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Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent - Nature

  • ️Cambillau, Christian
  • ️Thu Apr 16 1992
  • Letter
  • Published: 16 April 1992

Nature volume 356pages 615–618 (1992)Cite this article

Abstract

LIPASES belong to a class of esterases whose activity on trigly-cerides is greatly enhanced at lipid–water interfaces1. This phenomenon, called interfacial activation2, has a structural explanation: a hydrophobic lid, which at rest covers the catalytic site, is displaced on substrate or inhibitor binding, and probably interacts with the lipid matrix3–6. Fusarium solani pisi cutinase belongs to a group of homologous enzymes of relative molecular mass 22–25K (ref. 7) capable of degrading cutin, the insoluble lipid-polyester matrix covering the surface of plants7, and hydrolysing triglycerides7,8. Cutinases differ from classical Upases in that they do not exhibit interfacial activation; they are active on soluble as well as on emulsified triglycerides. Cutinases therefore establish a bridge between esterases and lipases. We report here the three-dimensional structure of a recombinant cutinase from F. solani pisi, expressed in Escherichia coli9,10. Cutinase is an α–β protein; the active site is composed of the triad Ser 120, His 188 and Asp 175. Unlike other lipases, the catalytic serine is not buried under surface loops, but is accessible to solvent. This could explain why cutinase does not display interfacial activation.

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References

  1. Sarda L. & Desnuelle, P. Biochem. biophys. Acta 30, 513–521 (1958).

    Article  CAS  Google Scholar 

  2. Verger, R. & de Haas, G. H. A. Rev. Biophys. Bioengng 5, 77–117 (1976).

    Article  CAS  Google Scholar 

  3. Brady, L. et al. Nature 343, 767–770 (1990).

    Article  ADS  CAS  Google Scholar 

  4. Brzozowski, A. M. et al. Nature 351, 491–494 (1991).

    Article  ADS  CAS  Google Scholar 

  5. Winkler, F. K., D'Arcy, A. & Hunziker, W. Nature 343, 771–774 (1990).

    Article  ADS  CAS  Google Scholar 

  6. Schrag, J. D., Li, Y., Wu, S. & Cygler, M. Nature 351, 761–764 (1991).

    Article  ADS  CAS  Google Scholar 

  7. Kolattudkudy, P. E. in Lipases (eds Brorström, B & Brackman, H) 471–504 (Elsevier, Amsterdam, 1984).

    Google Scholar 

  8. Lauwereys, M., de Geus, P., de Meutter, J., Stanssens, P. & Matthyssens, G. in Lipases-Structure, Mechanism and Genetic Engineering, Vol. 16 (eds Alberghina, L. et al.) 243–251 (VCH, Weinheim, 1991).

    Google Scholar 

  9. De Geus, P., Lauwereys, M. & Matthyssens, G. European Patent Application N. PCT 89.400.462.1.

  10. Abergel, C. et al. J. molec. Biol. 215, 215–216 (1990).

    Article  CAS  Google Scholar 

  11. Liao, D.-L. & Remington, S. J. J. biol. Chem. 265, 6528–6531 (1990).

    CAS  PubMed  Google Scholar 

  12. Sussman, J. L. et al. Science 253, 872–879 (1991).

    Article  ADS  CAS  Google Scholar 

  13. Franken, S. M., Robezoom, H. J., Kalk, K. H. & Dijkstra, B. W. EMBO J. 10, 1297–1302 (1991).

    Article  CAS  Google Scholar 

  14. Ettinger, W. F., Thukral, S. K. & Kolattukudy, P. E. Biochemistry 26, 7883–7892 (1987).

    Article  CAS  Google Scholar 

  15. Derewenda, Z. S. & Derewenda, U. Biochem. Cell Biol. (in the press).

  16. Sibanda, B. L., Blundell, T. L. & Thornton, J. M. J. molec. Biol. 206, 759–777 (1989).

    Article  CAS  Google Scholar 

  17. Pullman, B., Maigret, B. & Perahia, D. Theor. Chim. Acta 18, 344–354 (1970).

    Article  Google Scholar 

  18. Scott, D. L. et al. Science 250, 1541–1546 (1990).

    Article  ADS  CAS  Google Scholar 

  19. Blow, D. Nature 351, 444–445 (1991).

    Article  ADS  CAS  Google Scholar 

  20. Kabsch, W. J. appl. Crystallogr. 21, 67–71 (1988).

    Article  CAS  Google Scholar 

  21. Kabsch, W. J. appl. Crystallogr. 21, 916–924 (1988).

    Article  CAS  Google Scholar 

  22. Howard, A. J., J. appl. Crystallogr. 20, 383 (1987).

    Article  CAS  Google Scholar 

  23. Roussel, A. & Cambillau, C. in Silicon Graphics Directory 86 (Mountain View, California, 1991).

    Google Scholar 

  24. Brünger, A. T., Karplus, M. & Petsko, G. Acta crystallogr. A45, 50–61 (1989).

    Article  Google Scholar 

  25. Connolly, M. L. Science 306, 287–290 (1983).

    Google Scholar 

  26. Colloc'h, N., & Mornon, J. P. J. molec graphics 5, 170 (1987).

    Article  Google Scholar 

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Author information

Author notes

  1. Pieter De Geus

    Present address: Unilever Research Laboratorium, Oliver van Noortlaan 120, 3133 AT, Vlaardingen, The Netherlands

  2. Christian Cambillau: To whom correspondence should be addressed

Authors and Affiliations

  1. LCCMB-CNRS, Faculté de médecine Nord, 13326, Marseille, Cedex 15, France

    Chrislaine Martinez & Christian Cambillau

  2. CORVAS International N.V., J. Plateaustraat 22, B9000, Gent, Belgium

    Pieter De Geus, Marc Lauwereys & Gaston Matthyssens

Authors

  1. Chrislaine Martinez

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  2. Pieter De Geus

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  3. Marc Lauwereys

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  4. Gaston Matthyssens

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  5. Christian Cambillau

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Martinez, C., De Geus, P., Lauwereys, M. et al. Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent. Nature 356, 615–618 (1992). https://doi.org/10.1038/356615a0

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  • Received: 30 December 1991

  • Accepted: 12 February 1992

  • Issue Date: 16 April 1992

  • DOI: https://doi.org/10.1038/356615a0

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