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A new arylsulfatase from the marine mollusk Turbo chrysostomus

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Chemistry of Natural Compounds Aims and scope

A new arylsulfatase (EC 3.1.6.1) was isolated from the liver of the marine mollusk Turbo chrysostomus. The enzyme catalyzed hydrolysis of potassium p-nitrophenylsulfate, did not affect natural fucoidan, and catalyzed cleavage of sulphate in the C4 position of xylose included in carbohydrate chains of holothurian triterpene glycosides. Halistanol sulphate and glycosides from starfish that contained sulfates in the aglycon part of the molecule inhibited the activity of the arylsulfatase. Several holothurian glycosides in small concentrations (3.5–8 × 10–10 M) increased the enzyme activity. The arylsulfatase activity was maximal at pH 7. Its molecular weight was 35 kDa according to gel-filtration. The Michaelis constant (KM) for hydrolysis of p-nitrophenylsulfate was 10 mM. The inactivation half-life of the enzyme was 15 min at 55°C.

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References

  1. D. P. Wright, D. I. Rosendale, and A. M. Robertson, FEMS Microbiol. Lett., 190, 73 (2000).

    Article  PubMed  CAS  Google Scholar 

  2. Q. Yang, L. M. Anderer, and R. C. Anderer, Dev. Biol., 135, 53 (1989).

    Article  PubMed  Google Scholar 

  3. A. Hallman and M. Sumper, Eur. J. Biochem., 221, 143 (1994).

    Article  Google Scholar 

  4. G. Parenti, G. Meroni, and A. Ballabio, Curr. Opin. Genet. Dev., 7, 386 (1997).

    Article  PubMed  CAS  Google Scholar 

  5. P. F. Lloyd and K. O. Lloyd, Nature, 199, 287 (1963).

    Article  CAS  Google Scholar 

  6. N. M. Thanassi and H. I. Nakada, Arch. Biochem. Biophys., 118, 172 (1967).

    Article  CAS  Google Scholar 

  7. K. Kitamura, M. Matsuo, and T. Yasui, Biosci. Biotechnol. Biochem., 56, 490 (1992).

    Article  CAS  Google Scholar 

  8. S. Agogbua, E. Anosike, and E. Ugochukwu, Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol., 59, 169 (1978).

    Google Scholar 

  9. H. Banna, Histochem. J., 12, 145 (1980).

    Article  PubMed  CAS  Google Scholar 

  10. E. Corner, J. Mar. Biol. Assoc. U. K., 39, 51 (1960).

    Article  CAS  Google Scholar 

  11. T. Selmer, A. Hallman, B. Schmidt, M. Sumper, and K. von Figura, Eur. J. Biochem., 238, 341 (1996).

    Article  PubMed  CAS  Google Scholar 

  12. B. Schmidt, T. Selmer, F. Ingendoh, and K. von Figura, Cell, 82, 271 (1995).

    Article  PubMed  CAS  Google Scholar 

  13. C. S. Bond, P. R. Clements, S. J. Ashby, C. A. Collyer, S. J. Harrop, J. J. Hopwood, and J. M. Guss, Structure, 5, 277 (1997).

    Article  PubMed  CAS  Google Scholar 

  14. G. Lukatela, N. Krauss, K. Theis, T. Selmer, V. Gieselmann, K. von Figura, and W. Saenger, Biochemistry, 37, 3654 (1998).

    Article  PubMed  CAS  Google Scholar 

  15. A. B. Roy, Anal. Biochem., 165, 1 (1987).

    Article  PubMed  CAS  Google Scholar 

  16. H. Hatanaka, Y. Ogawa, and F. Egami, Biochem. J., 159, 445 (1979).

    Google Scholar 

  17. R. Daniel, O. Berteau, L. Chevolot, A. Varenne, P. Gareil, and R. Goasdoue, Eur. J. Biochem., 268, 5617 (2001).

    Article  PubMed  CAS  Google Scholar 

  18. D. C. Spaulding and D. E. Morse, J. Comp. Physiol., B, 161, 498 (1991).

    Google Scholar 

  19. T. Ueki, Y. Sawada, Y. Fukagawa, and T. Oki, Biosci. Biotechnol. Biochem., 59, 1062 (1995).

    Article  PubMed  CAS  Google Scholar 

  20. W. Knoess and K.-W. Glombitza, Phytochemistry, 32, 1119 (1993).

    Article  CAS  Google Scholar 

  21. V. Descamps, S. Colin, M. Lahaye, M. Jam, C. Richard, P. Potin, T. Barberon, J.-C. Yvin, and B. Kloareg, Mar. Biotechnol., 8, 27 (2006).

    Article  PubMed  CAS  Google Scholar 

  22. S. D. Anastyuk, N. M. Shevchenko, P. S. Dmitrenok, and T. N. Zvyagintseva, Carbohydr. Res., 346, 2975 (2011).

    Article  PubMed  CAS  Google Scholar 

  23. I. Yu. Bakunina, V. V. Sova, L. A. Elyakova, T. N. Makar′eva, V. A. Stonik, E. A. Permyakov, and V. I. Emel′yanenko, Biokhimiya, 56 (8), 1397 (1991).

    CAS  Google Scholar 

  24. M. I. Kusaykin, M. S. Pesentseva, A. S. Sil′chemko, S. A. Avilov, V. V. Sova, T. N. Zvyagintseva, and V. A. Stonik, Bioorg. Khim., 32 (1), 71 (2006).

    Google Scholar 

  25. N. V. Ivanchina, T. V. Malyrenko, A. A. Kicha, A. I. Kalinovsky, P. S. Dmitrenok, and S. P. Ermakova, Bioorg. Khim., 37 (4), 559 (2011).

    PubMed  CAS  Google Scholar 

  26. N. Fusetani, Y. Kato, K. Hashimoto, T. Komori, Y. Itakura, and T. Kawasaki, J. Nat. Prod., 47, 995 (1984).

    Article  Google Scholar 

  27. V. I. Kalinin, A. S. Silchenko, S. A. Avilov, V. A. Stonik, and A. V. Smirnov, Phytochem. Rev., 4 (2–3), 221 (2005).

    Article  CAS  Google Scholar 

  28. A. S. Silchenko, S. A. Avilov, V. I. Kalinin, A. I. Kalinovsky, P. S. Dmitrenok, S. N. Fedorov, V. G. Stepanov, Z. Dong, and V. A. Stonik, J. Nat. Prod., 71 (3), 351 (2008).

    Article  PubMed  CAS  Google Scholar 

  29. A. S. Silchenko, A. I. Kalinovsky, S. A. Avilov, P. V. Andryjaschenko, P. S. Dmitrenok, E. A. Yurchenko, and V. I. Kalinin, Nat. Prod. Commun., 6, 1075 (2011).

    PubMed  CAS  Google Scholar 

  30. A. A. Kicha, A. I. Kalinovsky, E. V. Levina, V. A. Stonik, and G. B. Elyakov, Tetrahedron Lett., 24 (36), 3893 (1983).

    Article  CAS  Google Scholar 

  31. A. A. Kicha, N. V. Ivanchina, A. I. Kalinovsky, P. S. Dmitrenok, E. V. Sokolova, and I. G. Agafonova, Khim. Prir. Soedin., 64 (2007).

  32. I. Kitagawa and M. Kobayashi, Chem. Pharm. Bull., 26 (6), 1864 (1978).

    Article  CAS  Google Scholar 

  33. M. Bradford, Anal. Biochem., 72 (1–2), 248 (1976).

    Article  PubMed  CAS  Google Scholar 

Download references

Acknowledgment

This work was supported by the program of the Russian Academy of Science “Molecular and Cellular Biology”.

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Authors and Affiliations

  1. G. B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-East Branch, Russian Academy of Sciences, 690022, Vladivostok, Russia

    M. S. Pesentseva, V. V. Sova, Al. S. Sil′chenko, A. A. Kicha, Ar. S. Sil′chenko & T. N. Zvyagintseva

  2. Laboratoire d’Etude des Interactions des Molecules Alimentaires, Institut National de la Recherche Agronomique, B. P. 71627, 44316, Nantes, Cedex 3, France

    T. Haertle

Authors
  1. M. S. Pesentseva
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  2. V. V. Sova
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  3. Al. S. Sil′chenko
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  4. A. A. Kicha
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  5. Ar. S. Sil′chenko
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  6. T. Haertle
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  7. T. N. Zvyagintseva
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Correspondence to M. S. Pesentseva.

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Translated from Khimiya Prirodnykh Soedinenii, No. 5, September–October, 2012, pp. 759–764.

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Pesentseva, M.S., Sova, V.V., Sil′chenko, A.S. et al. A new arylsulfatase from the marine mollusk Turbo chrysostomus . Chem Nat Compd 48, 853–859 (2012). https://doi.org/10.1007/s10600-012-0400-4

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  • DOI: https://doi.org/10.1007/s10600-012-0400-4

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