Blar i NTNU Open på forfatter "Forsberg, Zarah"
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1H, 13C, 15N resonance assignment of the chitin-active lytic polysaccharide monooxygenase BlLPMO10A from Bacillus licheniformis
Courtade, Gaston; Balzer, Simone; Forsberg, Zarah; Vaaje-Kolstad, Gustav; Eijsink, Vincent; Aachmann, Finn Lillelund (Journal article; Peer reviewed, 2015)The chitin-active 19.2 kDa lytic polysaccharide monooxygenase BlLPMO10A from Bacillus licheniformis has been isotopically labeled and recombinantly expressed. In this paper, we report the 1H, 13C, 15N resonance assignment ... -
Chemical shift assignments for the apo-form of the catalytic domain, the linker region, and the carbohydrate-binding domain of the cellulose-active lytic polysaccharide monooxygenase ScLPMO10C
Courtade, Gaston; Forsberg, Zarah; Vaaje-Kolstad, Gustav; Eijsink, Vincentius Gerardus Henricus; Aachmann, Finn Lillelund (Journal article; Peer reviewed, 2017)The apo-form of the 21.4 kDa catalytic domain and the 10.7 kDa carbohydrate binding domain of the AA10 family lytic polysaccharide monooxygenase ScLPMO10C from Streptomyces coelicolor have been isotopically labeled and ... -
The effect of linker conformation on performance and stability of a two-domain lytic polysaccharide monooxygenase
Forsberg, Zarah; Stepnov, Anton; Tesei, Giulio; Wang, Yong; Buchinger, Edith; Kristiansen, Sandra; Aachmann, Finn Lillelund; Arleth, Lise; Eijsink, Vincent; Lindorff-Larsen, Kresten; Courtade, Gaston (Journal article; Peer reviewed, 2023)A considerable number of lytic polysaccharide monooxygenases (LPMOs) and other carbohydrate-active enzymes are modular, with catalytic domains being tethered to additional domains, such as carbohydrate-binding modules, by ... -
Mechanistic basis of substrate–O2 coupling within a chitin-active lytic polysaccharide monooxygenase: An integrated NMR/EPR study
Courtade, Gaston; Ciano, Luisa; Paradisi, Alessandro; Lindley, Peter J.; Forsberg, Zarah; Sørlie, Morten; Wimmer, Reinhard; Davies, Gideon J.; Eijsink, Vincent; Walton, Paul H.; Aachmann, Finn Lillelund (Peer reviewed; Journal article, 2020)Lytic polysaccharide monooxygenases (LPMOs) have a unique ability to activate molecular oxygen for subsequent oxidative cleavage of glycosidic bonds. To provide insight into the mode of action of these industrially important ... -
On the impact of carbohydrate-binding modules (CBMs) in lytic polysaccharide monooxygenases (LPMOs)
Forsberg, Zarah; Courtade, Gaston (Peer reviewed; Journal article, 2022)Lytic 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 ... -
Polysaccharide degradation by lytic polysaccharide monooxygenases
Forsberg, Zarah; Sørlie, Morten; Petrovic, Dejan; Courtade, Gaston; Aachmann, Finn Lillelund; Vaaje-Kolstad, Gustav; Bissaro, Bastien; Kjendseth, Åsmund Røhr; Eijsink, Vincent (Journal article; Peer reviewed, 2019)The discovery of oxidative cleavage of glycosidic bonds by enzymes currently known as lytic polysaccharide monooxygenases (LPMOs) has had a major impact on our current understanding of the enzymatic conversion of recalcitrant ... -
Structural and functional variation of chitin-binding domains of a lytic polysaccharide monooxygenase from Cellvibrio japonicus
Madland, Eva; Forsberg, Zarah; Wang, Yong; Lindorff-Larsen, Kresten; Niebisch, Axel; Modregger, Jan; Eijsink, Vincent; Aachmann, Finn Lillelund; Courtade, Gaston (Peer reviewed; Journal article, 2021)Among the extensive repertoire of carbohydrate-active enzymes, lytic polysaccharide monooxygenases (LPMOs) have a key role in recalcitrant biomass degradation. LPMOs are copper-dependent enzymes that catalyze oxidative ... -
The carbohydrate-binding module and linker of a modular lytic polysaccharide monooxygenase promote localized cellulose oxidation
Courtade, Gaston; Forsberg, Zarah; Heggset, Ellinor Bævre; Eijsink, Vincent; Aachmann, Finn Lillelund (Journal article; Peer reviewed, 2018)Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze the oxidative cleavage of polysaccharides such as cellulose and chitin, a feature that makes them key tools in industrial biomass ...