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Average = 70.0 = B- Approximate Grades: A = 86+B= 73-78C = 60-64 A- = 83-85B- = 67-72C- = 55-59 B+ = 79-82C+ = 64-67
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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
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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
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Figure 18-12 A bicyclic enzyme cascade. Page 638
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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)
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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
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Figure 18-14 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
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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
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Phosphorylase Kinase Senses Ca +2 –Activated by [Ca +2 ] as low as 10 -7 M!! –4 subunits (αβγδ) 4 active structure a tetramer of tetramers! –Subunit γ has catalytic activity –Others are inhibitory –Subunit δ = Calmodulin (CaM)
![Phosphorylase Kinase Senses Ca +2 –Activated by [Ca +2 ] as low as M!.](http://images.slideplayer.com/16/5188891/slides/slide_11.jpg "–4 subunits (αβγδ) 4 active structure a tetramer of tetramers. –Subunit γ has catalytic activity –Others are inhibitory –Subunit δ = Calmodulin (CaM).")
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Figure 18-16X-Ray structure of rat testis calmodulin. Page 642
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Figure 18-17EF hand. Page 642
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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
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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
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Figure 18-19 Schematic diagram of the Ca 2+ – CaM-dependent activation of protein kinases.
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Figure 18-13Schematic diagram of the major enzymatic modification/demodification systems involved in the control of glycogen metabolism in muscle. Page 639
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Figure 18-21The antagonistic effects of insulin and epinephrine on glycogen metabolism in muscle. Page 645
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Figure 18-22The enzymatic activities of phosphorylase a and glycogen synthase in mouse liver in response to an infusion of glucose. Page 648
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Figure 18-23Comparison of the relative enzymatic activities of hexokinase and glucokinase over the physiological blood glucose range. Page 649
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Figure 18-24Formation and degradation of -D- fructose-2,6-bisphosphate as catalyzed by PFK-2 and FBPase-2. Page 649
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Figure 18-25X-ray structure of the H256A mutant of rat testis PFK-2/FBPase-2. Page 650
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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
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Figure 18-26b The liver’s response to stress. (b) The participation of two second messenger systems. Page 652
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Fig. 19-16 Receptor-mediated activation/inhibition of Adenylate Cyclase
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Figure 19-13 Activation/deactivation cycle for hormonally stimulated AC. Page 674
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Figure 19-14General structure of a G protein-coupled receptor (GPCR). Page 674
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Figure 19-51Role of PIP 2 in intracellular signaling. Page 708
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Figure 19-21Schematic diagram of a typical mammalian AC. Page 682
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Figure 19-50 Molecular formula of the phosphatidylinositides. Page 707
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Figure 19-52A phospholipase is named according to the bond that it cleaves on a glycerophospholipid. Page 709
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Figure 19-57Activation of PKC. Page 713
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Figure 19-64Insulin signal transduction. Page 719
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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)
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Table 18-1Hereditary Glycogen Storage Diseases. Page 651
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Figure 20.2
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For diffusion K eq = 1, thus G°’ = 0 Start of “reaction” equilibrium
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For diffusion K eq = 1, thus G°’ = 0
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Figure 20.3
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“non-mediated” transport
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Table 20-1
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Figure 20.4
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Figure 20-9 Valinomycin (K + complex)
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Figure 20-9 Monensin (Na + complex)
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Gramicidin A See Figure 20.11 -hemolysin (Staph. aureus) “IONOPHORES”
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Figure 20.14
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Figure 20.15
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Figure 20.18
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Table 20-3
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Figure 20.21
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Figure 20.27
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“Alfonse, Biochemistry makes my head hurt!!” \
![Alfonse, Biochemistry makes my head hurt!! \](http://images.slideplayer.com/16/5188891/slides/slide_57.jpg "Alfonse, Biochemistry makes my head hurt!! \")
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