Average = 70.0 = B- Approximate Grades: A = 86+B= 73-78C = A- = 83-85B- = 67-72C- = B+ = 79-82C+ = 64-67

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

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

Figure A bicyclic enzyme cascade. Page 638

Regulation of Glycogen Phosphorylase Allosteric control: AMP activates, Glc, G6P, ATP inhibits (T vs. R) Signal cascade: Phosphorylase Kinase Protein Kinase A Phosphoprotein phosphatase (dephosphorylates Glyc phosphorylase and Phosphorylase Kinase)

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

Figure X-ray structure of the catalytic (C) subunit of mouse protein kinase A (PKA). Page 641 PKs have KEY roles in signalling 1.7% of human genome = kinases 1000 putative kinase genes! inhibitor ATP

Figure 18-15X-ray structure of the regulatory (R) subunit of bovine protein kinase A (PKA). Page 641 Autoinhibitory domain Fits in active site of C Keeps complex inactive

Phosphorylase Kinase Senses Ca +2 –Activated by [Ca +2 ] as low as M!! –4 subunits (αβγδ) 4 active structure a tetramer of tetramers! –Subunit γ has catalytic activity –Others are inhibitory –Subunit δ = Calmodulin (CaM)

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

Figure 18-17EF hand. Page 642

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

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

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

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

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

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

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

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

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

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

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

Fig Receptor-mediated activation/inhibition of Adenylate Cyclase

Figure Activation/deactivation cycle for hormonally stimulated AC. Page 674

Figure 19-14General structure of a G protein-coupled receptor (GPCR). Page 674

Figure 19-51Role of PIP 2 in intracellular signaling. Page 708

Figure 19-21Schematic diagram of a typical mammalian AC. Page 682

Figure Molecular formula of the phosphatidylinositides. Page 707

Figure 19-52A phospholipase is named according to the bond that it cleaves on a glycerophospholipid. Page 709

Figure 19-57Activation of PKC. Page 713

Figure 19-64Insulin signal transduction. Page 719

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)

Table 18-1Hereditary Glycogen Storage Diseases. Page 651

Figure 20.2

For diffusion K eq = 1, thus  G°’ = 0 Start of “reaction” equilibrium

For diffusion K eq = 1, thus  G°’ = 0

Figure 20.3

“non-mediated” transport

Table 20-1

Figure 20.4

Figure 20-9 Valinomycin (K + complex)

Figure 20-9 Monensin (Na + complex)

Gramicidin A See Figure  -hemolysin (Staph. aureus) “IONOPHORES”

Figure 20.14

Figure 20.15

Figure 20.18

Table 20-3

Figure 20.21

Figure 20.27

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