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More Lipids!. Figure 25-19 The propionyl-CoA carboxylase reaction. Page 922. Figure 25-20 The rearrangement catalyzed by methylmalonyl-CoA mutase. Page 923. Figure 25-21 Structure of 5’-deoxyadenosyl- cobalamin (coenzyme B 12 ). Page 923.
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Figure 25-19The propionyl-CoA carboxylase reaction. Page 922
Figure 25-20 The rearrangement catalyzed by methylmalonyl-CoA mutase. Page 923
Figure 25-21Structure of 5’-deoxyadenosyl-cobalamin (coenzyme B12). Page 923
Figure 25-23Proposed mechanism of methylmalonyl-CoA mutase. Page 926
Figure 25-28 A comparison of fatty acid oxidation and fatty acid biosynthesis. Page 931
Figure 25-29 The phosphopantetheine group in acyl-carrier protein (ACP) and in CoA. Page 931
Figure 25-30 Association of acetyl-CoA carboxylase protomers. Page 932
Figure 25-31 Reaction cycle for the biosynthesis of fatty acids. Page 933
Figure 25-32The mechanism of carbon–carbon bond formation in fatty acid biosynthesis. Page 934
Figure 25-33 Schematic diagram of the order of the enzymatic activities along the polypeptide chain of a monomer of fatty acid synthase (FAS). Page 935
Figure 25-36Transfer of acetyl-CoA from mitochondrion to cytosol via the tricarboxylate transport system. Page 937
Figure 25-38 The electron-transfer reactions mediated by the D9-fatty acyl-CoA desaturase complex. Page 938
Figure 25-39The reactions of triacylglycerol biosynthesis. Page 939
Figure 25-40Sites of regulation of fatty acid metabolism. Page 941
Figure 25-89 The breakdown of sphingolipids by lysosomal enzymes. Page 978
Figure 25-90 Model for GM2-activator protein–stimulated hydrolysis of ganglioside GM2 by hexosaminidase A. Page 978
Figure 25-91 Cytoplasmic membranous body in a neuron affected by Tay–Sachs disease. Page 979
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.. Page 986
Figure 26-2 The mechanism of PLP- dependent enzyme-catalyzed transamination. Page 987
Figure 26-4 The oxidative deamination of glutamate by glutamate DH.
Figure 26-6 Inhibition of human glutamate dehydrogenase (GDH) by GTP. Page 990
Page 992 Figure 26-7The urea cycle.
Figure 26-9X-Ray structure of E. coli carbamoyl phosphate synthetase (CPS). Page 993
Figure 26-10 The mechanism of action of argininosuccinate synthetase. Page 994
Figure 26-11 Degradation of amino acids to one of seven common metabolic intermediates. Page 995
Figure 26-12 The pathways converting alanine, cysteine, glycine, serine, and threonine to pyruvate. Page 996
Figure 26-26The pathway of phenylalanine degradation. Page 1009
Figure 26-26The pathway of phenylalanine degradation. Page 1009
Figure 26-26The pathway of phenylalanine degradation. Page 1009
Figure 26-27 The pteridine ring, the nucleus of biopterin and folate. Page 1009
Figure 26-28 Formation, utilization, and regeneration of 5,6,7,8- tetrahydrobiopterin (BH4) in the phenylalanine hydroxylase reaction. Page 1010
Page 1012 Figure 26-30 Proposed mechanism of the NIH shift in the phenylalanine hydroxylase reaction.
Figure 26-31 The NIH shift in the p-hydroxy- phenyl- pyruvate dioxygenase reaction. Page 1013 Homogentisate
Figure 26-32 Structure of heme. Page 1013
Figure 26-47 Tetrahydrofolate (THF). Page 1028
Figure 26-48 The two-stage reduction of folate to THF. Page 1028
Table 26-1Oxidation Levels of C1 Groups Carried by THF. Page 1028
Figure 26-49 Interconversion of the C1 units carried by THF. Page 1029
Figure 26-50 The biosynthetic fates of the C1 units in the THF pool. Page 1029
Figure 26-51 The sequence of reactions catalyzed by glutamate synthase. Page 1031
