Allosteric modulators bind to the active site of the enzyme
b. Negative allosteric modulators decrease the Km for the substrate
c. Positive allosteric modulators cause a conformational change from the R to the T state
d. Show a sigmoidal v vs. [S] plot
39. Which of following proteins is a regulatory protein that affects enzyme activity through direct
protein to protein interactions.
a. Calmodulin
b. Aspartate transcarbamyolase
c. Protein kinase A
d. Plasmin
40. Protein kinase A
a. Causes irreversible activation of its protein substrates
b. Uses cyclic AMP as the phosphate donor
c. Transfers a hydroxyl group to an ATP molecule in its protein substrate
d. May cause either enhanced or decreased activity of its target enzyme protein
41. A blood clot consists of a giant protein precipitate of what protein?
a. Thrombin
b. Factor X
 c. Plasmin
d. Fibrin
42. Allosteric inhibition is different from pure Michaelis-Menten noncompetitive inhibition
because allosteric inhibition can be shown to produce:
a. Unchanged substrate affinity
b. Lower apparent Km
c. Linear rate vs. [S] plot
d. A distinct right shift of the Rate vs. [S] plot
43. What is the role of covalent modification of histones in the structure and function of DNA?

44. Discuss the general principles of the coagulation cascade and give examples of how these
pathways are examples of enzyme regulation by zymogen activation, covalent modification
and compartmentation.