The Stoichiometry of Binding of ATP and Its Derivatives to a Recombinant Selenophosphate Synthetase E197D Catalytically Inactive Mutant C17S
Advances in Biochemistry
Volume 5, Issue 2, April 2017, Pages: 31-34
Received: Dec. 30, 2014;
Accepted: Feb. 26, 2015;
Published: Apr. 24, 2017
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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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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.
Selenophosphate Synthetase, ATP-Binding, Monomer, TNP-ATP
To cite this article
Yuliya V. Preobrazhenskaya,
Anna I. Sten'ko,
Vladimir Yu. Lugovtsev,
Andrej G. Moiseenok,
Olga M. Kuratchik,
Konstantin A. Mandrik,
Alexander I. Voskoboev,
The Stoichiometry of Binding of ATP and Its Derivatives to a Recombinant Selenophosphate Synthetase E197D Catalytically Inactive Mutant C17S, Advances in Biochemistry.
Vol. 5, No. 2,
2017, pp. 31-34.
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