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Die Funktion des Arginins in den Enzymen

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. 1.

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

  2. 2.

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

  3. 3.

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

  4. 4.

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

  5. 5.

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

  6. 6.

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

  7. 7.

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

  8. 8.

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

  9. 9.

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

  10. 10.

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

  11. 11.

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

  12. 12.

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

  13. 13.

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

  14. 14.

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

  15. 15.

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

  16. 16.

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

  17. 17.

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

  18. 18.

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

  19. 19.

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

  20. 20.

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

  21. 21.

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

  22. 22.

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

  23. 23.

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

  24. 24.

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

  25. 25.

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

  26. 26.

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

  27. 27.

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

  28. 28.

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

  29. 29.

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

  30. 30.

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

  31. 31.

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

  32. 32.

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

  33. 33.

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

  34. 34.

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

  35. 35.

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

  36. 36.

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

  37. 37.

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

  38. 38.

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

  39. 39.

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

  40. 40.

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

  41. 41.

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

  42. 42.

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

  43. 43.

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

  44. 44.

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

  45. 45.

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

  46. 46.

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

  47. 47.

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

  48. 48.

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

  49. 49.

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

  50. 50.

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

  51. 51.

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

  52. 52.

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

  53. 53.

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

  54. 54.

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

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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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