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dc.contributor.authorForsberg, Zarah
dc.contributor.authorCourtade, Gaston
dc.date.accessioned2023-03-10T13:28:52Z
dc.date.available2023-03-10T13:28:52Z
dc.date.created2023-01-17T07:50:23Z
dc.date.issued2022
dc.identifier.citationEssays in Biochemistry. 2022, .en_US
dc.identifier.issn0071-1365
dc.identifier.urihttps://hdl.handle.net/11250/3057746
dc.description.abstractLytic polysaccharide monooxygenases (LPMOs) have revolutionized our understanding of how enzymes degrade insoluble polysaccharides. Compared with the substantial knowledge developed on the structure and mode of action of the catalytic LPMO domains, the (multi)modularity of LPMOs has received less attention. The presence of other domains, in particular carbohydrate-binding modules (CBMs), tethered to LPMOs has profound implications for the catalytic performance of the full-length enzymes. In the last few years, studies on LPMO modularity have led to advancements in elucidating how CBMs, other domains, and linker regions influence LPMO structure and function. This mini review summarizes recent literature, with particular focus on comparative truncation studies, to provide an overview of the diversity in LPMO modularity and the functional implications of this diversity.en_US
dc.language.isoengen_US
dc.publisherPortland Pressen_US
dc.rightsNavngivelse 4.0 Internasjonal*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/deed.no*
dc.titleOn the impact of carbohydrate-binding modules (CBMs) in lytic polysaccharide monooxygenases (LPMOs)en_US
dc.title.alternativeOn the impact of carbohydrate-binding modules (CBMs) in lytic polysaccharide monooxygenases (LPMOs)en_US
dc.typePeer revieweden_US
dc.typeJournal articleen_US
dc.description.versionpublishedVersionen_US
dc.source.pagenumber14en_US
dc.source.journalEssays in Biochemistryen_US
dc.identifier.doi10.1042/EBC20220162
dc.identifier.cristin2108212
dc.relation.projectNovo Nordisk Fonden: NNF-0055736en_US
dc.relation.projectNovo Nordisk Fonden: 0032242en_US
dc.relation.projectNovo Nordisk Fonden: NNF-0032242en_US
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode1


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