Форма представления | Статьи в зарубежных журналах и сборниках |
Год публикации | 2018 |
Язык | английский |
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Гимадутдинов Олег Александрович, автор
Трушин Максим Викторович, автор
Хамидуллина Раиса Гусмановна, автор
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Фазлеева Ильмира Ильдаровна, автор
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Библиографическое описание на языке оригинала |
R.G. Khamidullina. Reactivation of Serratia marcescens Mutant Endonuclease by Hydroxilamine/R.G. Khamidullina, I.I. Fazleeva, M.V.Trushin, O.A. Gimadutdinov///J. Pharm. Sci. & Res. Vol. 10(9), 2018, 2341-2345 |
Аннотация |
It is known that histidine plays an important role in the catalytic activity of many nucleases. Performing the function of a common base of these enzymes, it activates the formation of hydroxyl from the water molecule, which, in turn, by attacking the phosphorus atom of the diester bond causes its rupture. It was previously shown that in the endonuclease Serratia marcescens, the replacement of histidine with glycine results in its inactivation. We were able to restore the hydroxylamine activity of the mutant enzyme Serratia marcescens endonuclease, in which histidine in the 89th position is replaced by glycine.
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Ключевые слова |
Key words: endonuclease, plasmid, basal level of expression, hydroxylamine, histidine. |
Название журнала |
Journal of Pharmaceutical Sciences and Research
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https://repository.kpfu.ru/?p_id=187009 |
Полная запись метаданных |
Поле DC |
Значение |
Язык |
dc.contributor.author |
Гимадутдинов Олег Александрович |
ru_RU |
dc.contributor.author |
Трушин Максим Викторович |
ru_RU |
dc.contributor.author |
Хамидуллина Раиса Гусмановна |
ru_RU |
dc.contributor.author |
Фазлеева Ильмира Ильдаровна |
ru_RU |
dc.date.accessioned |
2018-01-01T00:00:00Z |
ru_RU |
dc.date.available |
2018-01-01T00:00:00Z |
ru_RU |
dc.date.issued |
2018 |
ru_RU |
dc.identifier.citation |
R.G. Khamidullina. Reactivation of Serratia marcescens Mutant Endonuclease by Hydroxilamine/R.G. Khamidullina, I.I. Fazleeva, M.V.Trushin, O.A. Gimadutdinov///J. Pharm. Sci. & Res. Vol. 10(9), 2018, 2341-2345 |
ru_RU |
dc.identifier.uri |
https://repository.kpfu.ru/?p_id=187009 |
ru_RU |
dc.description.abstract |
Journal of Pharmaceutical Sciences and Research |
ru_RU |
dc.description.abstract |
It is known that histidine plays an important role in the catalytic activity of many nucleases. Performing the function of a common base of these enzymes, it activates the formation of hydroxyl from the water molecule, which, in turn, by attacking the phosphorus atom of the diester bond causes its rupture. It was previously shown that in the endonuclease Serratia marcescens, the replacement of histidine with glycine results in its inactivation. We were able to restore the hydroxylamine activity of the mutant enzyme Serratia marcescens endonuclease, in which histidine in the 89th position is replaced by glycine.
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ru_RU |
dc.language.iso |
ru |
ru_RU |
dc.subject |
Key words: endonuclease |
ru_RU |
dc.subject |
plasmid |
ru_RU |
dc.subject |
basal level of expression |
ru_RU |
dc.subject |
hydroxylamine |
ru_RU |
dc.subject |
histidine. |
ru_RU |
dc.title |
Reactivation of Serratia marcescens Mutant Endonuclease by Hydroxilamine |
ru_RU |
dc.type |
Статьи в зарубежных журналах и сборниках |
ru_RU |
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