• 1H, 13C, 15N resonance assignment of the apo form of the small, chitin-active lytic polysaccharide monooxygenase JdLPMO10A from Jonesia denitrificans 

      Christensen, Idd Andrea; Eijsink, Vincent; Aachmann, Finn Lillelund; Courtade, Gaston (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-11-19)
      The lytic polysaccharide monooxygenase <i>Jd</i>LPMO10A is the N-terminal domain of the multimodular protein Jd1381. The isolated <i>Jd</i>LPMO10A domain is one of the smallest chitin-active lytic polysaccharide monooxygenases known to date with a size of only 15.5 kDa. <i>Jd</i>LPMO10A is a copper-dependent oxidative enzyme that depolymerizes chitin by hydroxylating the C1 carbon in the glycosidic ...
    • 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 (Journal article; Tidsskriftartikkel; Peer reviewed, 2021-08-17)
      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 cleavage of glycosidic bonds in polysaccharides such as cellulose and chitin. Several LPMOs contain carbohydrate-binding modules (CBMs) that are known to promote LPMO efficiency. ...