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Tertiary structural differences between microbial serine proteases and pancreatic serine enzymes

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Abstract

Although primary structural homology between bacterial serine proteases and those from the mammalian pancreas is slight, two-thirds of the residues in the bacterial enzyme SGPB as seen at 2.8-Å resolution, adopt a similar polypeptide chain conformation to that of the chymotrypsin family. The three major regions of difference show how this family of proteolytic enzymes has developed from the more primitive bacterial to the relatively sophisticated pancreatic enzymes.

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References

  1. Hartley, B. S., and Kauffman, D. L., Biochem. J., 101, 229–231 (1966).

    Article  CAS  Google Scholar 

  2. Meloun, B., et al., Biochim. biophys. Acta, 130, 543–545 (1966).

    Article  CAS  Google Scholar 

  3. Blow, D. M., Birktoft, J. J., and Hartley, B. S., Nature, 221, 337–340 (1969).

    Article  ADS  CAS  Google Scholar 

  4. Smillie, L. B., Furka, A., Nagabhushan, N., Stevenson, K. J., and Parkes, C. O., Nature, 218, 343–346 (1968).

    Article  ADS  CAS  Google Scholar 

  5. Walsh, K. A., and Neurath, H., Proc. natn. Acad. Sci. U.S.A., 52, 884–889 (1964).

    Article  ADS  CAS  Google Scholar 

  6. Mikes, O., Holeysovsky, V., Tomásek, V., and Sorm, F., Biochem. biophys. Res. Commun., 24, 346–353 (1966).

    Article  CAS  Google Scholar 

  7. Hartley, B. S., Phil. Trans. R. Soc., B 257, 77–86 (1970).

    Article  CAS  Google Scholar 

  8. Shotton, D. M., and Hartley, B. S., Nature, 225, 802–806 (1970).

    Article  ADS  CAS  Google Scholar 

  9. Birktoft, J. J., and Blow, D. M., J. molec. Biol., 68, 187–240 (1972).

    Article  CAS  Google Scholar 

  10. Shotton, D. M., and Watson, H. C., Nature, 225, 811–816 (1970).

    Article  ADS  CAS  Google Scholar 

  11. Stroud, R. M., Kay, L. M., and Dickerson, R. E., J. molec. Biol., 83, 185–208 (1974).

    Article  CAS  Google Scholar 

  12. Olsen, M. O. J., Nagabhushan, N., Dzwiniel, M., Smillie, L. B., and Whitaker, D. R., Nature, 228, 438–442 (1970).

    Article  ADS  Google Scholar 

  13. Johnson, P., and Smillie, L. B., FEBS Lett., 47, 1–6 (1974).

    Article  CAS  Google Scholar 

  14. Jurásek, L., et al., Biochem. biophys. Res. Commun., 61, 1095–1100 (1974).

    Article  Google Scholar 

  15. McLachlan, A. D., and Shotton, D. M., Nature, 229, 202–205 (1971).

    Article  CAS  Google Scholar 

  16. Wright, C. S., Alden, R. A., and Kraut, J., Nature, 221, 235–242 (1969).

    Article  ADS  CAS  Google Scholar 

  17. Codding, P. W., et al., Can. J. Biochem. 52, 208–220 (1974).

    Article  CAS  Google Scholar 

  18. Blow, D. M., and Crick, F. H. C., Acta Crystallogr., 12, 794–802 (1959).

    Article  CAS  Google Scholar 

  19. Hartley, B. S., Nature, 201, 1284–1287 (1964).

    Article  ADS  CAS  Google Scholar 

  20. Dickerson, R. E., J. molec. Biol., 57, 1–15 (1971).

    Article  CAS  Google Scholar 

  21. Tulinsky, A., Vandlen, R. L., Morimoto, C. N., Mani, N. V., and Wright, L. H., Biochemistry, 12, 4185–4192 (1973).

    Article  CAS  Google Scholar 

  22. Mavridis, A., Tulinsky, A., and Liebman, M. N., Biochemistry, 13, 3661–3666 (1974).

    Article  CAS  Google Scholar 

  23. Shotton, D. M., White, N. J., and Watson, H. C., Cold Spring Harb. Symp. quant. Biol., 36, 91–105 (1971).

    Article  CAS  Google Scholar 

  24. Kaplan, H., and Dugas, H., Biochem. biophys. Res. Commun., 34, 681–685 (1969).

    Article  CAS  Google Scholar 

  25. Matthews, B. W., Sigler, P. B., Henderson, R., and Blow, D. M., Nature, 214, 652–656 (1967).

    Article  ADS  CAS  Google Scholar 

  26. Siegal, S., Brady, A. H., and Awad, W. M., J. biol. Chem., 247, 4155–4159 (1972).

    Google Scholar 

  27. deHaen, C., Neurath, H., and Teller, D. C., J. molec. Biol., 92, 225–259 (1975).

    Article  CAS  Google Scholar 

  28. Freer, S. T., Kraut, J., Robertus, J. D., Wright, H. T., and Xuong Ng, H., Biochemistry, 9, 1997–2009 (1970).

    Article  CAS  Google Scholar 

  29. Henderson, R., J. molec. Biol., 54, 341–354 (1970).

    Article  CAS  Google Scholar 

  30. Narahashi, Y., and Yoda, K., J. Biochem., 73, 831–841 (1973).

    Article  CAS  Google Scholar 

  31. Johnson, P., and Smillie, L. B., Can. J. Biochem., 49, 548–562 (1971).

    Article  CAS  Google Scholar 

  32. McLachlan, A. D., J. molec Biol., 64, 417–437 (1972).

    Article  CAS  Google Scholar 

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Author notes

  1. Michael N. G. James: On leave, Department of Structural Chemistry, Weizmann Institute of Science, Rehovot, Israel.

Authors and Affiliations

  1. Department of Biochemistry, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada

    Louis T. J. Delbaere, Wendy L. B. Hutcheon, Michael N. G. James & William E. Thiessen

  2. Chemistry Division, Oak Ridge National Laboratories, Oak Ridge, Tennessee, 37830

    William E. Thiessen

Authors
  1. Louis T. J. Delbaere
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  2. Wendy L. B. Hutcheon
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  3. Michael N. G. James
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  4. William E. Thiessen
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Delbaere, L., Hutcheon, W., James, M. et al. Tertiary structural differences between microbial serine proteases and pancreatic serine enzymes. Nature 257, 758–763 (1975). https://doi.org/10.1038/257758a0

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  • DOI: https://doi.org/10.1038/257758a0

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