Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Zarah Forsberg"'
Autor:
Kelsi R. Hall, Maja Mollatt, Zarah Forsberg, Ole Golten, Lorenz Schwaiger, Roland Ludwig, Iván Ayuso-Fernández, Vincent G. H. Eijsink, Morten Sørlie
Publikováno v:
ACS Omega, Vol 9, Iss 21, Pp 23040-23052 (2024)
Externí odkaz:
https://doaj.org/article/85ba9c9b01274892bd286e2702b778f7
Autor:
Amanda K. Votvik, Åsmund K. Røhr, Bastien Bissaro, Anton A. Stepnov, Morten Sørlie, Vincent G. H. Eijsink, Zarah Forsberg
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-18 (2023)
Abstract Bacterial lytic polysaccharide monooxygenases (LPMOs) are known to oxidize the most abundant and recalcitrant polymers in Nature, namely cellulose and chitin. The genome of the model actinomycete Streptomyces coelicolor A3(2) encodes seven p
Externí odkaz:
https://doaj.org/article/01c3173525704e17b6f55c8848450f00
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-11 (2022)
Abstract Lytic polysaccharide monooxygenases (LPMOs) are mono-copper enzymes that catalyze oxidative depolymerization of recalcitrant substrates such as chitin or cellulose. Recent work has shown that LPMOs catalyze fast peroxygenase reactions and th
Externí odkaz:
https://doaj.org/article/bb79a607f496457c9f32944aaf831e3c
Autor:
Anton A. Stepnov, Zarah Forsberg, Morten Sørlie, Giang-Son Nguyen, Alexander Wentzel, Åsmund K. Røhr, Vincent G. H. Eijsink
Publikováno v:
Biotechnology for Biofuels, Vol 14, Iss 1, Pp 1-14 (2021)
Abstract Background Lytic polysaccharide monooxygenases (LPMOs) are monocopper enzymes that catalyze oxidative depolymerization of industrially relevant crystalline polysaccharides, such as cellulose, in a reaction that depends on an electron donor a
Externí odkaz:
https://doaj.org/article/8a245d9e279d49e2b6af102a59d2f131
Autor:
Tina Rise Tuveng, Marianne Slang Jensen, Lasse Fredriksen, Gustav Vaaje-Kolstad, Vincent G. H. Eijsink, Zarah Forsberg
Publikováno v:
Biotechnology for Biofuels, Vol 13, Iss 1, Pp 1-15 (2020)
Abstract Background Lytic polysaccharide monooxygenases (LPMOs) are oxidative, copper-dependent enzymes that function as powerful tools in the turnover of various biomasses, including lignocellulosic plant biomass. While LPMOs are considered to be of
Externí odkaz:
https://doaj.org/article/f2aac97534184c91895e7a7424bc5229
Autor:
Vincent G. H. Eijsink, Dejan Petrovic, Zarah Forsberg, Sophanit Mekasha, Åsmund K. Røhr, Anikó Várnai, Bastien Bissaro, Gustav Vaaje-Kolstad
Publikováno v:
Biotechnology for Biofuels, Vol 12, Iss 1, Pp 1-16 (2019)
Abstract Lytic polysaccharide monooxygenases (LPMOs) are abundant in nature and best known for their role in the enzymatic conversion of recalcitrant polysaccharides such as chitin and cellulose. LPMO activity requires an oxygen co-substrate, which w
Externí odkaz:
https://doaj.org/article/1ee975783e4b4065927ab3ccc93b821a
Autor:
Zarah Forsberg, Gaston Courtade
Publikováno v:
Essays in Biochemistry
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 the catalytic LPMO domains, t
Publikováno v:
ChemBioChem.
Autor:
Cristina M. Cordas, Gabriel N. Valério, Anton Stepnov, Eirik Kommedal, Åsmund R. Kjendseth, Zarah Forsberg, Vincent G.H. Eijsink, José J.G. Moura
Publikováno v:
Journal of inorganic biochemistry. 238
Research on enzymes for lignocellulose biomass degradation has progressively increased in recent years due to the interest in taking advantage of this natural resource. Among these enzymes are the lytic polysaccharide monooxygenases (LPMOs) that oxid
Autor:
Alessandro Paradisi, Finn Lillelund Aachmann, Gaston Courtade, Zarah Forsberg, Gideon J. Davies, Peter J. Lindley, Reinhard Wimmer, Luisa Ciano, Paul H. Walton, Vincent G. H. Eijsink, Morten Sørlie
Publikováno v:
Proceedings of the National Academy of Sciences
Courtade, G, Ciano, L, Paradisi, A, Lindley, P J, Forsberg, Z, Sørlie, M, Wimmer, R, Davies, G J, Eijsink, V G H, Walton, P H & Aachmann, F L 2020, ' Mechanistic basis of substrate-O 2 coupling within a chitin-active lytic polysaccharide monooxygenase : An integrated NMR/EPR study ', Proceedings of the National Academy of Sciences of the United States of America, vol. 117, no. 32, pp. 19178-19189 . https://doi.org/10.1073/pnas.2004277117
Proceedings of the National Academy of Sciences of the United States of America
Courtade, G, Ciano, L, Paradisi, A, Lindley, P J, Forsberg, Z, Sørlie, M, Wimmer, R, Davies, G J, Eijsink, V G H, Walton, P H & Aachmann, F L 2020, ' Mechanistic basis of substrate-O 2 coupling within a chitin-active lytic polysaccharide monooxygenase : An integrated NMR/EPR study ', Proceedings of the National Academy of Sciences of the United States of America, vol. 117, no. 32, pp. 19178-19189 . https://doi.org/10.1073/pnas.2004277117
Proceedings of the National Academy of Sciences of the United States of America
Significance Lytic polysaccharide monooxygenases (LPMOs) have unique catalytic centers, at which a single copper catalyzes the oxidative cleavage of a glycosidic bond. The mechanism by which LPMOs activate molecular oxygen is key to understanding cop