Enzyme pp 399-413 | Cite as

Anhydrid-hydrolysierende Enzyme und Phosphoamidase

  • Otto Hoffmann-Ostenhof
Part of the Handbuch der Physiologisch- und Pathologisch-Chemischen Analyse book series (HOPPE-SEYLER, volume Teil C)

Zusammenfassung

In diesem Kapitel sollen Enzyme behandelt werden, welche Derivate der Phosphorsäure, die keine Phosphorsäure-Ester sind, hydrolytisch spalten. Unter den Substraten dieser Enzyme sind die einfachen kondensierten Phosphate (Pyrophosphat, Polyphosphate, Tri- und Tetrametaphosphat) und deren Substitutionsprodukte (Nucleosiddi- und triphosphate), die Acylphosphate und schließlich die Phosphoamide vom Typus des Kreatinphosphats und Argininphosphats zu nennen.

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Referenzen

  1. 1.
    Kunitz, M.: J. gen. Physiol. 35, 432 (1952).Google Scholar
  2. 2.
    Seal, U. S., and F. Binkley: J. biol. Ch. 228, 193 (1957).Google Scholar
  3. 3.
    Robbins, E. A., M. P. Stulberg and P. D. Boyer: Arch. Biochem. 54, 215 (1955).PubMedCrossRefGoogle Scholar
  4. 4.
    Bloch-Frankenthal, L.: Biochem. J. 57, 87 (1954).PubMedCentralPubMedGoogle Scholar
  5. 5.
    Rafter, G. W.: J. biol. Ch. 235, 2475 (1960).Google Scholar
  6. 1.
    Bamann, E., u. H. Gall: B. Z. 202, 466 (1937).Google Scholar
  7. 2.
    Ebel, J.-P., et L. Mehr: Bull. Soc. Chim. biol. 39, 1535 (1957).PubMedGoogle Scholar
  8. 3.
    Norberg, B.: Acta chem. scand. 4, 601 (1957).CrossRefGoogle Scholar
  9. 4.
    Elliott, W. H.: Biochem. J. 65, 315 (1957).PubMedCentralPubMedGoogle Scholar
  10. 5.
    Kornberg, A.: Adv. Enzymol. 18, 191 (1957).Google Scholar
  11. 6.
    Hoffmann-Ostenhof, O., and L. Šlechta: Proc. int. Symp. Enzyme Chem., Tokyo and Kyoto 1957, S. 180.Google Scholar
  12. 7.
    Swanson, M. A.: J. biol. Ch. 194, 685 (1950).Google Scholar
  13. 8.
    Kunitz, M.: J. gen. Physiol. 35, 432 (1952).Google Scholar
  14. 9.
    Heppel, L. A., and R. J. Hilmoe: J. biol. Ch. 192, 87 (1951).Google Scholar
  15. 10.
    Seal, U. S., and F. Binkley: J. biol. Ch. 228, 193 (1957).Google Scholar
  16. 1.
    Seal, U. S., and F. Binkley: J. biol. Ch. 228, 193 (1957).Google Scholar
  17. 1.
    Heppel, L. A.; in: Colowick-Kaplan, Meth. Enzymol. Bd. II, S. 570.Google Scholar
  18. 2.
    Fiske, C. H., and Y. Subbarow: J. biol. Ch. 66, 375 (1925).Google Scholar
  19. 3.
    Rafter, G. W.: J. biol. Ch. 235, 2475 (1960).Google Scholar
  20. 1.
    Kunitz, M., and P. W. Robbins; in: Boyer-Lardy-Myrbäck, Enzymes Bd. V, S. 169.Google Scholar
  21. 2.
    Lowry, O. H.; in: Waelsch, H.: Biochemistry of the Developing Nervous System. S. 355, New York 1955.Google Scholar
  22. 3.
    Seal, U. S., and F. Binkley: J. biol. Ch. 228, 193 (1957).Google Scholar
  23. 4.
    Rafter, G. W.: J. biol. Ch. 230, 643 (1958).Google Scholar
  24. 1.
    Kafter, G. W.: J. biol. Ch. 230, 643 (1958).Google Scholar
  25. 2.
    Robbins, E. A., M. P. Stulberg and P. D. Boyer: Arch. Biochem. 54, 215 (1955).PubMedCrossRefGoogle Scholar
  26. 3.
    Bloch-Frankenthal, L.: Biochem. J. 57, 87 (1954).PubMedCentralPubMedGoogle Scholar
  27. 4.
    Bauer, E.: H. 238, 213 (1937).Google Scholar
  28. 5.
    Segal, H. L., J. F. Kachmar and P. D. Boyer: Enzymologia 15, 187 (1952).PubMedGoogle Scholar
  29. 6.
    Naganna, B., and V. K. N. Menon: J. biol. Ch. 174, 501 (1948).Google Scholar
  30. 7.
    Gordon, J. J.: Biochem. J. 46, 96 (1950).PubMedCentralPubMedGoogle Scholar
  31. 1.
    Bloch-Frankenthal, L.: Biochem. J. 57, 87 (1954).PubMedCentralPubMedGoogle Scholar
  32. 2.
    Mattenheimer, H.; in: Kondensierte Phosphate in Lebensmitteln. S. 45. Berlin, Göttingen, Heidelberg 1958.CrossRefGoogle Scholar
  33. 1.
    Frankenthal, L., and C. Neuberg: Exp. Med. Surg. 1, 386 (1943).Google Scholar
  34. 2.
    Fodor, P. J., and A. Lehrman: Arch. Biochem. 69, 277 (1957).PubMedCrossRefGoogle Scholar
  35. 3.
    Berg, G. G.: J. cellul. comp. Physiol. 45, 435 (1955).CrossRefGoogle Scholar
  36. 4.
    Mattenheimer, H.: H. 303, 107, 115, 127 (1956).Google Scholar
  37. 5.
    Laki, K.: Stud. Inst. med. Chem. Szeged 3, 16 (1943).Google Scholar
  38. 1.
    Banga, I., and G. Josepovits; in: Szent-Györgyi, A.: Chemistry of Muscular Contraction. S. 51. New York 1947.Google Scholar
  39. 2.
    Strominger, J. L., L. A. Heppel and E. S. Maxwell: Arch. Biochem. 52, 488 (1954).CrossRefGoogle Scholar
  40. 3.
    Plaut, G. W. E.: J. biol. Ch. 217, 235 (1955).Google Scholar
  41. 4.
    Gregory, J. D.: Fed. Proc. 14, 221 (1955).Google Scholar
  42. 5.
    Gibson, D. M., P. Ayengar and D. K. Sanadi: Biochim. biophys. Acta 16, 536 (1955).PubMedCrossRefGoogle Scholar
  43. 6.
    Horecker, B. L., J. Hurwitz and L. A. Heppel: Am. Soc. 79, 701 (1957).CrossRefGoogle Scholar
  44. 7.
    Heppel, L. A., J. L. Strominger and E. S. Maxwell: Biochim. biophys. Acta 32, 422 (1959).PubMedCrossRefGoogle Scholar
  45. 8.
    Horecker, B. L.: J. biol. Ch. 183, 593 (1950).Google Scholar
  46. 1.
    Heppel, L. A., J. L. Strominger and E. S. Maxwell: Biochim. biophys. Acta 32, 422 (1959).PubMedCrossRefGoogle Scholar
  47. 1.
    Fiske, C. H., and Y. Subbarow: J. biol. Ch. 66, 375 (1925).Google Scholar
  48. 2.
    Gregory, J. D.: Fed. Proc. 14, 221 (1955).Google Scholar
  49. 3.
    Heppel, L. A., J. L. Strominger and E. S. Maxwell: Biochim. biophys. Acta 32, 422 (1959)PubMedCrossRefGoogle Scholar
  50. 4.
    Plaut, G. W. E.: J. biol. Ch. 217, 235 (1955).Google Scholar
  51. 5.
    Chain, E.: Biochem. J. 33, 407 (1939).PubMedCentralPubMedGoogle Scholar
  52. 6.
    Wang, T. P., and N. O. Kaplan: J. biol. Ch. 206, 311 (1954).Google Scholar
  53. 7.
    Butler, G. C.; in: Colowick-Kaplan, Meth. Enzymol. Bd. II, S. 564.Google Scholar
  54. 8.
    Kornberg, A., and W. E. Pricer jr.: J. biol. Ch. 182, 763 (1950).Google Scholar
  55. 9.
    Swarz, M. N., N. O. Kaplan and M. E. Fresh: Science, N. Y. 123, 50 (1956).CrossRefGoogle Scholar
  56. 10.
    Kornberg, A.; in: Colowick-Kaplan, Meth. Enzymol. Bd. II, S. 655.Google Scholar
  57. 1.
    Lipmann, F.: Adv. Enzymol. 6, 231 (1946).Google Scholar
  58. 2.
    Lehninger, A. L.: J. biol. Ch. 162, 340 (1946).Google Scholar
  59. 3.
    Harary, I.: Biochim. biophys. Acta 26, 434 (1957).PubMedCrossRefGoogle Scholar
  60. 4.
    Grisolia, S., J. Caravaca and B. K. Joyce: Biochim. biophys. Acta 29, 432 (1958).PubMedCrossRefGoogle Scholar
  61. 5.
    Koshland jr., D. E.; in: Colowick-Kaplan, Meth. Enzymol. Bd. II, S. 555.Google Scholar
  62. 1.
    Koshland jr., D. E.; in: Colowick- Kaplan, Meth. Enzymol. Bd. II, S. 555.Google Scholar
  63. 2.
    Grisolia, S., J. Caravaca and B. K. Joyce: Biochim. biophys. Acta 29, 432 (1958).PubMedCrossRefGoogle Scholar
  64. 3.
    Llpmann, F., and L. C. Tuttle: J. biol. Ch. 159, 21 (1945).Google Scholar
  65. 4.
    Lehninger, A. L.: J. biol. Ch. 162, 340 (1946).Google Scholar
  66. 5.
    Harary, I.: Biochim. biophys. Acta 25, 193 (1957).PubMedCrossRefGoogle Scholar
  67. 6.
    Harary, I.: Biochim. biophys. Acta 29, 432 (1958).CrossRefGoogle Scholar
  68. 7.
    Bentley, K.: Am. Soc. 71, 2765 (1946).CrossRefGoogle Scholar
  69. 1.
    Koshland, D. E.; in: McElroy-Glass, Phosphorus Metabolism, Bd. I, S. 536.Google Scholar
  70. 2.
    Koshland jr., D. E.: Am. Soc. 74, 2286 (1952).Google Scholar
  71. 3.
    Ichihara, M.: J. Biochem., Tokyo 18, 87 (1933).Google Scholar
  72. 4.
    Waldschmidt-Leitz, E.: B. Z. 258, 360 (1933).Google Scholar
  73. 5.
    Winnick, T., and E. M. Scott: Arch. Biochem. 12, 201, 209 (1947).PubMedGoogle Scholar
  74. 6.
    Meyerhof, O., and H. Green: J. biol. Ch. 178, 655 (1949); 183, 377 (1950).Google Scholar
  75. 7.
    Perlmann, G. E.; in: McElroy-Glass, Phosphorus Metabolism, Bd. II, S. 167.Google Scholar
  76. 8.
    Morton, E. K.: Nature 172, 65 (1953).PubMedCrossRefGoogle Scholar
  77. 9.
    Møller, K. M.: Biochim. biophys. Acta 16, 162 (1955).PubMedCrossRefGoogle Scholar
  78. 10.
    Holter, H., and Si-Oh-Li: Acta chem. scand. 4, 1321 (1950).CrossRefGoogle Scholar
  79. 11.
    Güntelberg, A. V., and M. Ottesen: C. R. Lab. C.rlsberg, Sér. chim. 29, 36 (1954).Google Scholar
  80. 12.
    Singer, M. F., and J. S. Fruton: J. biol. Ch. 229, 111 (1957).Google Scholar
  81. 13.
    Hofman, T.: Biochem. J. 69, 139 (1958).PubMedCentralPubMedGoogle Scholar
  82. 14.
    Glomset, J. A.: Biochim. biophys. Acta 32, 349 (1959).PubMedCrossRefGoogle Scholar
  83. 15.
    Conway, E. J.: Biochem. J. 29, 2755 (1935).PubMedCentralPubMedGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1967

Authors and Affiliations

  • Otto Hoffmann-Ostenhof
    • 1
  1. 1.Organisch-chemisches Institut der UniversitätWienÖsterreich

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