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dc.contributor.authorStanisci, Annalucia
dc.contributor.authorTøndervik, Anne
dc.contributor.authorGaardløs, Margrethe
dc.contributor.authorLervik, Anders
dc.contributor.authorSkjåk-Bræk, Gudmund
dc.contributor.authorSletta, Håvard
dc.contributor.authorAachmann, Finn Lillelund
dc.date.accessioned2021-08-26T11:11:49Z
dc.date.available2021-08-26T11:11:49Z
dc.date.created2020-08-19T16:42:31Z
dc.date.issued2020
dc.identifier.citationACS Omega. 2020, 5 (8), 4352-4361.en_US
dc.identifier.issn2470-1343
dc.identifier.urihttps://hdl.handle.net/11250/2771389
dc.description.abstractAlginate is a linear copolymer composed of 1→4 linked β-d-mannuronic acid (M) and its epimer α-l-guluronic acid (G). The polysaccharide is first produced as homopolymeric mannuronan and subsequently, at the polymer level, C-5 epimerases convert M residues to G residues. The bacterium Azotobacter vinelandii encodes a family of seven secreted and calcium ion-dependent mannuronan C-5 epimerases (AlgE1–AlgE7). These epimerases consist of two types of structural modules: the A-modules, which contain the catalytic site, and the R-modules, which influence activity through substrate and calcium binding. In this study, we rationally designed new hybrid mannuronan C-5 epimerases constituting the A-module from AlgE6 and the R-module from AlgE4. This led to a better understanding of the molecular mechanism determining differences in MG- and GG-block-forming properties of the enzymes. A long loop with either tyrosine or phenylalanine extruding from the β-helix of the enzyme proved essential in defining the final alginate block structure, probably by affecting substrate binding. Normal mode analysis of the A-module from AlgE6 supports the results.en_US
dc.language.isoengen_US
dc.publisherAmerican Chemical Societyen_US
dc.rightsNavngivelse-Ikkekommersiell 4.0 Internasjonal*
dc.rights.urihttp://creativecommons.org/licenses/by-nc/4.0/deed.no*
dc.titleIdentification of a Pivotal Residue for Determining the Block Structure-Forming Properties of Alginate C-5 Epimerasesen_US
dc.typePeer revieweden_US
dc.typeJournal articleen_US
dc.description.versionpublishedVersionen_US
dc.rights.holderThis is an open access article published under an ACS AuthorChoice License, which permits copying and redistribution of the article or any adaptations for non-commercial purposes.en_US
dc.source.pagenumber4352-4361en_US
dc.source.volume5en_US
dc.source.journalACS Omegaen_US
dc.source.issue8en_US
dc.identifier.doi10.1021/acsomega.9b04490
dc.identifier.cristin1824132
dc.relation.projectNorges forskningsråd: 294946en_US
dc.relation.projectNorges forskningsråd: 250875en_US
dc.relation.projectNorges forskningsråd: 226244en_US
dc.relation.projectNorges forskningsråd: 221576en_US
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode1


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Navngivelse-Ikkekommersiell 4.0 Internasjonal
Except where otherwise noted, this item's license is described as Navngivelse-Ikkekommersiell 4.0 Internasjonal