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Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase.

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cam.issuedOnline2015-01-22
dc.audienceOA-4719
dc.contributor.authorLo Leggio, Leila
dc.contributor.authorSimmons, Thomas J
dc.contributor.authorPoulsen, Jens-Christian N
dc.contributor.authorFrandsen, Kristian EH
dc.contributor.authorHemsworth, Glyn R
dc.contributor.authorStringer, Mary A
dc.contributor.authorvon Freiesleben, Pernille
dc.contributor.authorTovborg, Morten
dc.contributor.authorJohansen, Katja S
dc.contributor.authorDe Maria, Leonardo
dc.contributor.authorHarris, Paul V
dc.contributor.authorSoong, Chee-Leong
dc.contributor.authorDupree, Paul
dc.contributor.authorTryfona, Theodora
dc.contributor.authorLenfant, Nicolas
dc.contributor.authorHenrissat, Bernard
dc.contributor.authorDavies, Gideon J
dc.contributor.authorWalton, Paul H
dc.contributor.orcidDupree, Paul [0000-0001-9270-6286]
dc.contributor.orcidTryfona, Theodora [0000-0002-1618-3521]
dc.date.accessioned2015-07-24T14:47:45Z
dc.date.available2015-07-24T14:47:45Z
dc.date.issued2015-01-22
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.description.versionThis is the final version of the article. It first appeared from NPG via http://dx.doi.org/10.1038/ncomms6961
dc.identifier.citationLeggio et al. Nature Communications (2015) 6, Article number 5961. DOI:10.1038/ncomms6961
dc.identifier.eissn2041-1723
dc.identifier.issn2041-1723
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/249072
dc.languageEnglish
dc.language.isoeng
dc.publisherSpringer Science and Business Media LLC
dc.publisher.urlhttp://dx.doi.org/10.1038/ncomms6961
dc.rightsAttribution 2.0 UK: England & Wales
dc.rights.urihttp://creativecommons.org/licenses/by/2.0/uk/
dc.rightsHolderBBSRC
dc.rioxxterms.projectidBB/L000423
dc.subjectAcids
dc.subjectCatalytic Domain
dc.subjectCellulose
dc.subjectCopper
dc.subjectCrystallography, X-Ray
dc.subjectElectron Spin Resonance Spectroscopy
dc.subjectEvolution, Molecular
dc.subjectFungi
dc.subjectGenomics
dc.subjectHistidine
dc.subjectMaltose
dc.subjectMixed Function Oxygenases
dc.subjectOligosaccharides
dc.subjectOxygen
dc.subjectPhylogeny
dc.subjectPolysaccharides
dc.subjectProtein Conformation
dc.subjectProtein Structure, Tertiary
dc.subjectSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
dc.subjectStarch
dc.subjectSubstrate Specificity
dc.subjectbeta-Amylase
dc.titleStructure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase.
dc.typeArticle
dcterms.dateAccepted2014-11-25
prism.number5961
prism.publicationDate2015
prism.publicationNameNat Commun
prism.volume6
pubs.funder-project-idBBSRC (via University of York) (R1500502)
pubs.funder-project-idBiotechnology and Biological Sciences Research Council (BB/L000423/1)
rioxxterms.licenseref.startdate2015-01-22
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.typeJournal Article/Review
rioxxterms.versionofrecord10.1038/ncomms6961

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