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Unformatted text preview: __________________________________ _____________________________________ Name (Last, First) SOLAR ID 1 BIO 361 EXAM 2 FALL 2008 VERSION 1 NAME:_________________________________________________ ID:_____________________________________________________ 1. Write Your name and ID on all pages 2. Write all answers in pen only 3. Make sure your exam has ten pages including this cover page Page 2 _______________ Page 3 _______________ Page 4 _______________ Page 5 _______________ Page 6 _______________ Page 7 _______________ Page 8 _______________ Page 9 _______________ Page 10 _______________ Total _______________ __________________________________ _____________________________________ Name (Last, First) SOLAR ID 2 [Questions 1-26: 3 points each except as indicated] 1. Which statement most accurately describes the consequences of forming an Enzyme-Substrate Complex according to the original ideas of Michaelis and Menten? a. the enzyme distorts the substrate b. the substrate induces a conformational change in the enzyme c. the enzyme-substrate complex is formed by the simple association of enzyme and substrate which can be reversed to release unmodified enzyme and unmodified substrate but which can also go on to undergo a catalyzed chemical transformation to product. d. the enzyme is covalently linked to the substrate in the Michaelis-type enzyme substrate complex. e. the transition state is destabilized in the enzyme-substrate complex to account for the role of the enzyme in accelerating the formation of product. 2-6. [2 points each] You have determined the Kms and the k cat s for two enzymes. Enzyme F: Km = 200 mM, k cat = 100 micromoles/sec ; Enzyme G: Km = 20 mM, k cat = 10 micromoles/sec. They both convert the same substrate to the same product. Which statements are True and which are False (please write out, not just T or F)? 2._______ If the substrate concentration were 2000 mM, you would need ten times as much of enzyme G to generate product at the same rate as you could with enzyme F. 3._______ If you had a noncompetitive inhibitor which you added only to enzyme F at a concentration to achieve 90% saturation of that enzyme by the inhibitor and the substrate concentration were 2000 mM, you would observe the same rate of product formation from equal concentrations of enzymes F and G. 4._______ Based on the kcat/Km ratios, Lineweaver-Burk plots at equal concentrations of the two enzymes in the absence of inhibitors would yield equal estimated values of Vmax. 5._______ You would find that the slopes of Lineweaver-Burk plots of the two enzymes would be equal as long as they were determined over appropriate substrate concentration ranges and at the same concentration of each of the enzymes....
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This note was uploaded on 11/19/2010 for the course BIO 361 taught by Professor Lake during the Fall '08 term at SUNY Stony Brook.
- Fall '08