Biochemsitry 3304 Midterm 3

1. Which of the following general properties are properties of enzymes?

a. Very high acceleration of reaction rates.
b. Physiological reaction conditions.
c. Highly specific reactions for substrate selectivity and stereospecificity.
d. All of the above are properties of enzymes.

2. Enzymes act on specific substrates using complementarity. What would be the most significant kind of
complementarity would be utilized by the enzyme Succinate Dehydrogenase to differentiate succinate from the
structurally similar malonate?


a. Electronic complementarity
b. Geometric complementarity
c. Charge complementarity
d. Stereochemical complementarity

3. TEV Protease is a highly specific protease and cleaves the sequence ENLYFNG at the NG bond. What would you
predict to be the effect of replacing the L-Phenylalanine residue with a D-Phenylalanine?
a. No effect.
b. Cleavage would be more efficient.
c. Cleavage would be a little less efficient.
d. Cleavage would likely not occur or be drastically reduced.

4. The best idea of complementarity suggested in Question 3 would be which of the following?
a. Electronic complementarity
b. Geometric complementarity
c. Charge complementarity
d. Stereochemical complementarity

5. Vitamins are examples of what kind of enzymatic species?
a. Coenzyme molecule.
b. Cofactor molecule.
c. Structural molecule.
d. Organic molecule.

6. Metal ions such as Cu++, Fe++ and Zn++ are examples of what kind of enzymatic species?
a. Coenzyme molecule.
b. Cofactor molecule.
c. Structural molecule.
d. Organic molecule.


7. The following diagram is for both standard and catalyzed reactions converting Substrate S into Product P.


Which double arrow denotes the activation energy for the uncatalyzed reaction?
a. a
b. b
c. c
d. d

8. Which double arrow denotes the difference in activation energy between the catalyzed and uncatalyzed reaction?
a. a
b. b
c. c
d. d

9. Which double arrow denotes the G for the conversion of S to P?
a. a
b. b
c. c
d. d

10. The diagram in Question suggests what about how a catalyst can accelerate a reaction?
a. The activation energy for a catalyzed reaction is less than that for the uncatalyzed reaction.
b. The catalyzed reaction transition state is stabilized compared to the uncatalyzed reaction.
c. The free energy change of the reaction is unchanged.
d. (a) is a consequence of (b), which is the major mechanism for accelerating a reaction with a catalyst.

11. For the diagram in Question 7, the rate of the catalyzed reaction is 148.4 times that of the uncatalyzed reaction.
What is the stabilization energy of the catalyzed reaction at standard temperature?
a. 5.4 kJ/mol
b. 11.3 kJ/mol
c. 12.4 kJ/mol
d. 15.4 kJ/mol


The following first step of an enzymatic reaction is referred to for Questions 12 and 13.


12. What is the type of mechanism used in this example?
a. Covalent catalysis.
b. Metal catalysis.
c. General Acid-Base catalysis.
d. Cannot determine.

13. Would you predict that DNA could be cleaved by this enzyme?
a. Yes
b. No
c. More slowly
d. Cannot determine with this information.

14. The following mechanism is for Pyruvate Decarboxylase.

What type of catalysis mechanism would best describe this reaction pathway as shown?
a. Covalent catalysis.
b. Metal catalysis.
c. General Acid-Base catalysis.
d. Cannot determine.


15. The following is a step in the mechanism of Lysozyme.


What other amino acid would you expect to be able to substitute for Glu35 based on pH and ability to stabilize the
transition state oxonium ion?
a. Histidine
b. Serine
c. Valine
d. Arginine

16. Acetylcholine esterase is a serine esterase critical for hydrolyzing the neurotransmitter acetylcholine. Nerve gases
such as Sarin and DIPF inhibit this enzyme as a primary mode of their toxicity. What is the most correct mechanism for
this inhibition?

a. These agents bind to the enzyme and mimic the substrate, acetylcholine.
b. These agents bind to the enzyme and mimic the products, acetic acid and choline.
c. These agents form a stable covalent bond with the active site serine and mimic the transition state.
d. These agents release HF from their reaction with the active site serine.
17. What three amino acids comprise the catalytic triad for serine proteases?
a. Lysine-Histidine-Serine
b. Aspartic or Glutamic Acid-Histidine-Serine
c. Tyrosine-Histidine-Serine
d. Arginine-Histidine-Serine

18. Many proteases are produced as longer precursors. Why would this be the case?
a. Maintains a blocked or disordered active site until activated by proteolysis or cleavage of the inactive precursor.
b. Prevention of activation of the protease when synthesized, thus protecting the synthesizing organ.
c. Regulated activation of the protease when and where it is required.
d. All of the above.

19. A First Order reaction is linear in respect to which variables?
a. [A] and t
b. 1/[A] and t
c. ln[A] and t
d. k and t

20. A Second Order reaction is linear with respect to which variables?
a. [A] and t
b. 1/[A] and t
c. ln[A] and t
d. k and t

21. The following reaction data was obtained for an experiment. Is the data most consistent with a First or Second Order
reaction? HINT: The graphing diagrams below are to assist you in plotting these data.
T [A]
0 10.0
4 3.0
8 1.8
16 1.0


a. First order b. Second order c. Zero order d. Cannot determine

22. From the graphing in Question 21, what is the value for the k constant for the reaction?
a. 0.02
b. 0.05
c. 0.1
d. 0.5

23. What are the simplifying assumptions made for Michaelis-Menten enzyme kinetics?
a. Substrate concentration greatly exceeds enzyme concentration.
b. The enzyme-substrate complex concentration remains in steady state.
c. Equilibrium between the enzyme, substrate, and enzyme-substrate complex.
d. (b) and (c) are the fundamental simplifying assumptions with (b) deriving from performing the experiment under
conditions of (a).

24. Which of the following equations is the Michaelis-Menten Equation for a competitive inhibitor?
a. v
o
= Vmax [S] / Km + [S]
b. v
o
= Vmax [S] / Km + [S]
c. v
o
= Vmax [S] / Km + [S]
d. v
o
= Vmax [S] / Km + [S]

25. A reaction was analyzed with only 2 points. Assuming linearity, estimate the Vmax and Km from these
measurements. Hint: Slope = rise/run
v
o
(M/s)

[S] (M)
10 2
40 10

a. Vmax = 80 M/s, Km = 10 M
b. Vmax = 120 M/s , Km = 20 M
c. Vmax = 160 M/s , Km = 30 M
d. Vmax = 200 M/s, Km = 40 M

26. What is the type of inhibition for the following graph?


a. Competitive
b. Uncompetitive
c. Mixed
d. Pure noncompetitive

27. What type of inhibition for the following graph?


a. Competitive
b. Uncompetitive
c. Mixed
d. Pure noncompetitive

28. What type of inhibition for the following graph?

a. Competitive
b. Uncompetitive
c. Mixed
d. Pure noncompetitive


Analysis of an inhibitor on an enzyme reaction rate produced the following graph:


29. What type of inhibition is this?
a. Competitive
b. Uncompetitive
c. Mixed
d. Pure noncompetitive

30. The value at the X-intercept (1) has what value?
a. -1/Km
b. 1/Km
c. /Km
d. /Km, but with =

31. The value at the Y-intercept (2) has what value?
a. 1/Vmax
b. /Vmax
c. /Vmax
d. None of the above.

32. In these data, the lowest line has no inhibitor with a Y-intercept of 0.05 s/nM. The next higher line has 100 nM of an
inhibitor and a Y-intercept of 0.25 s/nM. What is the for this inhibitor?
a. 1
b. 2
c. 5
d.10

33. From this , what is the Ki for this inhibitor given the inhibitor concentration in Question 32?
a. 2.5 nM
b. 25 nM
c. 100 nM
d. 250 nM

34. Analysis of a novel enzyme apparently using multiple substrates (S
A
and S
B
) produces the Reaction Rate (v
o
) versus
Substrate A reaction profile observed in Curve 1 at a constant level of Substrate B. Adding more Substrate B shifts the
observed rate to Curve 2. What could explain this observation?


a. Substrate B inhibits the reaction of the enzyme with Substrate A.
b. Substrate B activates the reaction of the enzyme with Substrate A.
c. The enzyme appears to be cooperative and Substrate B appears to increase the cooperativity.
d. Both (b) and (c) are possible.

35. Degradation of nutrients and cell components to be used for energy or to rebuild other cellular components and
structures is an example of what type of metabolism?
a. Catabolism
b. Anabolism
c. Reduction/Oxidation
d. Aerobic

36. How is metabolism controlled?
a. Genetic regulation of the same metabolic pathways in different organs and tissues like isozymes.
b. Different pathways for catabolic and anabolic metabolism.
c. Allosteric signaling and covalent modifications of enzymes involved in metabolic processes.
d. All of these are significant mechanisms to control metabolism.

37. What type of organic molecules assist many enzymatic reactions involved in metabolism?
a. Proteins
b. Carbohydrates
c. Nucleic acids
d. Vitamins

38. What is the equilibrium constant for phosphoenolpyruvate (PEP) hydrolyzing to pyruvate and phosphate at human
physiological temperature? Hint: Remember the energy of hydrolysis of PEP is about twice that of ATP.
a. 2.9 x 10E10
b. 7.3 x 10E10
c. 2.8 x 10E11
d. 7.2 x 10E11

39. What electrochemical potential would you observe for a highly spontaneous redox reaction?
a. Positive
b. Negative
c. Near zero
d. Zero

40. Undersea bacteria can use alternative sources of energy including sulfurous materials like H
2
S. Using the standard
half-cell potentials for these reactions, calculate the electrochemical potential and direction for this reaction?
Pyruvate- + 2H+ + 2 e- = lactate- Eo = -0.185V
S + 2H+ + 2 e- = H
2
S Eo = -0.230V

a. -0.045V, lactate- + S = H2S + pyruvate-
b. 0.045V, lactate- + S = H2S + pyruvate-
c. 0.045V, pyruvate- + H2S = lactate- + S
d. -0.045V, pyruvate- + H2S = lactate- + S

41. Calculate the G for this reaction using the Faraday Constant = 96,485 J/V mol.
a. -4.3 kJ/mol
b. -8.7 kJ/mol
c. -10.5 kJ/mol
d. -18.5 kJ/mol

42. What carbohydrate is the following structure?

a. -D-Glucose
b. -D-Mannose
c. -D-Mannose
d. -D-Glucose

43. Which of the following linear structures would correlate with the above cyclic structure?
a. b. c. d.


44. A highly purified sample of polysaccharide was mixed with Tollens Reagent. This reagent provides Ag+ ions
complexed with ammonia to form a diamminesilver(I)+ cation. When mixed with the polysaccharide, the container
became rapidly coated with a mirror-like silver surface. What is the conclusion from this test?
a. The polysaccharide formed a silver complex and precipitated.
b. The polysaccharide is a reducing sugar.
c. The polysaccharide is not a reducing sugar.
d. Cannot determine from this information.

45. The following structure is for hyaluronic acid glycosaminoglycan. The repeating structure is a disaccharide unit.


What monosaccharides comprise this disaccharide unit?
a. glucose and N-acetyl-glucosamine
b. galactose and N-acetyl-glucosamine
c. glucuronic acid and N-acetyl-glucoseamine
d. N-acetyl-galactoseamine and glucuronic acid

46. What linkage is between these sugar residues (not the linkage between the disaccharide units at the ends, but
between the sugars in the disaccharide unit itself)?
a. -(1-2)
b. -(1-3)
c. -(1-3)
d. -(1-4)

47. Why would the highly branched storage polysaccharide glycogen be important for energy storage rather than having
all of the carbohydrates as single or smaller monosaccharides?
a. Monosaccharides at high concentration would produce very significant osmotic pressure within cells.
b. Monosaccharides can produce energy rapidly.
c. Monosaccharides are easily transported.
d. Monosaccharides are the primary structure necessary for metabolic processing.

48. Which of the following is important properties of peptidoglycans involved in bacterial cell wall synthesis?
a. Peptidoglycans are a crosslinked meshwork of carbohydrates and short peptides.
b. Gram positive bacteria have thick peptidoglycan cell walls.
c. Peptidoglycans often have isopeptide bonds and amino acids with alternative chirality.
d. (a) and (c) are both important for peptidoglycans in bacteria.


49. The following peptide sequence from CD34, a human hematopoetic progenitor cell antigen, is known to be heavily
glycosylated. Where would you predict glycosylation to occur?

MSLDNNGTAT PELPTQGTFS NVSTNVSYQE
Section 1 Section 2 Section 3

a. Section 1 and Section 2
b. Section 2 and Section 3
c. Section 1 and Section 3
d. Section 1, 2 and 3.

50. Which of the following enzyme(s) are important for defense against bacteria with peptidoglycan cell walls?
a. RNAse
b. Lysozyme
c. Trypsin
d. Acetylcholine Esterase