| Autor: |
Andrej G. Moiseenok, Yuliya V. Preobrazhenskaya, Vladimir Yu. Lugovtsev, Olga M. Kuratchik, Anna I. Sten'ko, Alexander I. Voskoboev, Konstantin A. Mandrik |
| Rok vydání: |
2017 |
| Předmět: |
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| Zdroj: |
Advances in Biochemistry. 5:31 |
| ISSN: |
2329-0870 |
| Popis: |
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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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