Reactivation of Serratia marcescens mutant endonuclease by Hydroxilamine

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.