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Die Funktion des Arginins in den Enzymen

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Abstract

The average arginine content of proteins is 3.9%. Its frequency among the 20 amino acids of the proteins (13th position) is far lower than would be anticipated from the fact that 6 of the 61 codons for amino acids in the genetic code are arginine codons. Possible explanations for the relatively low frequency of arginine in proteins are discussed. The chemical and physicochemical properties of arginine, which are determined by the guanido group, and the methods for chemical modification of arginine residues in proteins are described. The most important function of arginine residues in enzymes seems to be the recognition, binding, and orientation of anionic substrates and cofactors. This function is illustrated by numerous examples.

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References

  1. King, J.L., Jukes, T.H.: Science 164, 788 (1969)

    Article  CAS  PubMed  Google Scholar 

  2. Jukes, T.H.: Biochem. Biophys. Res. Commun. 53, 709 (1973)

    Article  CAS  PubMed  Google Scholar 

  3. Dayhoff, M.O.: Atlas of Protein Structure. Washington, D.C.: Nat. Biomed. Res. Found. Georgetown Univ. Medical Center 1972

    Google Scholar 

  4. Wallis, M.: Biochem. Biophys. Res. Commun. 56, 711 (1974)

    Article  CAS  PubMed  Google Scholar 

  5. Ames, B.N., Hartman, P.E.: Cold Spring Harbour Symp. Quant. Biol. 28, 349 (1963)

    Article  CAS  Google Scholar 

  6. Boyer, S.H., in: Modern Trends in Human Genetics, Vol. 1, p. 1 (ed. A.E. Emery). London: Butterworth 1970

    Google Scholar 

  7. Anderson, W.F.: Proc. Nat. Acad. Sci. USA 62, 566 (1969)

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  8. Pauling, L.: Die Natur der chemischen Bindung, S. 272. Weinheim: Verlag Chemie 1973

    Google Scholar 

  9. Ingraham, L.L.: Biochemical Mechanisms, p. 29. New York: Wiley 1962

    Google Scholar 

  10. Erlanger, B.F.: Proc. Nat. Acad. Sci. USA 46, 1430 (1960)

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  11. Harden, A., Norris, D.: J. Physiol. 42, 332 (1911)

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  12. Means, G.E., Feeney, R.E.: Chemical Modification of Proteins, p. 194. San Francisco: Holden-Day 1971

    Google Scholar 

  13. Toi, K., et al.: J. Biol. Chem. 242, 1036 (1967)

    CAS  PubMed  Google Scholar 

  14. Liu, W.H., et al.: Biochemistry 7, 2886 (1968)

    Article  CAS  PubMed  Google Scholar 

  15. Dieth, Th., Tschesche, H.: Hoppe Seyler's Z. physiol. Chem. 357, 657 (1976)

    Article  Google Scholar 

  16. Takahashi, K.: J. Biol. Chem. 243, 6171 (1968)

    CAS  PubMed  Google Scholar 

  17. Takahashi, K.: J. Biochem. (Tokyo) 81, 403 (1977)

    CAS  Google Scholar 

  18. Cornforth, J.W., Huang, H.T.: J. Chem. Soc. 1948, 731

  19. Riordan, J.F.: Biochemistry 12, 3915 (1973)

    Article  CAS  PubMed  Google Scholar 

  20. Sakaguchi, S.: J. Biochem. (Tokyo) 37, 231 (1950)

    CAS  Google Scholar 

  21. Nees, St., Schmidt, W., Schneider, Fr.: Hoppe Seyler's Z. physiol. Chem. 352, 355 (1971)

    Article  CAS  PubMed  Google Scholar 

  22. Riordan, J.F., McElvany, K.D., Borders, Jr., C.L.: Science 195, 884 (1977)

    Article  CAS  PubMed  Google Scholar 

  23. Borders, Jr., C.L., Riordan, J.F.: Biochemistry 14, 4699 (1975)

    Article  CAS  PubMed  Google Scholar 

  24. Cotton, F.A., et al.: Biochim. Biophys. Acta 481, 1 (1972)

    Article  Google Scholar 

  25. Markland, F.S., et al.: J. Biol. Chem. 250, 1301 (1975)

    CAS  PubMed  Google Scholar 

  26. Burton, P.M., Waley, S.G.: Biochem. J. 104, 3P (1967)

  27. Banner, D.W., et al.: Nature 255, 609 (1975)

    Article  CAS  PubMed  Google Scholar 

  28. Marcus, Fr.: Biochemistry 14, 3916 (1977)

    Article  Google Scholar 

  29. Kantrowitz, E.R., Lipscomb, W.N.: J. Biol. Chem. 252, 2873 (1977)

    CAS  PubMed  Google Scholar 

  30. Borders, C.L., Riordan, J.F., Auld, D.S.: Biochem. Biophys. Res. Commun. 66, 490 (1975)

    Article  CAS  PubMed  Google Scholar 

  31. Armstrong, V.W., Sternbach, H., Eckstein, F.: FEBS Lett. 70, 48 (1976)

    Article  CAS  PubMed  Google Scholar 

  32. Riordan, J.F.: Biochemistry 12, 3915 (1973)

    Article  CAS  PubMed  Google Scholar 

  33. Weber, M., Moldovan, M., Sokolovsky, M.: Eur. J. Biochem. 53, 207 (1975)

    Article  Google Scholar 

  34. Gawron, O., Jones, L.: Biochim. Biophys. Acta 484, 453 (1977)

    Article  CAS  PubMed  Google Scholar 

  35. Chatagner, F., Pierre, Y.: FEBS Lett. 81, 335 (1977)

    Article  CAS  PubMed  Google Scholar 

  36. Crifó, C., et al.: Mol. Cell. Biochem. 17, 7 (1977)

    Article  PubMed  Google Scholar 

  37. Arnone, A., et al.: J. Biol. Chem. 246, 2302 (1971)

    CAS  PubMed  Google Scholar 

  38. Adams, M.J., et al.: Proc. Nat. Acad. Sci. USA 70, 1968 (1973)

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  39. Eklund, H., et al.: FEBS Lett. 44, 200 (1974)

    Article  CAS  PubMed  Google Scholar 

  40. Yang, C.C., Chang, C.C., Liou, J.F.: Biochim. Biophys. Acta 365, 1 (1974)

    Article  CAS  PubMed  Google Scholar 

  41. Dietl, Th., Tschesche, H.: Hoppe Seyler's Z. physiol. Chem. 357, 657 (1976)

    Article  CAS  PubMed  Google Scholar 

  42. Hazum, E., et al.: FEBS Lett. 76, 187 (1977)

    Article  CAS  PubMed  Google Scholar 

  43. Weitzel, G., Bauer, F.U., Rehe, A.: Hoppe Seyler's Z. physiol. Chem. 358, 1573 (1977)

    Article  CAS  PubMed  Google Scholar 

  44. Grossberg, A.L., et al.: J. Immunol. 113, 1807 (1974)

    CAS  PubMed  Google Scholar 

  45. Grossberg, A.L.: Int. Convocation Immun. 3rd 1972 (pub. 1973), p. 476

  46. Canella, M., Sodini, G.: Eur. J. Biochem. 59, 119 (1975)

    Article  CAS  PubMed  Google Scholar 

  47. Jornvall, H., et al.: Biochem. Biophys. Res. Commun. 77, 73 (1977)

    Article  CAS  PubMed  Google Scholar 

  48. Ehrlich, R.S., Colmann, R.F.: Biochemistry 16, 3378 (1977)

    Article  CAS  PubMed  Google Scholar 

  49. Berghäuser, J.: Hoppe Seyler's Z. physiol. Chem. 358, 1565 (1977)

    Article  PubMed  Google Scholar 

  50. Berghäuser, J.: Biochim. Biophys. Acta 397, 370 (1975)

    Article  PubMed  Google Scholar 

  51. Daemen, F.J., Takahashi, K.: J. Biochem. 75, 455 (1974)

    Google Scholar 

  52. Cooperman, B.S., Chin, N.Y.: Biochemistry 12, 1676 (1973)

    Article  CAS  PubMed  Google Scholar 

  53. Mahlen, A.: FEBS Lett. 51, 294 (1975)

    Article  CAS  PubMed  Google Scholar 

  54. Powers, S.G., Riordan, J.F.: Proc. Nat. Acad. Sci. USA 72, 2616 (1975)

    Article  CAS  PubMed  PubMed Central  Google Scholar 

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Professor Adolf Butenandt zum 75. Geburtstag gewidmet

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Schneider, F. Die Funktion des Arginins in den Enzymen. Naturwissenschaften 65, 376–381 (1978). https://doi.org/10.1007/BF00439701

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  • DOI: https://doi.org/10.1007/BF00439701

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