exam 1 key #2 spring 2010

exam 1 key #2 spring 2010 - Feb 26, 2010, BIOC 460, Exam #1...

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Feb 26, 2010, BIOC 460, Exam #1 Form A NAME Key page 3 D. The researchers discover an inhibitor for this protein . Below is the double reciprocal (Lineweaver-Burk) plot, 1/V o vs. 1/[Substrate] for the enzyme in the absence of any inhibitor, and in the presence of an inhibitor. i. ( 4pts ) What is K M for this enzyme in the presence of inhibitor ? Indicate how you obtained your answer. (No credit without explanation) State units of answer . 0.5 mM = – 1/x intercept (State units for full credit) ii. ( 4pts ) This inhibitor is a transition state analog. Based on chymotrypsin mechanism, how would you expect this inhibitor to interact with Serpro? Transition state analog are bound more tightly than the substrate. This inhibitor could be binding in an “oxyanion hole”, with new hydrogen bonds formed from enzyme backbone N–H groups to bind the –O– (oxyanion) of the inhibitor. Problem 5: Figure on the right shows the mechanism by which enzyme ABC converts its substrate to product A. ( 4pts ) What is the role of LYS in this mechanism (step 1)? Explain your reasoning. Abstract a proton, general base catalyst
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This note was uploaded on 05/06/2010 for the course BIOC 460 taught by Professor Ziegler during the Spring '07 term at University of Arizona- Tucson.

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exam 1 key #2 spring 2010 - Feb 26, 2010, BIOC 460, Exam #1...

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