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Table 25-2 Sphingolipid Storage Diseases.
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Figure 25-89 The breakdown of sphingolipids by lysosomal enzymes.
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Figure 25-90 Model for GM2-activator protein–stimulated hydrolysis of
ganglioside GM2 by hexosaminidase A.
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Figure 25-91 Cytoplasmic membranous body in a neuron
affected by Tay–Sachs disease.
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Chapter 27, Nitrogen Metabolism
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Figure 26-1 Forms of pyridoxal-5’-phosphate.(a) Pyridoxine (vitamin B6) and (b) Pyridoxal-5’-phosphate
(PLP) (c) Pyridoxamine-5’-phosphate (PMP) and (d) The Schiff base that forms between PLP and an enzyme -
amino group..
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Figure 26-2 The mechanism of PLP-dependent enzyme-catalyzed transamination.
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Figure 26-3 The glucose–alanine cycle.
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Figure 26-4 The oxidative deamination of glutamate by glutamate DH.
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Figure 26-7The urea cycle.
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Figure 26-8 The mechanism of action of CPS I.
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Figure 26-9 X-Ray structure of E. coli carbamoyl phosphate synthetase (CPS).
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Figure 26-10 The mechanism of action of argininosuccinate
synthetase.
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Figure 26-11
Degradation of amino acids
to one of seven
common metabolic
intermediates.
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Figure 26-12 The
pathways converting
alanine, cysteine, glycine,
serine, and threonine to
pyruvate.
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Figure 26-26The pathway of phenylalanine degradation.
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Figure 26-26The pathway of phenylalanine degradation.
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Figure 26-26The pathway of phenylalanine degradation.
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Figure 26-27 The
pteridine ring, the
nucleus of biopterin
and folate.
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10Figure 26-28 Formation, utilization, and regeneration of 5,6,7,8-tetrahydrobiopterin (BH4) in the phenylalanine hydroxylase reaction.
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Figure 26-30 Proposed mechanism of the NIH shift in the phenylalanine hydroxylase reaction.
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Figure 26-31 The NIH shift in the p-hydroxy-phenyl-pyruvate dioxygenase reaction.
Homogentisate
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Figure 26-32Structure of heme.
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Figure 26-47 Tetrahydrofolate (THF).
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Figure 26-48 The two-stage reduction of folate to THF.
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Table 26-1 Oxidation Levels of C1 Groups Carried by THF.
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Figure 26-49Interconversion of the C1 units carried by THF.
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Figure 26-50 The biosynthetic fates of the C1 units in the THF
pool.
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Figure 26-51The sequence of reactions catalyzed by glutamate synthase.
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Table 26-2 Essential and Nonessential Amino Acids in Humans.
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We can’t make these! We can
makethese!
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Figure 26-54The syntheses of alanine, aspartate, glutamate, asparagine, and glutamine.
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Figure 26-55a X-Ray structure of S. typhimurium glutamine synthetase.
(a) View down the 6-fold axis of symmetry showing only the six subunits of the upper ring in alternating blue and
green.
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35Figure 26-56The regulation of bacterial glutamine synthetase.
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Figure 26-57The biosynthesis of the “glutamate family” of amino acids: arginine, ornithine, and
proline.
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Figure 26-58The conversion of
3-phosphoglycerate
to serine.
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Figure 26-66 Photograph showing the root nodules of the
legume bird’s foot trefoil.
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Figure 26-67 X-Ray structure of the A. vinelandii nitrogenase in
complex with ADP · AlF4 .
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Figure 26-69 The flow of electrons in the nitrogenase-catalyzed reduction of N2.
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Figure 26-59a Cysteine biosynthesis. (a) The synthesis of cysteine from serine in plants and
microorganisms.
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Figure 26-59b Cysteine biosynthesis. (b) The 8-electron reduction of sulfate to sulfide in
E. coli.
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Figure 26-60 The biosynthesis of the “aspartate family” of
amino acids: lysine, methionine, and threonine.
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Table 26-3 Differential Control of Aspartokinase Isoenzymes in
E. Coli.
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Figure 26-61 The biosynthesis of the “pyruvate family” of
amino acids: isoleucine, leucine, and valine.
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Figure 26-62 The biosynthesis of chorismate, the aromatic
amino acid precursor.
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Figure 26-63 The biosynthesis of phenylalanine, tryptophan, and
tyrosine from chorismate.
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Figure 26-64 A ribbon diagram of the bifunctional enzyme tryptophan synthase
from S. typhimurium
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Figure 26-65 The biosynthesis of histidine.
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