Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Idd A. Christensen"'
Autor:
Heidi Østby, Idd A. Christensen, Karen Hennum, Anikó Várnai, Edith Buchinger, Siri Grandal, Gaston Courtade, Olav A. Hegnar, Finn L. Aachmann, Vincent G. H. Eijsink
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-18 (2023)
Abstract Lytic polysaccharide monooxygenases (LPMOs) are mono-copper enzymes that use O2 or H2O2 to oxidatively cleave glycosidic bonds. LPMOs are prevalent in nature, and the functional variation among these enzymes is a topic of great interest. We
Externí odkaz:
https://doaj.org/article/3b50424632b4425e80bcf0b002ffb232
Autor:
Idd A. Christensen, Vincent G. H. Eijsink, Anton A. Stepnov, Gaston Courtade, Finn L. Aachmann
Publikováno v:
Biochemistry.
Autor:
Idd A. Christensen, Vincent G. H. Eijsink, Anton A. Stepnov, Gaston Courtade, Finn L. Aachmann
Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze oxidative cleavage of polysaccharides, such as cellulose and chitin. LPMO action is key to the efficient varlorization of biomass, but the instability of LPMOs in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ddae19f85f5887dfdac40124f20d0adb
https://doi.org/10.1101/2023.02.02.526831
https://doi.org/10.1101/2023.02.02.526831
Autor:
Agnes Beenfeldt Petersen, Idd Andrea Christensen, Mette E. Rønne, Emil G. P. Stender, David Teze, Birte Svensson, Finn Lillelund Aachmann
Publikováno v:
Petersen, A B, Christensen, I A, Rønne, M E, Stender, E G P, Teze, D, Svensson, B & Aachmann, F L 2022, ' 1 H, 13 C, 15 N resonance assignment of the enzyme KdgF from Bacteroides eggerthii ', Biomolecular N M R Assignments, vol. 16, pp. 343-347 . https://doi.org/10.1007/s12104-022-10102-6
To fully utilize carbohydrates from seaweed biomass, the degradation of the family of polysaccharides known as alginates must be understood. A step in the degradation of alginate is the conversion of 4,5-unsaturated monouronates to 4-deoxy-L-erythro-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3790f74cf10e156b171d10e93275c8b
https://orbit.dtu.dk/en/publications/e4bbb3b6-3518-4cd5-b50a-dcebd1fb6cef
https://orbit.dtu.dk/en/publications/e4bbb3b6-3518-4cd5-b50a-dcebd1fb6cef
Autor:
Zarah Forsberg, Anton A. Stepnov, Vincent G. H. Eijsink, Idd Andrea Christensen, Finn Lillelund Aachmann, Gaston Courtade
Publikováno v:
FEBS lettersReferences. 596(1)
Monocopper lytic polysaccharide monooxygenases (LPMOs) catalyze oxidative cleavage of glycosidic bonds in a reductant-dependent reaction. Recent studies indicate that LPMOs, rather than being O2 -dependent monooxygenases, are H2 O2 -dependent peroxyg
The lytic polysaccharide monooxygenase JdLPMO10A is the N-terminal domain of the multimodular protein Jd1381. The isolated JdLPMO10A domain is one of the smallest chitin-active lytic polysaccharide monooxygenases known to date with a size of only 15.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a58de4b7c44f2468150b353164039227
https://hdl.handle.net/10037/20482
https://hdl.handle.net/10037/20482