Skip to main content
SpringerLink
Log in

Some newly characterized collagenases from procaryotes and lower eucaryotes

  • Review Articles
  • Published:
Molecular and Cellular Biochemistry Aims and scope Submit manuscript

Summary

Chemical and enzymatic properties of four collagenases newly isolated from anaerobic Clostridium histolyticum, aerobic Achromobacter iophagus, and from two lower eucaryotes, the fungus Entomophthora coronata and the insect Hypoderma lineatum are reviewed.

The problems of their biosynthesis and precursors, namely the effect of induction of collagenase and neutral proteinase in Achromobacter by their macromolecular substrates are discussed.

The two bacterial collagenases are Zn-metallo-enzymes; the highly purified Clostridium collagenase contains cyst(e)ine, serine phosphate and tryptophan additionally to amino acids reported previously. Achromobacter collagenase has the highest specific activity of all collagenases; it yields by autolysis enzymatically active degraded forms. The active dimer is composed of two identical subunits of molecular weight 35,000. Similarities between Achromobacter collagenase, thermolysin and Bacillus subtilis neutral proteinase in molecular weight, amino acid composition, and amino acids important for the active sites are discussed.

The two collagenases from low eucaryotes are serine proteinases; Hypoderma collagenase is homologous to the trypsin family in the amino terminal sequence.

The initial cleavage of native collagen by highly purified bacterial collagenases occurs in the central helical part of the a chains and not progressively from the amino terminal end. One of the two initial cleavages produced by Achromobacter collagenase is situated in the region cleaved specifically by vertebrate collagenases, but with different bond specificity. The same is true for the insect collagenase. Entomophthora collagenase is a proteinase of broad specificity which also cleaves collagen in its helical parts. All four collagenases also degrade other proteins according to their bond specificity.

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. Weinberg, M. and Séguin, P., 1916. Compt. Rend. Acad. Sci. (Paris) 163, 449–451.

    Google Scholar 

  2. Weinberg, M. and Randin, A., 1931. Compt. Rend. Soc. Biol. (Paris) 107, 27–28.

    Google Scholar 

  3. Keil, B., Gilles, A.-M., Lecroisey, A., Hurion, N. and Tong, N.-T., 1975, FEBS Letters 56, 292–296.

    Google Scholar 

  4. Lecroisey, A., Keil-Dlouha, V., Woods, D. R., Perrin, D. and Keil, B., 1975, FEBS Letters 59, 167–172.

    Google Scholar 

  5. Svensson, B., Siffert, O. and Keil, B., 1975. Eur. J. Biochem. 60, 423–425.

    Google Scholar 

  6. Keil-Dlouha, V., 1976. Biochim. Biophys. Acta 429, 239–251.

    Google Scholar 

  7. Gilles, A.-M. and Keil, B., 1976. FEBS Letters 65, 369–372.

    Google Scholar 

  8. Keil-Dlouha, V., Misrahi, R., and Keil, B. 1976. J. Mol. Biol. 107, 293–305.

    Google Scholar 

  9. Hurion, N., Fromentin, H. and Keil, B., 1977. Comp. Biochem. Physiol. 568, 259–264.

    Google Scholar 

  10. Emöd, I. and Keil, B., 1977. FEBS Letters 77, 51–56.

    Google Scholar 

  11. Keil-Dlouha, V. and Keil, B., 1978. Biochim. Biophys. Acta 522, 218–228.

    Google Scholar 

  12. Keil-Dlouha, V. and Keil, B., 1975. Proc. 10th FEBS-Meeting (Paris) Abstr. No 768.

  13. Lecroisey, A. and Keil, B., 1976. Proc. 11th FEBS Meeting (Cophenhagen) Abstr. No A6-1, 860.

  14. Trocheris, I., Herry, P., Keil-Dlouha, V. and Keil, B. 1976. Proc. 11th FEBS Meeting (Copenhagen) Abstr. No A6-1, 862.

  15. Fromentin, H., Hurion, N. and Mariat, F., 1978. Ann. Microbiol. Inst. Pasteur 129A, 425–431.

    Google Scholar 

  16. Lecroisey, A. and Keil, B., 1978. Biochem. J., in press.

  17. Hurion, N., Fromentin, H. and Keil, B., 1978. Arch. Biochem. Biophys., in press.

  18. Herry, P. and Keil-Dlouha, V., 1978. FEBS Letters, in press.

  19. Seifter, S. and Harper, E., 1970. Methods in Enzymol. 19, 613–635.

    Google Scholar 

  20. Harper, E. and Gross, J., 1970. Biochim. Biophys. Acta 198, 286–292.

    Google Scholar 

  21. Seifter, S. and Harper, E., 1971. The Enzymes (Boyer, P. D., ed.) Vol. II, pp. 649–697, Acad. Press New York & London.

  22. Woods, D. R., Welton, R. L. and Thomson, J. A., 1972. J. Applied Bact. 35, 123–128.

    Google Scholar 

  23. Welton, R. L. and Woods, D. R., 1973. J. Gen. Microbiol. 75, 191–196.

    Google Scholar 

  24. Welton, R. L. and Woods, D. R., 1975. Biochim. Biophys. Acta 384, 228–234.

    Google Scholar 

  25. Cooper, D. R., Galloway, A. C. and Woods, D. R., 1972. J. Soc. Leather Trades Chem. 56, 127–138.

    Google Scholar 

  26. Pore, R. S., Goodman, N. L. and Larsh, H. W., 1970. Am. Rev. Resp. Disease 101, 627–628.

    Google Scholar 

  27. Fromentin, H., 1975. Bull. Soc. Mycol. Med. 4, 215–220.

    Google Scholar 

  28. Lienert, E. and Thorsell, W., 1955. Expl. Parasit. 4, 117–122.

    Google Scholar 

  29. Boulard, C., 1969. Ann. Soc. Ent. France (N.S.) 5, 381–387.

    Google Scholar 

  30. Boulard, C., 1970. Compt. Rend. Acad. Sci. (Paris) 270, 1349–1351.

    Google Scholar 

  31. Boulard, C. and Weintraub, J., 1973. Int. J. Parasitol. 3, 379–386.

    Google Scholar 

  32. Boulard, C. and Garronne, R., 1978. Comp. Biochem. Physiol. 59B, 251–255.

    Google Scholar 

  33. Castaneda-Agullo, M., 1975. J. Gen. Physiol. 39, 369–375.

    Google Scholar 

  34. Liu, T.-Y. and Elliott, S. D., 1965. J. Biol. Chem. 240, 1138–1142.

    Google Scholar 

  35. Harper, E., Bloch, K. J. and Gross, J., 1971. Biochemistry 10, 3035–3041.

    Google Scholar 

  36. Kruze, D. and Wojtecka, E., 1972. Biochim. Biophys. Acta 285, 436–446.

    Google Scholar 

  37. Vaes, G., 1972. Biochem. J. 126, 275–289.

    Google Scholar 

  38. Eisen, A. Z., Henderson, K. O., Jeffrey, J. J., and Bradshaw, R. A., 1973. Biochemistry 12, 1814–1822.

    Google Scholar 

  39. Phillips, J. and Dresden, M. H., 1973. Biochem. J. 133. 329–334.

    Google Scholar 

  40. Wünsch, E. and Heidrich, H. G., 1963. Z. Physiol. Chem. 333, 149–151.

    Google Scholar 

  41. Grassman, W. and Nordwig, A., 1960. Z. Physiol. Chem. 322, 267–272.

    Google Scholar 

  42. Yagisawa, S., Morita, F., Nagai, Y., Noda, H. and Ogura, Y., 1965. J. Biochem. (Tokyo) 58, 407–416.

    Google Scholar 

  43. Seifter, S., Gallop, P. M., Klein, L. and Meilman, E., 1959. J. Biol. Chem. 234, 285–293.

    Google Scholar 

  44. Mandl, I., Keller, S. and Manahan, J., 1964. Biochemistry 3, 1737–1741.

    Google Scholar 

  45. Yoshida, E., and Noda, H., 1965. Biochim. Biophys. Acta 105, 562–574.

    Google Scholar 

  46. Harper, E., Seifter, S. and Hospelhorn, V., 1965. Biochem. Biophys. Res. Commun. 18, 627–632.

    Google Scholar 

  47. Takahashi, S. and Seifter, S., 1972. J. Applied Bacteriol. 35, 647–657.

    Google Scholar 

  48. Kono, T., 1968. Biochemistry 7, 1106–1114.

    Google Scholar 

  49. Mitchell, W. M., 1968. Biochim. Biophys. Acta 159, 554–557.

    Google Scholar 

  50. Kula, M. R., Hatef-Haghi, D., Tauber-Finkelstein, M. and Shaltiel, S., 1976. Biochem. Biophys. Res. Commun 69, 389–396.

    Google Scholar 

  51. Lwebuga-Mukasa, J. S., Harper, E. and Taylor, P., 1976. Biochemistry 15, 4736–4741.

    Google Scholar 

  52. The Nomenclature of Multiple Forms of Enzymes. UPAC-IUB Commission of Biochemical Nomenclature (1971) J. Biol. Chem. 246, 6127–6128.

    Google Scholar 

  53. Levdikova, G. A., Orekhovich, V. N., Solovjeva, V. N. and Shpikiter, V. O., 1963. Dokl. Akad. Nauk SSSR 153, 725–727.

    Google Scholar 

  54. Brown, J. R., Greenshields, R. N., Yamasaki, M. and Neurath, H., 1963. Biochemistry 2, 867–876.

    Google Scholar 

  55. Titani, K., Hermodson, M. A., Ericsson, L. H., Walsh, K. A. and Neurath, H., 1972. Nature New Biology 238, 35–37.

    Google Scholar 

  56. Keay, L., 1969. Biochem. Biophys. Res. Commun 36, 257–271.

    Google Scholar 

  57. Winter, W. P., and Neurath, H., 1970. Biochemistry 9, 4673–4679.

    Google Scholar 

  58. Nordwig, A., 1962. Leder 13, 10–19.

    Google Scholar 

  59. Hohmann, P., Tobey, R. A. and Gurley, L. R., 1975. Biochem. Biophys. Res. Commun 63, 126–133.

    Google Scholar 

  60. Kinnier, W. J. and Wilson, J. E., 1977. J. Chromat. 135, 508–510.

    Google Scholar 

  61. Harris, E. D. and Krane, S. M., 1974. New Engl. J. Med. 291, 557–568.

    Google Scholar 

  62. Weiss, J. B., 1976. Intern. Review of Connect. Tissue Res. (Hall, D. A. and Jackson, D. S. eds), vol. 7, pp. 102–157, Academic Press, New York.

  63. Piez, K. A., Bladen, H. A., Lane, J. M., Miller, E. J., Bornstein, P., Butler, N. T. and Kang, A. H., 1968. Brookhaven Symp. Biol. 21, 345.

    Google Scholar 

  64. Bruns, R. R., and Gross, J., 1973. Biochemistry 12, 808–815.

    Google Scholar 

  65. Kühn, K., and Eggl, M., 1966. Biochem. Ztschr. 346, 197–205.

    Google Scholar 

  66. Schmitt, F. O., Gross, J. and Highberger, J. H., 1953. Proc. Natl. Acad. Sci. (Wash.) 39, 459–470.

    Google Scholar 

  67. Stark, M., and Kühn, K., 1968. Eur. J. Biochem. 6, 542–544.

    Google Scholar 

  68. Gross, J. and Lapière, C. M., 1962. Proc. Natl. Acad. Sci. (Wash.) 48, 1014–1022.

    Google Scholar 

  69. Gross, J., Harper, E., Harris, E. D., McCroskery, P. A., Highberger, J. H., Corbett, C. and Kang, A. H., 1974. Biochem. Biophys. Res. Commun. 6, 605–612.

    Google Scholar 

  70. Leibovich, S. J., and Weiss, J. B., 1973. Connect. Tissue Res. 2, 11–19.

    Google Scholar 

  71. Nordwig, A., and John, W. F., 1968. Eur. J. Biochem. 3, 519–529.

    Google Scholar 

  72. Stevenson, K. J., and Gaucher, M., 1975. Biochem. J. 151, 527–542.

    Google Scholar 

  73. Rippon, J. W., and Peck, G. L., 1967. J. Invest. Dermatol. 49, 371–378.

    Google Scholar 

  74. Ribadeau-Dumas, B., Brignon, G., Grosclaude, F., and Mercier, J. C., 1972. Eur. J. Biochem. 25, 505–514.

    Google Scholar 

  75. Keil, B., 1977. Solid Phase Methods in Protein Sequence Analysis (Previero, A. and Coletti-Previero, M.-A., eds) Symp. 5, pp. 287–292, Elsevier/North-Holland.

  76. Coletti-Previero, M. C., and Cavadore, J. C., 1975. Immunochemistry 12, 93–95.

    Google Scholar 

  77. Spadari, S., Subramanian, A. R., and Kalnitsky, G., 1974. Biochim. Biophys. Acta 359, 267–272.

    Google Scholar 

  78. Takahashi, S., and Seifter, S., 1970. Biochim. Biophys. Acta 214, 556–558.

    Google Scholar 

  79. Solovjeva, N. I., and Orekhovich, V. N., 1969. Biokhimiya 34, 620–626.

    Google Scholar 

  80. Pangburn, M. K., and Walsh, K. A., 1975. Biochemistry 14, 4050–4054.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Institut Pasteur, 28 rue du Docteur Roux, 75724, Paris Cedex 15

    Borivoj Keil

Authors
  1. Borivoj Keil
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Keil, B. Some newly characterized collagenases from procaryotes and lower eucaryotes. Mol Cell Biochem 23, 87–108 (1979). https://doi.org/10.1007/BF00226230

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00226230

Keywords

Search

Navigation