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Determinant of efficiency of a monomeric enzyme: Acceleration by site-specific molecules for trypsin

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Summary

The interaction of a specific ligand at substrate binding site was shown to be responsible for the catalytic efficiency of trypsin. The reasoning of ‘induced fit’ theory was refined by kinetic analysis of characteristic properties of ‘inverse’ substrates.

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References

  1. G.P. Hess and B. Keil, in: The Enzymes, vol. 3, p. 213 and 250. Ed. P.D. Boyer. Academic Press, New York 1971.

    Google Scholar 

  2. K. Tanizawa, Y. Kasaba and Y. Kanaoka, J. Am. chem. Soc.99, 4485 (1977).

    PubMed  Google Scholar 

  3. K. Tanizawa, S. Ishii and Y. Kanaoka, Biochem. biophys. Res. Commun.32, 893 (1968).

    Article  PubMed  Google Scholar 

  4. K. Tanizawa, S. Ishii and Y. Kanaoka, J. Biochem.69, 893 (1971).

    PubMed  Google Scholar 

  5. T. Inagami and T. Murachi, J. biol. Chem.239, 1395 (1964).

    PubMed  Google Scholar 

  6. B.F. Erlanger and H. Castleman, Biochim. biophys. Acta85, 507 (1964).

    PubMed  Google Scholar 

  7. F. Seydoux, G. Coutouly and J. Yon, Biochemistry10, 2284 (1971).

    Article  PubMed  Google Scholar 

  8. B.M. Sanborn and G.E. Hein, Biochemistry7, 3616 (1968).

    Article  PubMed  Google Scholar 

  9. Preliminary results with p-amidinophenyl N-acetylglycinate suggest that assumption of the involvement of such additional subsites is not necessary; K. Tanizawa, M. Nakano and Y. Kanaoka, in preparation.

  10. The contribution of site-specific group in substrate has been analyzed thermodynamically and kinetically in the chymotrypsin-12 and trypsin-catalyzed reactions13. The presence of specificity in the deacylation step has been shown earlier12, while for trypsin not confirmed until the inverse technique now has been introduced.

  11. M.L. Bender, F.J. Kézdy and G.R. Gunter, J. Am. chem. Soc.86, 3714 (1964).

    Article  Google Scholar 

  12. F. Seydoux and J. Yon, Biochem. biophys. Res. Commun.44, 745 (1971).

    Article  PubMed  Google Scholar 

  13. D.E. Koshland, Jr, Proc. natl Acad. Sci. USA44, 98 (1958).

    Google Scholar 

  14. D.E. Koshland, Jr, in: The Enzymes, vol. 1, p. 342. Ed. P.D. Boyer. Academic Press, New York 1970.

    Google Scholar 

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Authors and Affiliations

  1. Faculty of Pharmaceutical Sciences, Hokkaido University, 060, Sapporo, (Japan)

    K. Tanizawa & Y. Kanaoka

Authors
  1. K. Tanizawa
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  2. Y. Kanaoka
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Additional information

This work was supported by grants from the Ministry of Education, Science and Culture, Japan.

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Tanizawa, K., Kanaoka, Y. Determinant of efficiency of a monomeric enzyme: Acceleration by site-specific molecules for trypsin. Experientia 35, 16–17 (1979). https://doi.org/10.1007/BF01917847

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  • DOI: https://doi.org/10.1007/BF01917847

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