Chapter 25: Lipid Metabolism Suggested problems: 1, 4, 5, 6, 8, 9

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More Lipids!
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Figure 25-19 The propionyl-CoA carboxylase
reaction.
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Figure 25-20 The rearrangement catalyzed by
methylmalonyl-CoA mutase.
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Figure 25-21 Structure of 5-deoxyadenosyl-coba
lamin (coenzyme B12).
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Figure 25-23 Proposed mechanism of
methylmalonyl-CoA mutase.
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Figure 25-28 A comparison of fatty acid ?
oxidation and fatty acid biosynthesis.
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Figure 25-29 The phosphopantetheine group in
acyl-carrier protein (ACP) and in CoA.
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Figure 25-30 Association of acetyl-CoA
carboxylase protomers.
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Figure 25-31 Reaction cycle for the biosynthesis
of fatty acids.
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Figure 25-32 The mechanism of carboncarbon
bond formation in fatty acid biosynthesis.
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Figure 25-33 Schematic diagram of the order of
the enzymatic activities along the polypeptide
chain of a monomer of fatty acid synthase (FAS).
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Figure 25-36 Transfer of acetyl-CoA from
mitochondrion to cytosol via the
tricarboxylate transport system.
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Figure 25-37 Mitochondrial fatty acid
elongation.
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Figure 25-38 The electron-transfer reactions
mediated by the D9-fatty acyl-CoA desaturase
complex.
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Figure 25-39 The reactions of triacylglycerol
biosynthesis.
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Figure 25-40 Sites of regulation of fatty acid
metabolism.
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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
proteinstimulated hydrolysis of ganglioside GM2
by hexosaminidase A.
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Figure 25-91 Cytoplasmic membranous body in a
neuron affected by TaySachs 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 glucosealanine cycle.
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Figure 26-4 The oxidative deamination of
glutamate by glutamate DH.
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Figure 26-6 Inhibition of human glutamate
dehydrogenase (GDH) by GTP.
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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 26-26 The pathway of phenylalanine
degradation.
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Figure 26-26 The pathway of phenylalanine
degradation.
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Figure 26-26 The pathway of phenylalanine
degradation.
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Figure 26-27 The pteridine ring, the nucleus of
biopterin and folate.
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Figure 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.
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Homogentisate
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Figure 26-32 Structure 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 26-49 Interconversion 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 26-51 The sequence of reactions
catalyzed by glutamate synthase.
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