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dc.contributor.authorLeggio, Leila Loen
dc.contributor.authorSimmons, Thomasen
dc.contributor.authorPoulsen, Jens-Christian Nen
dc.contributor.authorFrandsen, Kristian EHen
dc.contributor.authorHemsworth, Glyn Ren
dc.contributor.authorStringer, Mary Aen
dc.contributor.authorFreiesleben, Pernille vonen
dc.contributor.authorTovborg, Mortenen
dc.contributor.authorJohansen, Katja Sen
dc.contributor.authorMaria, Leonardo Deen
dc.contributor.authorHarris, Paul Ven
dc.contributor.authorSoong, Chee-Leongen
dc.contributor.authorDupree, Paulen
dc.contributor.authorTryfona, Theodoraen
dc.contributor.authorLenfant, Nicolasen
dc.contributor.authorHenrissat, Bernarden
dc.contributor.authorDavies, Gideon Jen
dc.contributor.authorWalton, Paul Hen
dc.date.accessioned2015-07-24T14:47:45Z
dc.date.available2015-07-24T14:47:45Z
dc.date.issued2015-01-22en
dc.identifier.citationLeggio et al. Nature Communications (2015) 6, Article number 5961. DOI:10.1038/ncomms6961en
dc.identifier.issn2041-1723
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/249072
dc.description.abstractLytic polysaccharide monooxygenases (LPMOs) are recently discovered enzymes that oxidatively deconstruct polysaccharides. LPMOs are fundamental in the effective utilization of these substrates by bacteria and fungi; moreover, the enzymes have significant industrial importance. We report here the activity, spectroscopy and three-dimensional structure of a starch-active LPMO, a representative of the new CAZy AA13 family. We demonstrate that these enzymes generate aldonic acid-terminated malto-oligosaccharides from retrograded starch and boost significantly the conversion of this recalcitrant substrate to ​maltose by β-amylase. The detailed structure of the enzyme’s active site yields insights into the mechanism of action of this important class of enzymes.
dc.description.sponsorshipThis work was supported by a grant from the European Research Agency—Industrial Biotechnology Initiative as financed by the national research councils: Biotechnology and Biological Sciences Research Council (grant number BB/L000423) and Agence Française de l'Environnement et de la Maîtrise de l'Energie (grant number 1201C102). The Danish Council for Strategic Research (grant numbers 12-134923 and 12-134922). The Danish Ministry of Higher Education and Science through the Instrument Center DANSCATT and the European Community’s Seventh Framework Programme (FP7/2007-2013) under BioStruct-X (grant agreement N°283570) funded travel to synchrotrons. P.H.W. acknowledges the experimental assistance of Rebecca Gregory and Dr Victor Chechik. L.L.L. acknowledges the experimental assistance of Dorthe Boelskifte and the ESRF and MAXLAB staff for assistance with data collection.
dc.languageEnglishen
dc.language.isoenen
dc.publisherNPG
dc.rightsAttribution 2.0 UK: England & Wales*
dc.rights.urihttp://creativecommons.org/licenses/by/2.0/uk/*
dc.subjectBiological sciencesen
dc.subjectBiochemistryen
dc.subjectBiotechnologyen
dc.titleStructure and boosting activity of a starch-degrading lytic polysaccharide monooxygenaseen
dc.typeArticle
dc.audienceOA-4719
dc.rightsHolderBBSRC
dc.description.versionThis is the final version of the article. It first appeared from NPG via http://dx.doi.org/10.1038/ncomms6961en
prism.number5961en
prism.publicationDate2015en
prism.publicationNameNature Communicationsen
prism.volume6en
dc.rioxxterms.projectidBB/L000423
dcterms.dateAccepted2014-11-25en
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserveden
rioxxterms.licenseref.startdate2015-01-22en
dc.contributor.orcidDupree, Paul [0000-0001-9270-6286]
dc.contributor.orcidTryfona, Theodora [0000-0002-1618-3521]
dc.identifier.eissn2041-1723
rioxxterms.typeJournal Article/Reviewen
pubs.funder-project-idBBSRC (via University of York) (R1500502)
pubs.funder-project-idBiotechnology and Biological Sciences Research Council (BB/L000423/1)


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Attribution 2.0 UK: England & Wales
Except where otherwise noted, this item's licence is described as Attribution 2.0 UK: England & Wales