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

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Chapter 25 Lipid MetabolismSuggested
problems 1, 4, 5, 6, 8, 9
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Table 25-1 Energy Content of Food Constituents.
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Figure 25-1 Mechanism of interfacial activation
of triacylglycerol lipase in complex with
procolipase.
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Figure 25-2 Catalytic action of phospholipase A2.
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Figure 25-3a Substrate binding to phospholipase
A2. (a) A hypothetical model of phospholipase A2
in complex with a micelle of lysophosphatidylethan
olamine.
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Figure 25-3b Substrate binding to phospholipase
A2.(b) Schematic diagram of a productive
interaction between phospholipase A2 and a
phospholipid contained in a micelle.
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Figure 25-4b Structure and mechanism of
phospholipase A2. (b) The catalytic mechanism of
phospholipase A2.
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Figure 25-7 X-Ray structure of human serum
albumin in complex with 7 molecules of palmitic
acid.
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Figure 25-8 Franz Knoops classic experiment
indicating that fatty acids are metabolically
oxidized at their b-carbon atom.
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Figure 25-9 Mechanism of fatty acid activation
catalyzed by acyl-CoA synthetase.
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Figure 25-10 Acylation of carnitine catalyzed by
carnitine palmitoyltransferase.
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Figure 25-11 Transport of fatty acids into the
mitochondrion.
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Figure 25-12 The ?-oxidation pathway of fatty
acyl-CoA.
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Figure 25-14 Metabolic conversions of hypoglycin
A to yield a product that inactivates acyl-CoA
dehydrogenase.
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Figure 25-15 Mechanism of action of
?-ketoacyl-CoA thiolase.
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Figure 25-16 Structures of two common unsaturated
fatty acids.
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Figure 25-17 Problems in the oxidation of
unsaturated fatty acids and their solutions.
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Figure 25-18 Conversion of propionyl-CoA to
succinyl-CoA.
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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 25-25 Ketogenesis the enzymatic
reactions forming acetoacetate from acetyl-CoA.
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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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Figure 25-41 All of cholesterols carbon atoms
are derived from acetate.
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Figure 25-42 Squalene. (a) Extended conformation.
Each box contains one isoprene unit. (b) Folded
in preparation for cyclization as predicted by
Bloch and Woodward.
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Figure 25-43 The branched pathway of
isoprenoid metabolism in mammalian cells.
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Figure 25-57 LDL receptor-mediated endocytosis in
mammalian cells.
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Figure 25-59 Control of plasma LDL production and
uptake by liver LDL receptors. (a) Normal human
subjects. (b) Familial hypercholesterolemia (FH).
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Figure 25-59c Control of plasma LDL production
and uptake by liver LDL receptors. (c) Long-term
high-cholesterol diet.
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Figure 25-60 Competitive inhibitors of HMG-CoA
reductase used for the treatment of
hypercholesterolemia.
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Figure 25-61 Simplified scheme of steroid
biosynthesis.
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Figure 25-62 Structures of the major bile acids
and their glycine and taurine conjugates.
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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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