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Exam 2 - Fal08 - BCH 3023 Fall 2008 Exam 2 Form C Name...

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BCH 3023 – Fall 2008 Exam 2, Form C 1 Name: ANSWER KEY In class, we discussed one method to linearize the Michaelis-Menton equation. There are other methods to do this, one being an Eadie-Hofstee plot. Given the Eadie-Hofstee plot below, answer questions 1 and 2. This plot might also help with question 3. 0 20 40 60 80 100 0 10 20 30 40 50 Eadie-Hofstee Plot of Enzyme Kinetic Data v/[S], sec -1 Rearrangement of Michaelis-Menten Equation : v = V MAX [S]/(K M + [S]) v (K M + [S]) = V MAX [S] (v /[S])(K M + [S]) = V MAX (v /[S])(K M ) + v = V MAX v = -(v /[S])(K M ) + V MAX Therefore: Slope = - K M = 2.0 mM “Y” - intercept = V MAX = 100 mM/sec “X”- intercept = V MAX /K M = 50 sec -1 1. What is the value for the K M ? a. 20 mM b. 20 μ M c. 2.0 mM d. 2.0 μ M e. 0.2 mM
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BCH 3023 – Fall 2008 Exam 2, Form C 2 2. What is the V MAX value? a. 1.0 sec/mM b. 1.0 mM/sec c. 2.0 mM/sec d. 100 mM/sec e. 1000 mM/sec 3. What is the pattern for a pure noncompetitive inhibitor on an Eadie-Hofstee plot? a. A series of parallel lines. b. A series of lines that intersect on the v/[S]-axis (the “X”-axis). c. A series of lines that intersect on the v-axis (the “Y”-axis). d. A series of lines with different slopes that do not intersect on either axis. e. A series of lines that yield different values of K M,app Pure non-competitve inhibition has no effect on the K M and V MAX decreases. Thus, the slope does not change while the intercepts on both axes decrease as [I] increases. 4. In the binding of O 2 to myoglobin, the relationship between the concentration of O 2 (or the partial pressure of O 2 ) and the fraction of binding sites occupied, θ , can best be described as: 5. A metabolic pathway proceeds according to the scheme R S T U V W. A regulatory enzyme, X, catalyzes the first reaction in the pathway. Which of the following is most likely correct for this pathway?
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BCH 3023 – Fall 2008 Exam 2, Form C 3
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