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

Yuliya V. Preobrazhenskaya; Anna I. Sten'ko; Vladimir Yu. Lugovtsev; Andrej G. Moiseenok; Olga M. Kuratchik; Konstantin A. Mandrik; Alexander I. Voskoboev

doi:doi:10.11648/j.ab.20170502.13

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

Yuliya V. Preobrazhenskaya, Anna I. Sten'ko, Vladimir Yu. Lugovtsev, Andrej G. Moiseenok, Olga M. Kuratchik, Konstantin A. Mandrik, Alexander I. Voskoboev

Published in Advances in Biochemistry (Volume 5, Issue 2)

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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APA Style

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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TY  - JOUR
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
AU  - Alexander I. Voskoboev
Y1  - 2017/04/24
PY  - 2017
N1  - https://doi.org/10.11648/j.ab.20170502.13
DO  - 10.11648/j.ab.20170502.13
T2  - Advances in Biochemistry
JF  - Advances in Biochemistry
JO  - Advances in Biochemistry
SP  - 31
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

Yuliya V. Preobrazhenskaya

Department of Biology and Ecology, Grodno State Kupala University, Grodno, Belarus
Anna I. Sten'ko

Department of Biology and Ecology, Grodno State Kupala University, Grodno, Belarus
Vladimir Yu. Lugovtsev

Food and Drug Administration, Bethesda, USA
Andrej G. Moiseenok

NPTS “Biochemistry and Pharmacology”, Grodno, Belarus
Olga M. Kuratchik

GR D-V Observation Station and Hospital, Grodno, Belarus
Konstantin A. Mandrik

Department of Biology and Ecology, Grodno State Kupala University, Grodno, Belarus
Alexander I. Voskoboev

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

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APA Style

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}
}

Copy | Download

TY  - JOUR
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
AU  - Alexander I. Voskoboev
Y1  - 2017/04/24
PY  - 2017
N1  - https://doi.org/10.11648/j.ab.20170502.13
DO  - 10.11648/j.ab.20170502.13
T2  - Advances in Biochemistry
JF  - Advances in Biochemistry
JO  - Advances in Biochemistry
SP  - 31
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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