pyruvate dehydrogenase and citrate cycle practice problems

pyruvate dehydrogenase and citrate cycle practice problems...

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Pyruvate Dehydrogenase and Citrate Cycle Practice Problems Reading Chapter 17 End of the chapter questions End of chapter (499-501): 5, 6, 9, 15 (focus on part a and d) Then try these: 1. What are the advantage of using a multisubunit complex (i.e. the pyruvate dehydrogenase complex) to catalyze the conversion of pyruvate to acetyl CoA? 2. The conversion of malate to oxaloacetate in reaction 8 of the citrate cycle has a Δ G °’ = + 29.7 kJ/mol yet the reaction process from malate to oxaloacetate. Explain how this is possible. 3. The citrate cycle only operates under aerobic conditions even though O 2 does not participate directly in any step in the cycle. Why is this so? 4. Lipoic acid and FAD serve as catalytic coenzymes for the enzyme isocitrate dehydrogenase. Based on your knowledge of the pyruvate dehydrogenase mechanism, propose a role for each of the coenzymes.
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Unformatted text preview: 5. The disease beriberi results from a lack of thiamin in the diet. What two metabolites would you expect to accumulate in individuals with beriberi after ingesting glucose. 6. Explain why it makes sense that citrate inhibits the key glycolytic enzyme phosphofructokinase I. 7. When I was taking biochemistry as an undergraduate, succinyl-CoA synthase, which catalyzes the conversion of succinyl-CoA to succinate in a reaction that yields 1 molecule of GTP, was called succinate thiokinase. Why can this enzyme be classified as a kinase? 8. Explain why plants must have an active glyoxylate pathway but this pathway is not necessary (and in fact not present) in animals. 9. Why have some proposed to develop inhibitors of enzymes in the glyoxylate pathway as antimicrobial agents? What type pathogens might be susceptible to this type of inhibitor?...
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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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