Metalloenzymes: From Bench to Bedside offers a thorough overview of metalloenzymes, spanning biochemical and structural features, pharmacology, and biotechnological applications. After a brief overview, international experts in the field discuss a wide range of magnesium, calcium, zinc, manganese, nickel, iron, copper, cadmium, molybdenum, and tungsten enzymes, along with catalytic roles within their active sites. With a uniform approach throughout, each chapter includes the structure and function of the enzyme, physiologic and pathologic roles, inhibitors and activators of the enzyme (and their design), and clinical agents or compounds applied in medicine and drug discovery. This book enables scientists across academia and industry to adopt ongoing metalloenzyme research, and continuous discovery of novel metalloenzymes, in new life science studies and clinical applications.
1. Chapter 1: Introduction to metalloenzymes: From bench to bedside - p. 3 2. Section B: Magnesium and calcium-containing enzymes - p. 5 3. Chapter 2.1: DNA and RNA polymerases - p. 9 4. Chapter 2.2: Reverse transcriptase - p. 23 5. Chapter 2.3: Integrase - p. 35 6. Chapter 2.4: Cyclin-dependent kinase 2 (CDK2) - p. 51 7. Chapter 2.5: Catechol-O-methyltransferase (COMT) - p. 63 8. Chapter 2.6: d-Alanine-d-alanine ligase - p. 83 9. Chapter 2.7: Paraoxonases - p. 93 10. Chapter 2.8: Phospholipases A2 - p. 101 11. Section C: Zinc enzymes - p. 136 12. Chapter 3.1: Carbonic anhydrases - p. 139 13. Chapter 3.2: Metallo-β-lactamases - p. 157 14. Chapter 3.3: Bacterial zinc proteases - p. 185 15. Chapter 3.4: Matrix metalloproteases - p. 197 16. Chapter 3.5: A disintegrin and metalloproteinases (ADAMs) and tumor necrosis factor-alpha-converting enzyme (TACE) - p. 207 17. Chapter 3.6: Angiotensin-converting enzyme - p. 239 18. Chapter 3.7: Histidinol dehydrogenase - p. 255 19. Chapter 3.8: Histone deacetylases and other epigenetic targets - p. 265 20. Chapter 3.9: CD73 (5′-Ectonucleotidase) - p. 283 21. Chapter 3.10: Glyoxalase II - p. 293 22. Chapter 3.11: Glutamate carboxypeptidase II - p. 305 23. Chapter 3.12: Neutral endopeptidase (neprilysin) - p. 321 24. Section D: Other metalloenzymes - p. 330 25. Chapter 4.1: The role of arginase in human health and disease - p. 333 26. Chapter 4.2: Methionine aminopeptidases - p. 343 27. Chapter 4.3: 1-Deoxy-d-xylulose 5-phosphate reductoisomerase, the first committed enzyme in the MEP terpenoid biosynthetic pathway—Its chemical mechanism and inhibition - p. 375 28. Section E: Nickel enzymes - p. 390 29. Chapter 5.1: Urease - p. 393 30. Chapter 5.2: Methyl-coenzyme M reductase - p. 411 31. Section F: Iron enzymes (heme-containing) - p. 427 32. Chapter 6.1: Cyclooxygenase - p. 431 33. Chapter 6.2: Cytochrome P450 (inhibitors for the metabolism of drugs) - p. 449 34. Chapter 6.3: Aromatase - p. 459 35. Section G: Iron enzymes, non-heme containing - p. 464 36. Chapter 7.1: Nonheme mono- and dioxygenases - p. 467 37. Chapter 7.2: Indoleamine 2,3-dioxygenase - p. 485 38. Section H: Copper enzymes - p. 519 39. Chapter 8.1: Superoxide dismutases inhibitors - p. 523 40. Chapter 8.2: Tyrosinase enzyme and its inhibitors: An update of the literature - p. 533 41. Section I: Cadmium enzymes CAs - p. 546 42. Chapter 9: CDCA1, a versatile member of the ζ-class of carbonic anhydrase family - p. 549 43. Section J: Molybdenum enzymes - p. 554 44. Chapter 10: Molybdenum enzymes - p. 557 45. Section K: Tungsten-containing enzymes - p. 580 46. Chapter 11: Tungsten-containing enzymes - p. 583 47. Index - p. 603
Metalloenzymes: From Bench to Bedside offers a thorough overview of metalloenzymes, spanning biochemical and structural features, pharmacology, and biotechnological applications. After a brief overview, international experts in the field discuss a wide range of magnesium, calcium, zinc, manganese, nickel, iron, copper, cadmium, molybdenum, and tungsten enzymes, along with catalytic roles within their active sites. With a uniform approach throughout, each chapter includes the structure and function of the enzyme, physiologic and pathologic roles, inhibitors and activators of the enzyme (and their design), and clinical agents or compounds applied in medicine and drug discovery. This book enables scientists across academia and industry to adopt ongoing metalloenzyme research, and continuous discovery of novel metalloenzymes, in new life science studies and clinical applications.
1. Chapter 1: Introduction to metalloenzymes: From bench to bedside - p. 3 2. Section B: Magnesium and calcium-containing enzymes - p. 5 3. Chapter 2.1: DNA and RNA polymerases - p. 9 4. Chapter 2.2: Reverse transcriptase - p. 23 5. Chapter 2.3: Integrase - p. 35 6. Chapter 2.4: Cyclin-dependent kinase 2 (CDK2) - p. 51 7. Chapter 2.5: Catechol-O-methyltransferase (COMT) - p. 63 8. Chapter 2.6: d-Alanine-d-alanine ligase - p. 83 9. Chapter 2.7: Paraoxonases - p. 93 10. Chapter 2.8: Phospholipases A2 - p. 101 11. Section C: Zinc enzymes - p. 136 12. Chapter 3.1: Carbonic anhydrases - p. 139 13. Chapter 3.2: Metallo-β-lactamases - p. 157 14. Chapter 3.3: Bacterial zinc proteases - p. 185 15. Chapter 3.4: Matrix metalloproteases - p. 197 16. Chapter 3.5: A disintegrin and metalloproteinases (ADAMs) and tumor necrosis factor-alpha-converting enzyme (TACE) - p. 207 17. Chapter 3.6: Angiotensin-converting enzyme - p. 239 18. Chapter 3.7: Histidinol dehydrogenase - p. 255 19. Chapter 3.8: Histone deacetylases and other epigenetic targets - p. 265 20. Chapter 3.9: CD73 (5′-Ectonucleotidase) - p. 283 21. Chapter 3.10: Glyoxalase II - p. 293 22. Chapter 3.11: Glutamate carboxypeptidase II - p. 305 23. Chapter 3.12: Neutral endopeptidase (neprilysin) - p. 321 24. Section D: Other metalloenzymes - p. 330 25. Chapter 4.1: The role of arginase in human health and disease - p. 333 26. Chapter 4.2: Methionine aminopeptidases - p. 343 27. Chapter 4.3: 1-Deoxy-d-xylulose 5-phosphate reductoisomerase, the first committed enzyme in the MEP terpenoid biosynthetic pathway—Its chemical mechanism and inhibition - p. 375 28. Section E: Nickel enzymes - p. 390 29. Chapter 5.1: Urease - p. 393 30. Chapter 5.2: Methyl-coenzyme M reductase - p. 411 31. Section F: Iron enzymes (heme-containing) - p. 427 32. Chapter 6.1: Cyclooxygenase - p. 431 33. Chapter 6.2: Cytochrome P450 (inhibitors for the metabolism of drugs) - p. 449 34. Chapter 6.3: Aromatase - p. 459 35. Section G: Iron enzymes, non-heme containing - p. 464 36. Chapter 7.1: Nonheme mono- and dioxygenases - p. 467 37. Chapter 7.2: Indoleamine 2,3-dioxygenase - p. 485 38. Section H: Copper enzymes - p. 519 39. Chapter 8.1: Superoxide dismutases inhibitors - p. 523 40. Chapter 8.2: Tyrosinase enzyme and its inhibitors: An update of the literature - p. 533 41. Section I: Cadmium enzymes CAs - p. 546 42. Chapter 9: CDCA1, a versatile member of the ζ-class of carbonic anhydrase family - p. 549 43. Section J: Molybdenum enzymes - p. 554 44. Chapter 10: Molybdenum enzymes - p. 557 45. Section K: Tungsten-containing enzymes - p. 580 46. Chapter 11: Tungsten-containing enzymes - p. 583 47. Index - p. 603
