Skip to main content
SpringerLink
Log in

Aktivierung, Aktivität und Inhibierung des Rindertrypsins

  • Published:
Naturwissenschaften Aims and scope Submit manuscript

Abstract

Trypsin is a prototype of a large group of enzymes belonging to serine proteinases. The X-ray crystal-structure analyses of its proenzyme trypsinogen, of the active trypsin and of their complexes formed with the pancreatic trypsin inhibitor (PTI) have considerably enhanced our understanding of the mechanisms of activitation, action and inhibition. The trypsinogen is an incompletely folded molecule. Its substrate-binding site becomes only completely fixed upon the enzymatic cleavage of an N-terminal peptide. The contact regions of trypsin and PTI are almost complementary. The complex formed is a (stable) intermediate in the normal tryptic substrate-cleavage reaction.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Neurath, H., Walsh, K.E.: Proc. Nat. Acad. Sci. USA73, 3825 (1976)

    Google Scholar 

  2. Devillers-Triery, A., et al.: ibid.72, 5016 (1975)

    Google Scholar 

  3. Maroux, S., Baratti, J., Desnuelle, P.: J. Biol. Chem.246, 5031 (1971)

    Google Scholar 

  4. Magnusson, S., et al.: Miami Winter Symp.11, 203 (1976)

    Google Scholar 

  5. Huber, R., Bode, W.: Acc. Chem. Res.11, 114 (1978)

    Google Scholar 

  6. Bode, W., Schwager, P.: J. Mol. Biol.98, 693 (1975)

    Google Scholar 

  7. Bode, W., Huber, R.: FEBS Lett.90, 265 (1978)

    Google Scholar 

  8. Bode, W., Fehlhammer, H., Huber, R.: J. Mol. Biol.106, 325 (1976)

    Google Scholar 

  9. Fehlhammer, H., Bode, W., Huber, R.: ibid.111, 415 (1977)

    Google Scholar 

  10. Huber, R., et al.: Bayer Symp. V on Proteinase Inhibitors, p. 497 (Fritz, H., et al., eds.). Berlin-Heidelberg-New York: Springer 1974

    Google Scholar 

  11. Huber, R., et al.: J. Mol. Biol.89, 73 (1974)

    Google Scholar 

  12. Huber, R., et al.: Biophys. Struct. Mech.1, 189 (1975)

    Google Scholar 

  13. Bode, W., Schwager, R., Huber, R.: J. Mol. Biol.118, 99 (1978)

    Google Scholar 

  14. Bode, W., Schwager, P., Huber, R.: Miami Winter Symp.11, 43 (1976)

    Google Scholar 

  15. De Haen, C., Neurath, H., Teller, D.C.: J. Mol. Biol.92, 225 (1975)

    Google Scholar 

  16. Delbaere, L.T.J., et al.: Nature257, 758 (1975)

    Google Scholar 

  17. Birktoft, J.J., Blow, D.M.: J. Mol. Biol.68, 187 (1972)

    Google Scholar 

  18. Bode, W., Schwager, P.: FEBS Lett.56, 139 (1975)

    Google Scholar 

  19. Sipos, T., Merkel, J.R.: Biochemistry9, 2766 (1970)

    Google Scholar 

  20. Schroeder, D.D., Shaw, E.: J. Biol. Chem.243, 2943 (1968)

    Google Scholar 

  21. Keil, B.: Enzymes3, 249 (1971)

    Google Scholar 

  22. Matthews, B.W., et al.: Nature214, 652 (1967)

    Google Scholar 

  23. Blow, D.M., Birktoft, J.J., Hartley, B.S.: ibid.221, 337 (1969)

    Google Scholar 

  24. Deisenhofer, J., Steigemann, W.: Acta Crystallogr., Sect.B31, 238 (1975)

    Google Scholar 

  25. Tschesche, H.: Angew. Chem.86, 21 (1974)

    Google Scholar 

  26. Vincent, J.-P., Lazdunski, M.: Biochemistry11, 2967 (1972)

    Google Scholar 

  27. Finkenstadt, W.R., et al.: Bayer Symp. V on Proteinase Inhibitors, p. 389 (1974)

  28. Quast, V., et al.: Biochemistry17, 1675 (1978)

    Google Scholar 

  29. Janin, J., Chothia, C.: J. Mol. Biol.100, 197 (1976)

    Google Scholar 

  30. Krieger, M., Kay, L.M., Stroud, R.M.: ibid.83, 209 (1974)

    Google Scholar 

  31. Bender, M.L., Killheffer, J.V.: CRC Crit. Rev. Biochem.1, 149 (1973)

    Google Scholar 

  32. Blow, D.M.: Acc. Chem. Res.9, 145 (1976)

    Google Scholar 

  33. Kraut, J.: Ann. Rev. Biochem.46, 331 (1977)

    Google Scholar 

  34. Bender, M.L., Kezdy, F.J.: J. Am. Chem. Soc.86, 3704 (1964)

    Google Scholar 

  35. Fink, A.: Biochemistry15, 1580 (1976)

    Google Scholar 

  36. Alber, T., Petsko, G.A., Tsernoglou, D.: Nature263, 397 (1976)

    Google Scholar 

  37. Henderson, R.: J. Mol. Biol.54, 341 (1970)

    Google Scholar 

  38. Sweet, R.M., et al.: Biochemistry13, 4212 (1974)

    Google Scholar 

  39. Hunkapiller, M., et al.: J. Biol. Chem.248, 8306 (1973)

    Google Scholar 

  40. Koeppe, R.E., Stroud, R.M.: Biochemistry15, 3450 (1976)

    Google Scholar 

  41. Markley, J.L., Porubcan, M.A.: J. Mol. Biol.102, 487 (1976)

    Google Scholar 

  42. Fersht, A.R., Sperling, J.: ibid.74, 137 (1973)

    Google Scholar 

  43. Neurath, H., Davie, E.: J. Biol. Chem.212, 515 (1955); Desnuelle, P., Fabre, C.: Biochim. Biophys. Acta18, 49 (1955)

    Google Scholar 

  44. Tschesche, H., Kupfer, S.: Hoppe-Seyler's Z. Physiol. Chem.358, 316 (1977)

    Google Scholar 

  45. Bode, W., Huber, R.: FEBS Lett.68, 231 (1976)

    Google Scholar 

  46. Bode, W.: J. Mol. Biol.127, 357 (1979)

    Google Scholar 

  47. Vincent, J.-P., Lazdunski, M.: FEBS Lett.63, 240 (1976)

    Google Scholar 

  48. Neurath, M., in: Proteases and Biological Control, p. 51. New York: Cold Spring Harbor Laboratory Press 1975

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Max-Planck-Institut für Biochemie, D-8033, Martinsried bei München

    Wolfram Bode

Authors
  1. Wolfram Bode
    View author publications

    You can also search for this author in PubMed Google Scholar

Additional information

Ich danke dem SFB 51 und der Deutschen Forschungsgemeinschaft für großzügige finanzielle Unterstützung und Prof. R. Huber und meinen Kollegen für die Überlassung von Ergebnissen und Abbildungen, für ihre Mithilfe und für viele stimulierende Diskussionen.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Bode, W. Aktivierung, Aktivität und Inhibierung des Rindertrypsins. Naturwissenschaften 66, 251–258 (1979). https://doi.org/10.1007/BF00571605

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00571605

Search

Navigation