1. Figure 17-24 Reaction mechanism of lactate dehydrogenase. Via accompan
direct hydride transfer from NADH to pyruvate’s carbonyl C
Figure Reaction mechanism of lactate dehydrogenase. Via accompan
Proton donation from His
Facilitated by Arg
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2. Figure 17-25 The two reactions of alcoholic fermentation.
Page 604

3. Figure 17-26 Thiamine pyrophosphate.
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4. Figure 17-27 Reaction mechanism of pyruvate decarboxylase.
Nucleophillic attack
elimination
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Protonation of carbanion
Voet Biochemistry 3e
© 2004 John Wiley & Sons, Inc.

5. Figure 17-29 The formation of the active ylid form of TPP in the pyruvate decarboxylase reaction.
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6. Figure The reaction mechanism of alcohol dehydrogenase involves direct hydride transfer of the pro-R hydrogen of NADH to the re face of acetaldehyde.
Page 606

7. Table 17-2 Some Effectors of the Nonequilibrium Enzymes of Glycolysis.
Please note that these are the 3 NON-reversible reactions of glycolysis.
All the others are freely reversible.
Page 613

8. Figure 17-32a. X-Ray structure of PFK
Figure 17-32a X-Ray structure of PFK. (a) A ribbon diagram showing two subunits of the tetrameric E. coli protein.
Mg+2
F6P
Page 614
ATP

9. Figure 17-33 PFK activity versus F6P concentration.
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10. Figure 17-35 Metabolism of fructose.
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11. Figure 17-36 Metabolism of galactose.
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12. Figure 17-37 Metabolism of mannose.
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13. Glycogen Metabolism
Chapter 18

14. Page 627
Figure 18-1a Structure of glycogen. (a) Molecular formula. (b) Schematic diagram illustrating its branched structure.
Page 627

15. Figure 18-2a. X-Ray structure of rabbit muscle glycogen phosphorylase
Figure 18-2a X-Ray structure of rabbit muscle glycogen phosphorylase. (a) Ribbon diagram of a phosphorylase b subunit.
Page 628

16. Figure 18-2b. X-Ray structure of rabbit muscle glycogen phosphorylase
Figure 18-2b X-Ray structure of rabbit muscle glycogen phosphorylase. (b) A ribbon diagram of the glycogen phosphorylase a dimer.
Page 628

17. Figure 18-2c. X-Ray structure of rabbit muscle glycogen phosphorylase
Figure 18-2c X-Ray structure of rabbit muscle glycogen phosphorylase. (c) An interpretive “low-resolution” drawing of Part b showing the enzyme’s various ligand-binding sites.
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18. Figure 18-3 The reaction mechanism of glycogen phosphorylase.
Page 630
Figure 18-3 The reaction mechanism of glycogen phosphorylase.

19. Figure 18-4 The mechanism of action of phosphoglucomutase.
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20. Figure 18-5 Reactions catalyzed by debranching enzyme.
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21. Figure 18-6 Reaction catalyzed by UDP–glucose pyrophos-phorylase.
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22. Figure 18-7 Reaction catalyzed by glycogen synthase.
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23. Figure 18-8 The branching of glycogen.
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24. Figure 18-9 The control of glycogen phosphorylase activity.
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25. (b) Ribbon diagram of one subunit (R-state) with bound AMP.
Figure 18-10a Conformational changes in glycogen phosphorylase. (a) Ribbon diagram of one subunit (T-state) in absence of allosteric effectors. a.
(b) Ribbon diagram of one subunit (R-state) with bound AMP. b.

26. Figure 18-10b. Conformational changes in glycogen phosphorylase
Figure 18-10b Conformational changes in glycogen phosphorylase. (b) The portion of the glycogen phosphorylase a dimer in the vicinity of the dimer interface.

27. Figure 18-11a. A monocyclic enzyme cascade
Figure 18-11a A monocyclic enzyme cascade. (a) General scheme, where F and R are, respectively, the modifying and demodifying enzymes.
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28. Figure 18-11b. A monocyclic enzyme cascade
Figure 18-11b A monocyclic enzyme cascade. (b) Chemical equations for the interconversion of the target enzyme’s unmodified and modified forms Eb and Ea.
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29. Figure 18-12 A bicyclic enzyme cascade.
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30. Figure Schematic diagram of the major enzymatic modification/demodification systems involved in the control of glycogen metabolism in muscle.
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31. Figure 18-14 X-ray structure of the catalytic (C) subunit of mouse protein kinase A (PKA).
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32. Figure 18-15 X-ray structure of the regulatory (R) subunit of bovine protein kinase A (PKA).
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33. Figure 18-16 X-Ray structure of rat testis calmodulin.
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34. Figure EF hand.
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35. Figure 18-18a. NMR structure of (Ca2+)4–CaM from Drosophila melanogaster in complex with its 26-residue target polypeptide from rabbit skeletal muscle myosin light chain kinase (MLCK). (a) A view of the complex in which the N-terminus of the target polypeptide is on the right.
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36. Figure 18-18b. NMR structure of (Ca2+)4–CaM from Drosophila melanogaster in complex with its 26-residue target polypeptide from rabbit skeletal muscle myosin light chain kinase (MLCK). (b) The perpendicular view as seen from the right side of Part a.
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37. Figure 18-19 Schematic diagram of the Ca2+–CaM-dependent activation of protein kinases.

38. Figure 18-21 The antagonistic effects of insulin and epinephrine on glycogen metabolism in muscle.
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39. Page 648
Figure The enzymatic activities of phosphorylase a and glycogen synthase in mouse liver in response to an infusion of glucose.

40. Figure Comparison of the relative enzymatic activities of hexokinase and glucokinase over the physiological blood glucose range.
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41. Figure Formation and degradation of -D-fructose-2,6-bisphosphate as catalyzed by PFK-2 and FBPase-2.
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42. Figure 18-25 X-ray structure of the H256A mutant of rat testis PFK-2/FBPase-2.
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43. Figure 18-26a. The liver’s response to stress
Figure 18-26a The liver’s response to stress. (a) Stimulation of α-adrenoreceptors by epinephrine activates phospholipase C to hydrolyze PIP2 to IP3 and DAG.
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44. Figure 18-26b. The liver’s response to stress
Figure 18-26b The liver’s response to stress. (b) The participation of two second messenger systems.
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45. Figure The ADP concentration in human forearm muscles during rest and following exertion in normal individuals and those with McArdle’s disease.
(Muscle Phosphorylase Deficiency)
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46. Table 18-1 Hereditary Glycogen Storage Diseases.
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47. “Alfonse, Biochemistry makes my head hurt!!”\