Zobrazeno 1 - 10
of 71
pro vyhledávání: '"Active site geometry"'
Autor:
Tobias Tandrup, Sebastian J. Muderspach, Sanchari Banerjee, Gianluca Santoni, Johan Ø. Ipsen, Cristina Hernández-Rollán, Morten H. H. Nørholm, Katja S. Johansen, Flora Meilleur, Leila Lo Leggio
Publikováno v:
IUCrJ, Vol 9, Iss 5, Pp 666-681 (2022)
The recently discovered lytic polysaccharide monooxygenases (LPMOs) are Cu-containing enzymes capable of degrading polysaccharide substrates oxidatively. The generally accepted first step in the LPMO reaction is the reduction of the active-site metal
Externí odkaz:
https://doaj.org/article/f55e8c4da97646a8aef9109ae3ae787c
Publikováno v:
In Analytical Biochemistry 15 August 2022 651
Autor:
Pérez-Amigot, Daniel a, b, 1, Taleb, Víctor a, b, 1, Boneta, Sergio b, c, Anoz-Carbonell, Ernesto a, b, Sebastián, María a, b, Velázquez-Campoy, Adrián a, b, d, e, f, Polo, Víctor b, c, Martínez-Júlvez, Marta a, b, ⁎, Medina, Milagros a, b, ⁎
Publikováno v:
In BBA - Bioenergetics 1 October 2019 1860(10)
Autor:
Tandrup, Tobias, Muderspach, Sebastian J., Banerjee, Sanchari, Santoni, Gianluca, Ipsen, Johan, Hernández-Rollán, Cristina, Nørholm, Morten H.H., Johansen, Katja S., Meilleur, Flora, Lo Leggio, Leila, Moffat, K.
Publikováno v:
Tandrup, T, Muderspach, S J, Banerjee, S, Santoni, G, Ipsen, J, Hernández-Rollán, C, Nørholm, M H H, Johansen, K S, Meilleur, F, Lo Leggio, L & Moffat, K 2022, ' Changes in active-site geometry on X-ray photoreduction of a lytic polysaccharide monooxygenase active-site copper and saccharide binding ', IUCrJ, vol. 9, pp. 666-681 . https://doi.org/10.1107/S2052252522007175
Tandrup, T, Muderspach, S J, Banerjee, S, Santoni, G, Ipsen, J O, Hernandez-Rollan, C, Norholm, M H H, Johansen, K S, Meilleur, F & Lo Leggio, L 2022, ' Changes in active-site geometry on X-ray photo-reduction of a lytic polysaccharide monooxygenase active-site copper and saccharide binding ', IUCrJ, vol. 9, no. 5, pp. 666-681 . https://doi.org/10.1107/S2052252522007175
IUCrJ 9(5), 666-681 (2022). doi:10.1107/S2052252522007175
Tandrup, T, Muderspach, S J, Banerjee, S, Santoni, G, Ipsen, J O, Hernandez-Rollan, C, Norholm, M H H, Johansen, K S, Meilleur, F & Lo Leggio, L 2022, ' Changes in active-site geometry on X-ray photo-reduction of a lytic polysaccharide monooxygenase active-site copper and saccharide binding ', IUCrJ, vol. 9, no. 5, pp. 666-681 . https://doi.org/10.1107/S2052252522007175
IUCrJ 9(5), 666-681 (2022). doi:10.1107/S2052252522007175
IUCrJ 9(5), 666 - 681 (2022). doi:10.1107/S2052252522007175
The recently discovered lytic polysaccharide monooxygenases (LPMOs) are Cu-containing enzymes capable of degrading polysaccharide substrates oxidatively. The generally accepted first st
The recently discovered lytic polysaccharide monooxygenases (LPMOs) are Cu-containing enzymes capable of degrading polysaccharide substrates oxidatively. The generally accepted first st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fafde217601c6b6be7a1cab2d68bf345
https://pubmed.ncbi.nlm.nih.gov/36071795
https://pubmed.ncbi.nlm.nih.gov/36071795
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 1986 Dec . 83(24), 9383-9387.
Externí odkaz:
https://www.jstor.org/stable/28625
Autor:
Siddhartha Kundu
Publikováno v:
Journal of Molecular Modeling
Biofuels such as γ-valerolactone, bioethanol, and biodiesel are derived from potentially fermentable cellulose and vegetable oils. Plant class C GH9 endoglucanases are CBM49-encompassing hydrolases that cleave the β (1 → 4) glycosidic linkage of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4798e0ac1832d97aedcd400ababe33e
https://doi.org/10.1007/s00894-020-04465-7
https://doi.org/10.1007/s00894-020-04465-7
Autor:
Sergio Boneta, Victor Polo, Daniel Pérez-Amigot, Víctor Taleb, Adrián Velázquez-Campoy, Ernesto Anoz-Carbonell, Marta Martínez-Júlvez, María Victoria Sebastián, Milagros Medina
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
12 pags., 6 figs.
Brucella ovis encodes a bacterial subclass 1 ferredoxin-NADP(H) reductase (BoFPR) that, by similarity with other FPRs, is expected either to deliver electrons from NADPH to the redox-based metabolism and/or to oxidize NADPH to
Brucella ovis encodes a bacterial subclass 1 ferredoxin-NADP(H) reductase (BoFPR) that, by similarity with other FPRs, is expected either to deliver electrons from NADPH to the redox-based metabolism and/or to oxidize NADPH to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04d7161b32672627ae00cf0ec17cd9f9
https://doi.org/10.1016/j.bbabio.2019.148058
https://doi.org/10.1016/j.bbabio.2019.148058
Autor:
Hudeček, Jiří a, 2, Anzenbacherová, Eva b, Anzenbacher, Pavel b, Munro, Andrew W. c, Hildebrandt, Peter d
Publikováno v:
In Archives of Biochemistry and Biophysics 1 November 2000 383(1):70-78
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Autor:
Soma Addya, Surajit Debnath
Publikováno v:
SpringerPlus
Correlating antifungal Azole drug resistance and mis-sense mutations of ERG11 has been paradoxical in pathogenic yeast Candida albicans. Amino acid substitutions (single or multiple) are frequent on ERG11, a membrane bound enzyme of Ergosterol biosyn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::460aaf84468b50d7fdd6aa5f3f92fd23
https://doi.org/10.1186/2193-1801-3-660
https://doi.org/10.1186/2193-1801-3-660