Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Anton A. Stepnov"'
Autor:
Anton A. Stepnov, Esteban Lopez-Tavera, Ross Klauer, Clarissa L. Lincoln, Ravindra R. Chowreddy, Gregg T. Beckham, Vincent G. H. Eijsink, Kevin Solomon, Mark Blenner, Gustav Vaaje-Kolstad
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-15 (2024)
Abstract Biocatalytic degradation of non-hydrolyzable plastics is a rapidly growing field of research, driven by the global accumulation of waste. Enzymes capable of cleaving the carbon-carbon bonds in synthetic polymers are highly sought-after as th
Externí odkaz:
https://doaj.org/article/4fac7be2349d4d5caf23eb63391071b2
Autor:
Iván Ayuso-Fernández, Tom Z. Emrich-Mills, Julia Haak, Ole Golten, Kelsi R. Hall, Lorenz Schwaiger, Trond S. Moe, Anton A. Stepnov, Roland Ludwig, George E. Cutsail III, Morten Sørlie, Åsmund Kjendseth Røhr, Vincent G. H. Eijsink
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-15 (2024)
Abstract Oxidoreductases have evolved tyrosine/tryptophan pathways that channel highly oxidizing holes away from the active site to avoid damage. Here we dissect such a pathway in a bacterial LPMO, member of a widespread family of C-H bond activating
Externí odkaz:
https://doaj.org/article/af35a6ac3afc4cd6b8384d682064752a
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:
Ole Golten, Iván Ayuso‐Fernández, Kelsi R. Hall, Anton A. Stepnov, Morten Sørlie, Åsmund Kjendseth Røhr, Vincent G. H. Eijsink
Publikováno v:
FEBS Letters. 597:1363-1374
Publikováno v:
PLoS ONE, Vol 14, Iss 9, p e0222216 (2019)
A novel GH9 cellulase (AMOR_GH9A) was discovered by sequence-based mining of a unique metagenomic dataset collected at the Jan Mayen hydrothermal vent field. AMOR_GH9A comprises a signal peptide, a catalytic domain and a CBM3 cellulose-binding module
Externí odkaz:
https://doaj.org/article/8c07677ca1f6436582009622431a3f7b
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:
Anton A. Stepnov, Vincent G.H. Eijsink
Publikováno v:
Integrated Methods in Protein Biochemistry: Part B ISBN: 9780323992640
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::365f0407bb5a123d212d214f3f1d1ebf
https://doi.org/10.1016/bs.mie.2022.08.049
https://doi.org/10.1016/bs.mie.2022.08.049