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The Stoichiometry of Binding of ATP and Its Derivatives to a Recombinant Selenophosphate Synthetase E197D Catalytically Inactive Mutant C17S

Received: 30 December 2014     Accepted: 26 February 2015     Published: 24 April 2017
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Abstract

Selenophosphate synthetase (SPS) catalyses formation of the universal donor of selenium equivalents in a living cell. It performs the selenophosphate formation from ATP and selenide in ATP-dependent manner. We have checked a catalytically inactive mutant C17S of bacterial SPS from E.coli, E197D, for ATP hydrolysis and ATP-binding. The ratio obtained for ATP-binding is 9.52 nM ATP: 7.0 nmol enzyme, however, the fraction of the protein applied to the size-exclusive column TSK 2000 under reaction conditions was homogenious. It is likely under the ATP-binding conditions C17S mutant of SPS represents a monomer. A sequence alignment of bacterial mutant C17S from strain K12 with a human SEPHSI shows it exhibits of 31% homology. It is supposingly SPSI is a functional and structural analogue of C17S and has a similar biological activity.

Published in Advances in Biochemistry (Volume 5, Issue 2)
DOI 10.11648/j.ab.20170502.13
Page(s) 31-34
Creative Commons

This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.

Copyright

Copyright © The Author(s), 2017. Published by Science Publishing Group

Keywords

Selenophosphate Synthetase, ATP-Binding, Monomer, TNP-ATP

References
[1] Hirosava-Takamori M., Jaecle H., Vorbruggen G. (2000). EMBO reports, 1, 441-446.
[2] Veres, Z., Kim, I. Y., Scholz, T. D., and Stadtman, T.C (1994) J. Biol. Chem., 269, 10597–10603.
[3] Lacourciere, G. M., Mihara, H., Kurihara, T., Esaki, N., and Stadtman, T.C. (2000) J. Biol. Chem., 275, 23769–23773.
[4] Mullins, L. S., et al (1997) J. Am.Chem.Soc., 119, 6684-6685.
[5] Preobrazhenskaya Y. V., Stenko A. I., Shvarts M. V., Lugovtsev V. Yu. (2013) J. Amino Acids, 2013.
[6] Kim, I. Y., Veres, Z., Stadtman, T. C. (1992) J. Biol. Chem., 267, 19650–19654.
[7] Low, S. C., Harney, J. W., Berry, M. J. (1995) J. Biol. Chem., 270, 21659-21664.
[8] Xu, Xue-M., Carlson, B. A , Mix, H., Irons R., Berry, M. J, Gladyshev V. N and Hatfield D.L. FASEB J. March 2006 20 (Meeting Abstract Supplement) A428.
[9] Selenium: Its Molecular Biology and Role in Human Health by Dolph L. Hatfield, Marla J. Berry, Vadim N. Gladyshev, Springer Science & Business media, 2011, p.27.
[10] Noinaj N., et al. (2012) J. Bacteriol., 194, 499-508.
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    Yuliya V. Preobrazhenskaya, Anna I. Sten'ko, Vladimir Yu. Lugovtsev, Andrej G. Moiseenok, Olga M. Kuratchik, et al. (2017). The Stoichiometry of Binding of ATP and Its Derivatives to a Recombinant Selenophosphate Synthetase E197D Catalytically Inactive Mutant C17S. Advances in Biochemistry, 5(2), 31-34. https://doi.org/10.11648/j.ab.20170502.13

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    ACS Style

    Yuliya V. Preobrazhenskaya; Anna I. Sten'ko; Vladimir Yu. Lugovtsev; Andrej G. Moiseenok; Olga M. Kuratchik, et al. The Stoichiometry of Binding of ATP and Its Derivatives to a Recombinant Selenophosphate Synthetase E197D Catalytically Inactive Mutant C17S. Adv. Biochem. 2017, 5(2), 31-34. doi: 10.11648/j.ab.20170502.13

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    AMA Style

    Yuliya V. Preobrazhenskaya, Anna I. Sten'ko, Vladimir Yu. Lugovtsev, Andrej G. Moiseenok, Olga M. Kuratchik, et al. The Stoichiometry of Binding of ATP and Its Derivatives to a Recombinant Selenophosphate Synthetase E197D Catalytically Inactive Mutant C17S. Adv Biochem. 2017;5(2):31-34. doi: 10.11648/j.ab.20170502.13

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  • @article{10.11648/j.ab.20170502.13,
      author = {Yuliya V. Preobrazhenskaya and Anna I. Sten'ko and Vladimir Yu. Lugovtsev and Andrej G. Moiseenok and Olga M. Kuratchik and Konstantin A. Mandrik and Alexander I. Voskoboev},
      title = {The Stoichiometry of Binding of ATP and Its Derivatives to a Recombinant Selenophosphate Synthetase E197D Catalytically Inactive Mutant C17S},
      journal = {Advances in Biochemistry},
      volume = {5},
      number = {2},
      pages = {31-34},
      doi = {10.11648/j.ab.20170502.13},
      url = {https://doi.org/10.11648/j.ab.20170502.13},
      eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ab.20170502.13},
      abstract = {Selenophosphate synthetase (SPS) catalyses formation of the universal donor of selenium equivalents in a living cell. It performs the selenophosphate formation from ATP and selenide in ATP-dependent manner. We have checked a catalytically inactive mutant C17S of bacterial SPS from E.coli, E197D, for ATP hydrolysis and ATP-binding. The ratio obtained for ATP-binding is 9.52 nM ATP: 7.0 nmol enzyme, however, the fraction of the protein applied to the size-exclusive column TSK 2000 under reaction conditions was homogenious. It is likely under the ATP-binding conditions C17S mutant of SPS represents a monomer. A sequence alignment of bacterial mutant C17S from strain K12 with a human SEPHSI shows it exhibits of 31% homology. It is supposingly SPSI is a functional and structural analogue of C17S and has a similar biological activity.},
     year = {2017}
    }
    

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    T1  - The Stoichiometry of Binding of ATP and Its Derivatives to a Recombinant Selenophosphate Synthetase E197D Catalytically Inactive Mutant C17S
    AU  - Yuliya V. Preobrazhenskaya
    AU  - Anna I. Sten'ko
    AU  - Vladimir Yu. Lugovtsev
    AU  - Andrej G. Moiseenok
    AU  - Olga M. Kuratchik
    AU  - Konstantin A. Mandrik
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    DO  - 10.11648/j.ab.20170502.13
    T2  - Advances in Biochemistry
    JF  - Advances in Biochemistry
    JO  - Advances in Biochemistry
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    EP  - 34
    PB  - Science Publishing Group
    SN  - 2329-0862
    UR  - https://doi.org/10.11648/j.ab.20170502.13
    AB  - Selenophosphate synthetase (SPS) catalyses formation of the universal donor of selenium equivalents in a living cell. It performs the selenophosphate formation from ATP and selenide in ATP-dependent manner. We have checked a catalytically inactive mutant C17S of bacterial SPS from E.coli, E197D, for ATP hydrolysis and ATP-binding. The ratio obtained for ATP-binding is 9.52 nM ATP: 7.0 nmol enzyme, however, the fraction of the protein applied to the size-exclusive column TSK 2000 under reaction conditions was homogenious. It is likely under the ATP-binding conditions C17S mutant of SPS represents a monomer. A sequence alignment of bacterial mutant C17S from strain K12 with a human SEPHSI shows it exhibits of 31% homology. It is supposingly SPSI is a functional and structural analogue of C17S and has a similar biological activity.
    VL  - 5
    IS  - 2
    ER  - 

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Author Information
  • Department of Biology and Ecology, Grodno State Kupala University, Grodno, Belarus

  • Department of Biology and Ecology, Grodno State Kupala University, Grodno, Belarus

  • Food and Drug Administration, Bethesda, USA

  • NPTS “Biochemistry and Pharmacology”, Grodno, Belarus

  • GR D-V Observation Station and Hospital, Grodno, Belarus

  • Department of Biology and Ecology, Grodno State Kupala University, Grodno, Belarus

  • Department of Biology and Ecology, Grodno State Kupala University, Grodno, Belarus

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