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Characterization of enzymatic activity of MlrB and MlrC proteins involved in bacterial degradation of cyanotoxins microcystins

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Characterization of enzymatic activity of MlrB and MlrC proteins involved in bacterial degradation of cyanotoxins microcystins

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dc.contributor.author Dziga, Dariusz [SAP11017672] pl
dc.contributor.author Zielińska, Gabriela [SAP14023260] pl
dc.contributor.author Władyka, Benedykt [SAP12119116] pl
dc.contributor.author Bocheńska, Oliwia [SAP12019980] pl
dc.contributor.author Maksylewicz, Anna [SAP14016428] pl
dc.contributor.author Strzałka, Wojciech [SAP11018339] pl
dc.contributor.author Meriluoto, Jussi pl
dc.date.accessioned 2016-04-18T11:40:12Z
dc.date.available 2016-04-18T11:40:12Z
dc.date.issued 2016 pl
dc.identifier.uri http://ruj.uj.edu.pl/xmlui/handle/item/24254
dc.language eng pl
dc.rights Udzielam licencji. Uznanie autorstwa 4.0 Międzynarodowa *
dc.rights.uri http://creativecommons.org/licenses/by/4.0/pl/legalcode *
dc.title Characterization of enzymatic activity of MlrB and MlrC proteins involved in bacterial degradation of cyanotoxins microcystins pl
dc.type JournalArticle pl
dc.abstract.en Bacterial degradation of toxic microcystins produced by cyanobacteria is a common phenomenon. However, our understanding of the mechanisms of these processes is rudimentary. In this paper several novel discoveries regarding the action of the enzymes of the mlr cluster responsible for microcystin biodegradation are presented using recombinant proteins. In particular, the predicted active sites of the recombinant MlrB and MlrC were analyzed using functional enzymes and their inactive muteins. A new degradation intermediate, a hexapeptide derived from linearized microcystins by MlrC, was discovered. Furthermore, the involvement of MlrA and MlrB in further degradation of the hexapeptides was confirmed and a corrected biochemical pathway of microcystin biodegradation has been proposed. pl
dc.subject.en microcystin pl
dc.subject.en biochemical pathway pl
dc.subject.en biodegradation pl
dc.subject.en recombinant enzymes pl
dc.description.volume 8 pl
dc.description.number 3 pl
dc.identifier.doi 10.3390/toxins8030076 pl
dc.identifier.eissn 2072-6651 pl
dc.title.journal Toxins pl
dc.language.container eng pl
dc.affiliation Wydział Biochemii, Biofizyki i Biotechnologii : Zakład Biotechnologii Roślin pl
dc.affiliation Wydział Biochemii, Biofizyki i Biotechnologii : Zakład Fizjologii i Biologii Rozwoju Roślin pl
dc.affiliation Wydział Biochemii, Biofizyki i Biotechnologii : Zakład Biochemii Analitycznej pl
dc.subtype Article pl
dc.identifier.articleid 76 pl
dc.rights.original CC-BY; otwarte czasopismo; ostateczna wersja wydawcy; w momencie opublikowania; 0; pl
dc.identifier.project ROD UJ / P pl
.pointsMNiSW [2016 A]: 35


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Udzielam licencji. Uznanie autorstwa 4.0 Międzynarodowa Except where otherwise noted, this item's license is described as Udzielam licencji. Uznanie autorstwa 4.0 Międzynarodowa