1 / 42

Figure 28-1 The biosynthetic origins of purine ring atoms.

Page 1069. Figure 28-1 The biosynthetic origins of purine ring atoms. Page 1071. Figure 28-2 The metabolic pathway for the de novo biosynthesis of IMP. Page 1072. Figure 28-3 The proposed mechanism of formylglycinamide ribotide (FGAM) synthetase. Page 1074.

Mercy
Télécharger la présentation

Figure 28-1 The biosynthetic origins of purine ring atoms.

An Image/Link below is provided (as is) to download presentation Download Policy: Content on the Website is provided to you AS IS for your information and personal use and may not be sold / licensed / shared on other websites without getting consent from its author. Content is provided to you AS IS for your information and personal use only. Download presentation by click this link. While downloading, if for some reason you are not able to download a presentation, the publisher may have deleted the file from their server. During download, if you can't get a presentation, the file might be deleted by the publisher.

E N D

Presentation Transcript


  1. Page 1069 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-1 The biosynthetic origins of purine ring atoms.

  2. Page 1071 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-2 The metabolic pathway for the de novo biosynthesis of IMP.

  3. Page 1072 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-3 The proposed mechanism of formylglycinamide ribotide (FGAM) synthetase.

  4. Page 1074 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-4 IMP is converted to AMP or GMP in separate two-reaction pathways.

  5. Page 1075 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-5 Control network for the purine biosynthesis pathway.

  6. Page 1077 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-6 The biosynthetic origins of pyrimidine ring atoms.

  7. Page 1077 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-7 Metabolic pathway for the de novo synthesis of UMP.

  8. Page 1078 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-8 Reactions catalyzed by eukaryotic dihydroorotate dehydrogenase.

  9. Page 1079 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-9 Proposed catalytic mechanism for OMP decarboxylase.

  10. Page 1080 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-10 Synthesis of CTP from UTP.

  11. Page 1080 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-11 Regulation of pyrimidine biosynthesis. The control networks are shown for (a) E. coli and (b) animals.

  12. Page 1082 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-12a Class I ribonucleotide reductase from E. coli. (a) A schematic diagram of its quaternary structure.

  13. Page 1082 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-12bClass I ribonucleotide reductase from E. coli. (b) The X-ray structure of R22.

  14. Page 1082 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-12c Class I ribonucleotide reductase from E. coli. (c) The binuclear Fe(III) complex of R2.

  15. Page 1082 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-12d Class I ribonucleotide reductase from E. coli. (d) The X-ray structure of the R1 dimer.

  16. Page 1083 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-13 Enzymatic mechanism of ribonucleotide reductase.

  17. Page 1085 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-14a Ribonucleotide reductase regulation. (a) A model for the allosteric regulation of Class I RNR via its oligomerization.

  18. Page 1085 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-14b Ribonucleotide reductase regulation. (b) The X-ray structure of the R1 hexamer, which has D3 symmetry, in complex with ADPNP as viewed along its 3-fold axis.

  19. Page 1085 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-14c Ribonucleotide reductase regulation. (c) The R1·ADPNP hexamer as viewed along the vertical 2-fold axis in Part b.

  20. Page 1086 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-15 X-Ray structure of human thioredoxin in its reduced (sulfhydryl) state.

  21. Page 1087 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-16 Electron-transfer pathway for nucleoside diphosphate (NDP) reduction.

  22. Page 1087 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-17a X-Ray structures of E. coli thioredoxin reductase (TrxR). (a) The C138S mutant TrxR in complex with NADP+.

  23. Page 1087 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-17b The C135S mutant thioredoxin reductase (TrxR) in complex with AADP+, disulfide-linked to the C35S mutant of Trx.

  24. Page 1089 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-18a X-Ray structure of human dUTPase. (a) The molecular surface at the substrate binding site showing how the enzyme differentiates uracil from thymine.

  25. Page 1089 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-18b X-Ray structure of human dUTPase. (b) The substrate binding site indicating how the enzyme differentiates uracil from cytosine and 2-deoxyribose from ribose.

  26. Page 1090 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-19 Catalytic mechanism of thymidylate synthase.

  27. Page 1091 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-20 The X-ray structure of the E. coli thymidylate synthase–FdUMP–THF ternary complex.

  28. Page 1091 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-21 Regeneration of N5,N10-methylenetetrahydrofolate.

  29. Page 1091 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-22 Ribbon diagram of human dihydrofolate reductase in complex with folate.

  30. Page 1093 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-23 Major pathways of purine catabolism in animals.

  31. Page 1094 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-24a Structure and mechanism of adenosine deaminase. (a) A ribbon diagram of murine adenosine deaminase in complex with its transition state analog HDPR.

  32. Page 1094 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-24b Structure and mechanism of adenosine deaminase. (b) The proposed catalytic mechanism of adenosine deaminase.

  33. Page 1095 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-25 The purine nucleotide cycle.

  34. Page 1095 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-26a X-Ray structure of xanthine oxidase from cow’s milk in complex with salicylic acid. (a) Ribbon diagram of its 1332-residue subunit.

  35. Page 1095 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-26b X-Ray structure of xanthine oxidase from cow’s milk in complex with salicylic acid. (b) The enzyme’s redox cofactors and salicylic acid (Sal).

  36. Page 1096 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-27 Mechanism of xanthine oxidase.

  37. Page 1097 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-28 Degradation of uric acid to ammonia.

  38. Page 1097 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-29The Gout, a cartoon by James Gilroy (1799).

  39. Page 1098 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-30 Major pathways of pyrimidine catabolism in animals.

  40. Page 1099 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-31 Pathways for the biosynthesis of NAD+ and NADP+.

  41. Page 1100 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-32 Biosynthesis of FMN and FAD from the vitamin precursor riboflavin.

  42. Page 1101 Voet Biochemistry 3e © 2004 John Wiley & Sons, Inc. Figure 28-33 Biosynthesis of coenzyme A from pantothenate, its vitamin precursor.

More Related