dc.contributor.author | Stanisci, Annalucia | |
dc.contributor.author | Tøndervik, Anne | |
dc.contributor.author | Gaardløs, Margrethe | |
dc.contributor.author | Lervik, Anders | |
dc.contributor.author | Skjåk-Bræk, Gudmund | |
dc.contributor.author | Sletta, Håvard | |
dc.contributor.author | Aachmann, Finn Lillelund | |
dc.date.accessioned | 2021-03-24T09:56:12Z | |
dc.date.available | 2021-03-24T09:56:12Z | |
dc.date.created | 2020-08-19T16:42:31Z | |
dc.date.issued | 2020 | |
dc.identifier.citation | ACS Omega. 2020, 5 (8), 4352-4361. | en_US |
dc.identifier.issn | 2470-1343 | |
dc.identifier.uri | https://hdl.handle.net/11250/2735247 | |
dc.description.abstract | Alginate 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.iso | eng | en_US |
dc.publisher | American Chemical Society | en_US |
dc.title | Identification of a Pivotal Residue for Determining the Block Structure-Forming Properties of Alginate C-5 Epimerases | en_US |
dc.type | Peer reviewed | en_US |
dc.type | Journal article | en_US |
dc.description.version | publishedVersion | en_US |
dc.source.pagenumber | 4352-4361 | en_US |
dc.source.volume | 5 | en_US |
dc.source.journal | ACS Omega | en_US |
dc.source.issue | 8 | en_US |
dc.identifier.doi | 10.1021/acsomega.9b04490 | |
dc.identifier.cristin | 1824132 | |
dc.relation.project | Norges forskningsråd: 294946 | en_US |
dc.relation.project | Norges forskningsråd: 250875 | en_US |
dc.relation.project | Norges forskningsråd: 226244 | en_US |
dc.relation.project | Norges forskningsråd: 221576 | en_US |
dc.description.localcode | This 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 |
cristin.ispublished | true | |
cristin.fulltext | original | |
cristin.qualitycode | 1 | |