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

4. Figure 18-2cX-Ray structure of rabbit muscle glycogen phosphorylase. (c) An interpretive “low- resolution” drawing of Part b showing the enzyme’s various ligand-binding sites. Page 628

5. Pyridoxal Phosphate

6. Figure 18-3 The reaction mechanism of glycogen phosphorylase. Page 630

7. Figure 18-4The mechanism of action of phosphoglucomutase. Page 631

8. Figure 18-5 Reactions catalyzed by debranching enzyme. Page 631

9. Figure 18-6 Reaction catalyzed by UDP–glucose pyrophos- phorylase. Page 633

10. Figure 18-7Reaction catalyzed by glycogen synthase. Page 633

11. Figure 18-8The branching of glycogen. Page 634

12. Figure 18-9The control of glycogen phosphorylase activity. Page 635

13. Figure 18-10a Conformationa l 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.

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

15. Figure 18-11aA monocyclic enzyme cascade. (a) General scheme, where F and R are, respectively, the modifying and demodifying enzymes. Page 637

16. Figure 18-11bA monocyclic enzyme cascade. (b) Chemical equations for the interconversion of the target enzyme’s unmodified and modified forms E b and E a. Page 637

17. Figure 18-12 A bicyclic enzyme cascade. Page 638

18. Figure 18-13Schematic diagram of the major enzymatic modification/demodification systems involved in the control of glycogen metabolism in muscle. Page 639

19. Figure 18-14 X-ray structure of the catalytic (C) subunit of mouse protein kinase A (PKA). Page 641

20. Figure 18-15X-ray structure of the regulatory (R) subunit of bovine protein kinase A (PKA). Page 641

21. Figure 18-16X-Ray structure of rat testis calmodulin. Page 642

22. Figure 18-17EF hand. Page 642

23. Figure 18-18a. NMR structure of (Ca 2+ ) 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. Page 643

24. Figure 18-18b. NMR structure of (Ca 2+ ) 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. Page 643

25. Figure 18-19 Schematic diagram of the Ca 2+ – CaM-dependent activation of protein kinases.

26. Figure 18-21The antagonistic effects of insulin and epinephrine on glycogen metabolism in muscle. Page 645

27. Figure 18-22The enzymatic activities of phosphorylase a and glycogen synthase in mouse liver in response to an infusion of glucose. Page 648

28. Figure 18-23Comparison of the relative enzymatic activities of hexokinase and glucokinase over the physiological blood glucose range. Page 649

29. Figure 18-24Formation and degradation of  -D- fructose-2,6-bisphosphate as catalyzed by PFK-2 and FBPase-2. Page 649

30. Figure 18-25X-ray structure of the H256A mutant of rat testis PFK-2/FBPase-2. Page 650

31. Figure 18-26a The liver’s response to stress. (a) Stimulation of α-adrenoreceptors by epinephrine activates phospholipase C to hydrolyze PIP 2 to IP 3 and DAG. Page 652

32. Figure 18-26b The liver’s response to stress. (b) The participation of two second messenger systems. Page 652

33. Figure 18-27The ADP concentration in human forearm muscles during rest and following exertion in normal individuals and those with McArdle’s disease. Page 653 (Muscle Phosphorylase Deficiency)

34. Table 18-1Hereditary Glycogen Storage Diseases. Page 651

35. “Alfonse, Biochemistry makes my head hurt!!” \