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Table 25-2Sphingolipid Storage Diseases. Page 979.

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Presentation on theme: "Table 25-2Sphingolipid Storage Diseases. Page 979."— Presentation transcript:

1 Table 25-2Sphingolipid Storage Diseases. Page 979

2 Figure 25-89 The breakdown of sphingolipids by lysosomal enzymes. Page 978

3 Figure 25-90Model for G M2 -activator protein–stimulated hydrolysis of ganglioside G M2 by hexosaminidase A. Page 978

4 Figure 25-91Cytoplasmic membranous body in a neuron affected by Tay–Sachs disease. Page 979

5 Chapter 27, Nitrogen Metabolism

6 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

7 Page 987 Figure 26-2The mechanism of PLP- dependent enzyme-catalyzed transamination.

8 Figure 26-3The glucose– alanine cycle. Page 988

9 Figure 26-4 The oxidative deamination of glutamate by glutamate DH.

10 Page 992 Figure 26-7 The urea cycle.

11 Figure 26-8The mechanism of action of CPS I. Page 993

12 Figure 26-9 X-Ray structure of E. coli carbamoyl phosphate synthetase (CPS). Page 993

13 Figure 26-10The mechanism of action of argininosuccinate synthetase. Page 994

14 Figure 26-11 Degradatio n of amino acids to one of seven common metabolic intermediates. Page 995

15 Figure 26-12 The pathways converting alanine, cysteine, glycine, serine, and threonine to pyruvate. Page 996

16 Figure 26-26 The pathway of phenylalanine degradation. Page 1009

17 Figure 26-26 The pathway of phenylalanine degradation. Page 1009

18 Figure 26-26 The pathway of phenylalanine degradation. Page 1009

19 Figure 26-27 The pteridine ring, the nucleus of biopterin and folate. Page 1009

20 Page 1010 Figure 26-28 Formation, utilization, and regeneration of 5,6,7,8- tetrahydrobiopterin (BH 4 ) in the phenylalanine hydroxylase reaction.

21 Page 1012 Figure 26-30Proposed mechanism of the NIH shift in the phenylalanine hydroxylase reaction.

22 Page 1013 Figure 26-31 The NIH shift in the p-hydroxy- phenyl- pyruvate dioxygenase reaction. Homogentisate

23 Page 1013 Figure 26-32 Structure of heme.

24 Figure 26-47Tetrahydrofolate (THF). Page 1028

25 Figure 26-48The two-stage reduction of folate to THF. Page 1028

26 Table 26-1Oxidation Levels of C 1 Groups Carried by THF. Page 1028

27 Page 1029 Figure 26-49 Interconversion of the C 1 units carried by THF.

28 Figure 26-50The biosynthetic fates of the C 1 units in the THF pool. Page 1029

29 Page 1031 Figure 26-51 The sequence of reactions catalyzed by glutamate synthase.

30 Table 26-2Essential and Nonessential Amino Acids in Humans. Page 1030 We can’t make these! We can make these!

31 Page 1033 Figure 26-54 The syntheses of alanine, aspartate, glutamate, asparagine, and glutamine.

32 Figure 26-55aX-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. Page 1034

33 Page 1035 Figure 26-56 The regulation of bacterial glutamine synthetase.

34 Figure 26-57The biosynthesis of the “glutamate family” of amino acids: arginine, ornithine, and proline. Page 1036

35 Figure 26-58The conversion of 3- phosphoglycerate to serine. Page 1037

36 Figure 26-66Photograph showing the root nodules of the legume bird’s foot trefoil. Page 1046

37 Figure 26-67X-Ray structure of the A. vinelandii nitrogenase in complex with ADP · AlF 4 . Page 1046

38 Figure 26-69The flow of electrons in the nitrogenase- catalyzed reduction of N 2. Page 1048

39 Figure 26-59aCysteine biosynthesis. (a) The synthesis of cysteine from serine in plants and microorganisms. Page 1038

40 Figure 26-59bCysteine biosynthesis. (b) The 8-electron reduction of sulfate to sulfide in E. coli. Page 1038

41 Figure 26-60The biosynthesis of the “aspartate family” of amino acids: lysine, methionine, and threonine. Page 1039

42 Table 26-3Differential Control of Aspartokinase Isoenzymes in E. Coli. Page 1041

43 Figure 26-61The biosynthesis of the “pyruvate family” of amino acids: isoleucine, leucine, and valine. Page 1040

44 Figure 26-62The biosynthesis of chorismate, the aromatic amino acid precursor. Page 1042

45 Figure 26-63The biosynthesis of phenylalanine, tryptophan, and tyrosine from chorismate. Page 1043

46 Figure 26-64A ribbon diagram of the bifunctional enzyme tryptophan synthase from S. typhimurium Page 1044

47 Figure 26-65The biosynthesis of histidine. Page 1045

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