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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 Page 603
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Figure 17-25 The two reactions of alcoholic fermentation.
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Figure 17-26 Thiamine pyrophosphate.
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Figure 17-27 Reaction mechanism of pyruvate decarboxylase.
Nucleophillic attack elimination Page 605 Protonation of carbanion Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc.
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Figure 17-29 The formation of the active ylid form of TPP in the pyruvate decarboxylase reaction.
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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
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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
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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
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Figure 17-33 PFK activity versus F6P concentration.
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Figure 17-35 Metabolism of fructose.
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Figure 17-36 Metabolism of galactose.
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Figure 17-37 Metabolism of mannose.
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Glycogen Metabolism Chapter 18
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Page 627 Figure 18-1a Structure of glycogen. (a) Molecular formula. (b) Schematic diagram illustrating its branched structure. Page 627
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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
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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
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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. Page 628
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Figure 18-3 The reaction mechanism of glycogen phosphorylase.
Page 630 Figure 18-3 The reaction mechanism of glycogen phosphorylase.
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Figure 18-4 The mechanism of action of phosphoglucomutase.
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Figure 18-5 Reactions catalyzed by debranching enzyme.
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Figure 18-6 Reaction catalyzed by UDP–glucose pyrophos-phorylase.
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Figure 18-7 Reaction catalyzed by glycogen synthase.
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Figure 18-8 The branching of glycogen.
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Figure 18-9 The control of glycogen phosphorylase activity.
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(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.
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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.
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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. Page 637
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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. Page 637
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Figure 18-12 A bicyclic enzyme cascade.
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Figure Schematic diagram of the major enzymatic modification/demodification systems involved in the control of glycogen metabolism in muscle. Page 639
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Figure 18-14 X-ray structure of the catalytic (C) subunit of mouse protein kinase A (PKA).
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Figure 18-15 X-ray structure of the regulatory (R) subunit of bovine protein kinase A (PKA).
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Figure 18-16 X-Ray structure of rat testis calmodulin.
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Figure EF hand. Page 642
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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. Page 643
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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. Page 643
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Figure 18-19 Schematic diagram of the Ca2+–CaM-dependent activation of protein kinases.
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Figure 18-21 The antagonistic effects of insulin and epinephrine on glycogen metabolism in muscle.
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Page 648 Figure The enzymatic activities of phosphorylase a and glycogen synthase in mouse liver in response to an infusion of glucose.
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Figure Comparison of the relative enzymatic activities of hexokinase and glucokinase over the physiological blood glucose range. Page 649
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Figure Formation and degradation of -D-fructose-2,6-bisphosphate as catalyzed by PFK-2 and FBPase-2. Page 649
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Figure 18-25 X-ray structure of the H256A mutant of rat testis PFK-2/FBPase-2.
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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. Page 652
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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. Page 652
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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) Page 653
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Table 18-1 Hereditary Glycogen Storage Diseases.
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“Alfonse, Biochemistry makes my head hurt!!”
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