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CH 369 Practice Exam 2 Name: _________________________________________ eID _________

Helpful Equations: Lineweaver-Burk:

Section I: 16 points (1 point each)


1. On a transition state diagram for a one-step, very spontaneous reaction (large negative !G), a large peak

(high !G ) would imply a ______ rate for the reaction. A) low B) high
2. Metal ion cofactors with more than one oxidation state may assist in catalysis by the ______ class of

enzymes. A) ligase B) lyase C) hydrolase form until they enter the digestive tract. A) denatured B) zymogen

D) oxidoreductase E) transferase

3. Proteolytic enzymes don't digest the pancreas, where they are synthesized, because they are in the ______ C) phosphorylated D) T form

4. ______ is a serine protease that recognizes residues with small neutral side chains. A) chymotrypsin B) subtilisin C) trypsin D) elastase 5. Which of the following amino acid residues would not provide a side chain for acid-base catalysis? A) leucine B) serine C) lysine D) aspartic acid E) histidine 6. In uncompetitive inhibition, the inhibitor binds only to the ______. A) free enzyme D) substrate B) enzyme-substrate complex E) transition state C) product 7. Enzymes accelerate biochemical reactions by A) decreasing the !G for the reactions B) increasing the !G for the reactions C) establishing a 'closed system' for each reaction D) promoting reaction pathways associated with a positive !G E) providing a more favorable pathway for the reactions

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8. Which of these amino acid groups would not make a good nucleophilic catalyst? A) amino B) sulfhydryl C) imidazole D) methyl 9. The height of the activation barrier determines: A) the free energy change of the reaction B) the rate of the reaction C) the probability that the reaction will be spontaneous D) A and C E) A, B, and C

E) hydroxyl

10. An enzyme has two inhibitors with KI values of 2 x 10 3 M and 2 x 10 6 M. The inhibitor that binds more

tightly has KI =______.


A) 2 x 10 3 M B) 2 x 10 6 M

11. Glycosphingolipids with complex carbohydrate head groups that often serve as cellular receptors are

______. A) cerebrosides

B) steroids

C) gangliosides

D) eicosanoids

12. Clusters of lipids and proteins in membranes are called ______. A) lipoproteins C) lipid rafts B) proteolipids D) integral lipid proteins 13. What type of transport does not require the assistance of a membrane protein? A) simple diffusion D) active transport B) facilitated diffusion E) none of the above C) passive transport 14. Which of the following is a secondary messenger? A) Cortisol B) cyclic AMP C) Insulin

D) G protein

E) Epinephrine

15. A pore that simultaneously transports two different molecules in different directions is called: A) a promiscuous pore D) an antiporter B) a symporter E) a gap junction C) an equilibrium machine 16. G proteins: A) consist of three subunits, G", G#, and G$. B) hydrolyze GTP to GMP + Pi + Pi . C) completely span the cell membrane.

D) A and B E) A and C

Section II: 66 points (2 points each)


17. If an enzyme-catalyzed reaction has a low rate at low pH and high rate at higher pH, this implies that a

group on either the enzyme or the substrate must be ______ for an efficient reaction. A) protonated B) deprotonated C) oxidized D) reduced

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18. On a LineweaverBurk plot, the intercept where 1/vo = 0 is ______. A) 1/KM B) KM C) 1/Vmax D) Vmax E) k cat

19. Which of the following is (are) not found as covalently attached anchors in lipid-linked proteins: A) isoprenoid groups D) glycosylphosphatidyl inositol groups B) fatty acids E) all of the above C) cholesterol and other sterols 20. An enzyme class that makes double bonds is A) transferase B) hydrolase C) isomerase

D) ligase E) none of the above

21. What limits the signaling activity of a G protein once it has been stimulated by an epinephrine binding

receptor? A) GTPase activity of the alpha subunit B) Phosphorylation of the trimeric complex
22. Phospholipase C cleaves PIP2 , generating A) cAMP and PPi

C) Dephosphorylation of tht trimeric complex D) none of the above

B) IP3 and DAG (inositol-1,4,5-trisphosphate and 1,2-diacylglycerol) C) IP3 and PPi D) cAMP and DAG E) IP3 and Pi 23. Competitive inhibition is revealed by______ on a LineweaverBurk plot. A) nonparallel lines that intersect on the y-axis B) parallel lines C) nonparallel lines that do not intersect on the y-axis 24. Find the initial velocity for an enzymatic reaction when Vmax = 3.6 x 10 5 mol-sec 1, [S] = 1.5 x 10 3 M,

and KM = 4.5 x 10 3 M. A) not enough information is given to make this calculation. B) 8.7 x 10 3 mol-sec 1 C) 9.0 x 10 6 mol-sec 1 D) 1.4 x 10 2 mol-sec 1 E) 3.9 x 10 5 mol-sec 1
25. An enzyme is considered to have evolved to its most efficient form if A) k cat is a large number D) KM is a large number B) KM is a small number C) k cat/KM is near the diffusion-controlled limit E) k cat/KM is a very small number

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26. The following question(s) refer to the overall transformation:

For the reaction, the steady state assumption assumes that A) k 1>> k2 D) [P]>>[E] B) [S] = [P] E) [P] is constant C) [ES] is constant
27. A reaction is carried out in the presence and absence of an inhibitor, and initial velocities are plotted as a

function of substrate concentration in the graph below. What type of inhibitor is this?

A) competitive inhibitor B) noncompetitive inhibitor C) mixed inhibitor

D) uncompetitive inhibitor E) irreversible inhibitor

28. Peanut oil contains a high percentage of monounsaturated triacylglycerols whereas vegetable oil contains a

higher percentage of polyunsaturated triacylglycerols. A bottle of peanut oil and a bottle of vegetable oil are stored in a pantry with an outside wall. During a cold spell, which oil will freeze? A) peanut oil B) vegetable oil
29. The imidazole side chain of histidine can function as either a general acid catalyst or a general base catalyst

because: A) in the physiological pH range both H+ and OH are present at high concentrations. B) the imidazole group is a strong reducing agent at physiological pH. C) one guanidino group is protonated, and the other is deprotonated at physiological pH. D) in the physiological pH range, the nitrogen in the ring can be easily protonated/deprotonated. E) the sulfur atoms in the ring can either gain or lose a proton at physiological pH.
30. In pure noncompetitive inhibition, how does inhibitor binding affect KM and Vmax? A) KM is increased but Vmax is not changed. B) KM is not changed but Vmax is decreased. C) KM is increased but Vmax is decreased. D) Both KM and Vmax are decreased.

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31. Rank the melting points of the following fatty acids:

(1) (2) (3)


A) 1 B) 2 C) 2

cis-oleate (18:1) trans-oleate (18:1) linoleate (18:2) > > > 2 1 3 > > > 3 3 1
D) 3 > 1 > 2 E) none of the above

32. Which of the following lipid types is the least polar? A) Triacylglycerols D) Gangliosides B) Glycerophospholipids E) none of the above C) Sphingolipids 33. Glucose is added to cells and the rate of glucose transport is plotted against glucose concentration. In the

presence of the galactose derivative 6-O-benzyl-D-galactose, the curve is shifted to the right (with no other change). What kind of agent is 6-O-benzyl-D-galactose? A) activator D) inactivator B) competitive inhibitor E) none of the above C) noncompetitive inhibitor
34. What is the proper order for the sequence of the following events in the catalytic mechanism of

chymotrypsin? a) The O atom of the active site Ser nucleophilically attacks the carbonyl C of the scissile bond. b) The active site His acts as an acid catalyst to the N atom of the scissile bond. c) The active site His acts as a base catalyst to the active site Ser residue. A) a, then b, then c D) b, then a, then c B) a, then c, then b E) c, then a, then b C) b, then c, then a F) c, then b, then a
35. What is the effect of cholesterol in a membrane? A) Increases membrane fluidity by preventing acyl chain packing. B) Reduces membrane fluidity by limiting acyl chain movement. C) Both of the above D) Neither of the above 36. Which of the following considerations in the rate of a given reaction can be optimized by enzymatic

catalysis: A) the proximity of the reacting groups B) the rotational motions of the substrates and catalytic groups C) the orientations of the substrates and catalytic groups D) all of the above E) none of the above

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37. !"#$%&'%#'()**#+",*#-%,#,./01,#-%)-#')-)(0/,*#-%,#2"(("$&.3#4,)'-&".#5,(".36

A) oxidoreductase B) lyase C) hydrolase

D) ligase E) isomerase

38. The initial velocity (v0 ) of an enzyme-catalyzed reaction A) B) C) D) E)

decreases as the substrate concentration increases is lowest when the enzyme is saturated with substrate is dependent upon the substrate concentration is independent of the pH of the solution none of the above are correct

39. In order for an enzymatic reaction obeying the MichaelisMenten equation to reach 3/4 of its maximum

velocity, A) [S] would need to be 2KM B) not enough information is given to make this calculation C) [S] would need to be 50% greater than KM D) [S] would need to be 3KM E) [S] would need to be 3/4KM
40. What is the relationship between the nucleophilicity and the acidity of an amino acid side chain? A) The greater the acidity, the more nucleophilic the group B) The greater the acidity, the less nucleophilic the group Use the following to answer questions 41-42.

The KM values for the reaction of chymotrypsin with two different substrates are given in the table below. Based on these data, answer the next two questions. Substrate N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester KM 8.8 x 10-2 6.6 x 10-4

41. Which substrate has the higher affinity for the enzyme? A) N-acetylvaline ethyl ester B) N-acetyltyrosine ethyl ester

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42. Which substrate is likely to give a higher value for Vmax? A) N-acetylvaline ethyl ester B) N-acetyltyrosine ethyl ester C) No way to tell

Use the following to answer questions 43-44.

The structure of the drug prednisone is shown below.

43. What is the most likely means of transport of this molecule into the cell? A) Binds to cell surface receptor C) Moves through gated channel B) Diffuses through lipid bilayer D) Moves by antiport or symport mechanism 44. What kind of molecule is this? A) glycerophospholipid B) sphingolipid Use the following to answer questions 45-46.

C) eicosanoid D) steroid

Shown below are three different types of lipids.

A)

B)

C)
45. Which of the structures would represent a triacylglycerol? A) A B) B 46. Which of the structures would represent a sphingolipid? A) A B) B C) C

C) C

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Use the following to answer questions 47-48.

Consider the enzyme plot below:

47. Which enzyme would generate product more rapidly when (a) [S] = 1 M and (b) [S] = 10 M? A) Enzyme A at [S] = 1 M; Enzyme B at [S] = 10 M B) Enzyme A at [S] = 10 M; Enzyme B at [S] = 1 M C) Enzyme A at [S] = 1 M and at [S] = 10 M D) Enzyme B at [S] = 1 M and at [S] = 10 M 48. Estimate the KM for each enzyme from the plot shown. A) KM (A) = 5 M; KM (B) = 7 M C) KM (A) = 1 M; KM (B) = 2 M B) KM (A) = 2 M; KM (B) = 5 M D) KM (A) = 3.5 M; KM (B) = 5 M 49. Rank the rate of transmembrane diffusion of the following compounds, from slowest to fastest:

!
A) C, A, B B) A, B, C C) B, A, C D) A, C, B

Section III: 18 points (3 points each)


50. Consider the following reaction information about substrate S. A reaction is carried out in which 100 M S is added to a mixture containing equivalent amounts of enzymes A and B. After 1 minute, which reaction product will be more abundant: P or Q?

A) P B) Q

C) both will be equal D) cannot calculate from this information

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51. In typical marine organisms, the intracellular concentrations of Na+ and Ca2+ are 10 mM and 0.1 M,

respectively. Extracellular concentrations of Na+ and Ca2+ are 450 mM and 4 mM, respectively. Calculate the free energy changes at 20C for the transmembrane movement of these ions. In which direction do the ions move? A) Na+ moves in because !G = +9.3 kJ/mol; Ca2+ moves out because !G = -25.8 kJ/mol B) Na+ moves out because !G = -9.3 kJ/mol; Ca2+ moves in because !G = +25.8 kJ/mol C) Na+ moves out because !G = +8.6 kJ/mol;Ca2+ moves out because !G = +11.2 kJ/mol D) Na+ moves in because !G = -4.0 kJ/mol;Ca2+ moves in because !G = -11.2 kJ/mol E) Na+ moves in because !G = -9.3 kJ/mol;Ca2+ moves in because !G = -25.8 kJ/mol F) Na+ moves out because !G = +4.0 kJ/mol; Ca2+ moves in because !G = -11.2 kJ/mol
Use the following to answer questions 52-53.

The tyrosinase enzyme catalyzes reactions that produce brown-colored products. In mammals, it is responsible for the production of melanin in the skin; in plants, it is responsible for the browning that occurs when foods such as apples or mushrooms are sliced open and exposed to air. Food scientists interested in preventing the browning process in plant-based foods have shown that dodecyl gallate is an inhibitor of tyrosinase. Enzyme studies were conducted in both the presence and absence of dodecyl gallate and the results are shown below as Lineweaver-Burk plots.

52. Calculate the true Vmax (OD/min) and the true KM (mM) for the enzyme. A) Vmax = 0.66 OD/min; KM = 1.0 mM B) Vmax = 0.23 OD/min; KM = 0.37 mM C) Vmax = 1.51 OD/min; KM = 1.0 mM D) Vmax = 4.27 OD/min; KM = 2.75 mM

53. If the concentration of the inhibitor (dodecyl gallate) in this study is 0.031 mM, what is the value of KI? A) 0.0095 mM B) 0.017 mM C) 0.061 mM D) 0.053 mM

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Use the following to answer questions 54-55.

Lysozyme catalyzes the hydrolysis of a polysaccharide component of bacterial cell walls. The damaged bacteria subsequently lyse (rupture). Part of lysozyme's mechanism is shown below. The enzyme catalyzes cleavage of a bond between two sugar residues (represented by hexagons). Catalysis involves shown below. The enzyme catalyzes cleavage of a bond between two sugar residues (represented by hexagons). Catalysis involves the side chains of Glu 35 and Asp 52. One of the residues has a pK of 4.5; the other has a pK of 5.9. Based on this information, answer the next two questions.

54. Which of the two residues in the active site would have a pK of 4.5? A) Glu35 B) Asp52 55. Under which of the conditions listed below would lysozyme most likely be active? A) pH < 2.0 C) 2.0 < pH < 8.0 (pH between 2.0 and 8.0) B) pH > 8.0

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Answer Key - PracticeExam2_F13 1. 2. 3. 4. 5. 6. 7. 8. 9. 10. 11. 12. 13. 14. 15. 16. 17. 18. 19. 20. 21. 22. 23. 24. 25. 26. 27. 28. 29. 30. 31. 32. 33. 34. 35. 36. 37. 38. 39. 40. 41. 42. 43. 44. 45. 46. 47. 48. 49. 50. 51. 52. 53. 54. 55. A D B D A B E D B B C C A B D A B A C E A B A C C C C A D B B A B E C D C C D B B C B D A C A B A A E A B B C Page 11