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Reactivation of Serratia marcescens mutant endonuclease by Hydroxilamine

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dc.contributor.author Khamidullina R.
dc.contributor.author Fazleeva I.
dc.contributor.author Trushin M.
dc.contributor.author Gimadutdinov O.
dc.date.accessioned 2019-01-22T20:52:49Z
dc.date.available 2019-01-22T20:52:49Z
dc.date.issued 2018
dc.identifier.uri https://dspace.kpfu.ru/xmlui/handle/net/149230
dc.description.abstract © 2018, Pharmainfo Publications. All rights reserved. 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 89thposition is replaced by glycine.
dc.subject Basal level of expression
dc.subject Endonuclease
dc.subject Histidine
dc.subject Hydroxylamine
dc.subject Plasmid
dc.title Reactivation of Serratia marcescens mutant endonuclease by Hydroxilamine
dc.type Article
dc.relation.ispartofseries-issue 9
dc.relation.ispartofseries-volume 10
dc.collection Публикации сотрудников КФУ
dc.relation.startpage 2341
dc.source.id SCOPUS-2018-10-9-SID85054284376

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  • Публикации сотрудников КФУ Scopus [24551]
    Коллекция содержит публикации сотрудников Казанского федерального (до 2010 года Казанского государственного) университета, проиндексированные в БД Scopus, начиная с 1970г.

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