Biochemistry: The Molecular Basis of Life
6th Edition
ISBN: 9780190209896
Author: Trudy McKee, James R. McKee
Publisher: Oxford University Press
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Chapter 9, Problem 6Q
Summary Introduction
To review:
Determining the structure of 2-hydroxyglutarate by reviewing the structures of isocitrate and alpha-ketoglutarate.
Introduction:
The citric acid cycle (or Krebs cycle) is a biochemical pathwa, yhich involves a series of enzyme-catalyzed reactions that results in the generation of high-energy compounds. Isocitrate and alpha-ketoglutarate are two of its intermediate products. The normal enzyme, isocitrate dehydrogenase (IDH), converts isocitrate into alpha-ketoglutarate. However, the mutated enzyme IDH1 converts it to 2- hydroxyglutarate. This enzyme is present in high concentration in patients suffering from brain cancer (glioblastoma).
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A mutated IDH1 isoenzyme is found in a high percentage of a type of brain cancer called glioblastoma. Instead of converting isocitrate to α-ketoglutarate, mutated IDH1 converts its substrate to 2-hydroxyglutarate, a circumstance that disrupts the citric acid cycle, among other effects. Review the structures of isocitrate and α-ketoglutarate and determine the structure of 2- hydroxyglutarate
Which reaction in the citric acid cycle is most analogous to the oxidative decarboxylation of 6- phosphogluconate to ribulose 5-phosphate? What kind of enzymebound intermediate is formed in both reactions?
Identify at least five biological effects of disorders of the citric acid cycle
Chapter 9 Solutions
Biochemistry: The Molecular Basis of Life
Ch. 9 - Prob. 1QCh. 9 - Prob. 2QCh. 9 - Prob. 3QCh. 9 - Prob. 4QCh. 9 - Prob. 5QCh. 9 - Prob. 6QCh. 9 - Prob. 7QCh. 9 - Prob. 1RQCh. 9 - Prob. 2RQCh. 9 - Prob. 3RQ
Ch. 9 - Prob. 4RQCh. 9 - Prob. 5RQCh. 9 - Prob. 6RQCh. 9 - Prob. 7RQCh. 9 - Prob. 8RQCh. 9 - Prob. 9RQCh. 9 - Prob. 10RQCh. 9 - Prob. 11RQCh. 9 - Prob. 12RQCh. 9 - Prob. 13RQCh. 9 - Prob. 14RQCh. 9 - Prob. 15RQCh. 9 - Prob. 16RQCh. 9 - Prob. 17RQCh. 9 - Prob. 18RQCh. 9 - Prob. 19RQCh. 9 - Prob. 20RQCh. 9 - Prob. 21RQCh. 9 - Prob. 22RQCh. 9 - Prob. 23RQCh. 9 - Prob. 24RQCh. 9 - Prob. 25RQCh. 9 - Prob. 26RQCh. 9 - Prob. 27RQCh. 9 - Prob. 28FBCh. 9 - Prob. 29FBCh. 9 - Prob. 30FBCh. 9 - Prob. 31FBCh. 9 - Prob. 32FBCh. 9 - Prob. 33FBCh. 9 - Prob. 34FBCh. 9 - Prob. 35FBCh. 9 - Prob. 36FBCh. 9 - Prob. 37FBCh. 9 - Prob. 38SACh. 9 - Prob. 39SACh. 9 - Prob. 40SACh. 9 - Prob. 41SACh. 9 - Prob. 42SACh. 9 - Prob. 43TQCh. 9 - Prob. 44TQCh. 9 - Prob. 45TQCh. 9 - Prob. 46TQCh. 9 - Prob. 47TQCh. 9 - Prob. 48TQCh. 9 - Prob. 49TQCh. 9 - Prob. 50TQCh. 9 - Prob. 51TQCh. 9 - Prob. 52TQCh. 9 - Prob. 53TQCh. 9 - Prob. 54TQCh. 9 - Prob. 55TQCh. 9 - Prob. 56TQCh. 9 - Prob. 57TQCh. 9 - Prob. 58TQCh. 9 - Prob. 59TQ
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- Although most enzymes are quite specific, they can catalyze side reactions with compounds that are structurally similar to their physiological substrates, but usually at much slower rates. For example, glyceraldehyde- 3-phosphate dehydrogenase (GAPDH), which normally catalyzes the oxidative phosphorylation of glyceraldehyde-3-phosphate, can slowly convert erythrose-4-phosphate, an intermediate in the pentose phosphate pathway, to 1,4-bisphosphoerythronate: Draw a plausible mechanism for this side reaction of GAPDH.arrow_forwardIf glutamate were labeled with C-14 at the delta-carbon and added via transamination to the citric acid cycle to produce alpha-ketoglutarate, how long would it take for the compounds containing C-14 to be reduced by 25% (assume 10 seconds per turn of the cycle)?arrow_forwardThe reaction catalyzed by malate dehydrogenase has a ΔG°′ value of +29.7 kJ⋅mol−1. Given what this says about the occurrence of the reaction catalyzed by malate dehydrogenase in cells explain how the reaction catalyzed by citrate synthase (−31.5 kJ⋅mol−1) influences that activity of malate dehydrogenase. In addition, explain how the activity of citrate synthase functions as a regulatory point for the citric acid cyclearrow_forward
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