Zobrazeno 1 - 10
of 38
pro vyhledávání: '"Uwe T. Bornscheuer"'
Publikováno v:
Biochemical Journal
The biochemical journal / Reviews 475(23), 3875-3886 (2018). doi:10.1042/BCJ20180762
The biochemical journal / Reviews 475(23), 3875-3886 (2018). doi:10.1042/BCJ20180762
The biochemical journal / Reviews 475(23), 3875 - 3886 (2018). doi:10.1042/BCJ20180762
Degradation of carbohydrates by bacteria represents a key step in energy metabolism that can be inhibited by methylated sugars. Removal of methyl groups, whic
Degradation of carbohydrates by bacteria represents a key step in energy metabolism that can be inhibited by methylated sugars. Removal of methyl groups, whic
Publikováno v:
Advanced Synthesis & Catalysis
Biotechnological strategies using renewable materials as starting substrates are a promising alternative to traditional oleochemical processes for the isolation of different fatty acids. Among them, long chain monounsaturated fatty acids are especial
Autor:
Lenka Hernychová, Zbynek Prokop, Mark Dörr, David Bednar, Andrea Schenkmayerova, Jiri Damborsky, Radka Chaloupková, Stéphane Emond, Daniel Pluskal, Uwe T. Bornscheuer, Veronika Liskova, Michal Vasina, Joan Planas-Iglesias, Martin Toul, Florian Hollfelder, Gaspar Pinto, Martin Marek
Publikováno v:
Nature Communications
'Nature Communications ', vol: 12, pages: 3616-1-3616-16 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
'Nature Communications ', vol: 12, pages: 3616-1-3616-16 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
Protein dynamics are often invoked in explanations of enzyme catalysis, but their design has proven elusive. Here we track the role of dynamics in evolution, starting from the evolvable and thermostable ancestral protein AncHLD-RLuc which catalyses b
Autor:
Isabelle André, Uwe T. Bornscheuer, Matthias Höhne, Moritz Voss, Marian J Menke, Alberto Nobili, Chao Xiang, Jérémy Esque
Publikováno v:
ACS Chemical Biology
ACS Chemical Biology, American Chemical Society, 2020, 15 (2), pp.416-424. ⟨10.1021/acschembio.9b00888⟩
ACS Chemical Biology, 2020, 15 (2), pp.416-424. ⟨10.1021/acschembio.9b00888⟩
ACS Chemical Biology, American Chemical Society, 2020, 15 (2), pp.416-424. ⟨10.1021/acschembio.9b00888⟩
ACS Chemical Biology, 2020, 15 (2), pp.416-424. ⟨10.1021/acschembio.9b00888⟩
International audience; The enzymatic transamination of ketones into (R)-amines represents an important route for accessing a range of pharmaceuticals or building blocks. Although many publications have dealt with enzyme discovery, protein engineerin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d232ba5bfaf0055d0e52ad4c430e679f
https://hal.inrae.fr/hal-02529029/file/acschembio.9b00888_HAL.pdf
https://hal.inrae.fr/hal-02529029/file/acschembio.9b00888_HAL.pdf
Autor:
Dominique Böttcher, Uwe T. Bornscheuer, Kathleen Balke, Lisa K. Morlock, Sascha Grobe, Stephan Mauersberger
Publikováno v:
ChemBioChem. 19:1954-1958
The CYP171 enzyme is known to catalyse a key step in the steroidogenesis of mammals. The substrates progesterone and pregnenolone are first hydroxylated at the C17 position, and this is followed by cleavage of the C17-C20 bond to yield important prec
Autor:
Christian Stanetty, Lukas Reisky, Marko D. Mihovilovic, Uwe T. Bornscheuer, Jan-Hendrik Hehemann, Thomas Schweder
Publikováno v:
Applied Microbiology and Biotechnology. 102:6987-6996
Carbohydrates are the product of carbon dioxide fixation by algae in the ocean. Their polysaccharides are depolymerized by marine bacteria, with a vast array of carbohydrate-active enzymes. These enzymes are important tools to establish biotechnologi
Autor:
Vishnu S. T. Srinivasamurthy, Uwe T. Bornscheuer, Anna Kohl, Dominique Böttcher, Johannes Kabisch
Publikováno v:
Enzyme and Microbial Technology. 108:53-58
The introduction of a three-enzyme cascade (comprising a cyclohexanone monooxygenase (CHMO), an alcohol dehydrogenase (ADH) and a lipase (CAL-A)) for the production of oligo-ε-caprolactone provided self-sufficiency with respect to NADPH-cofactor reg
Publikováno v:
Applied Microbiology and Biotechnology. 102:985-994
Cytochrome P450s belong to a large and diverse group of heme-containing enzymes. These monooxygenases catalyze the incorporation of a single atom of molecular oxygen into their substrate. In contrast to most other enzymes, the activity of P450 enzyme
Autor:
Martin Giersberg, Annett Mikolasch, Ann-Kristin Henning, Rabea Schlüter, Michael Lalk, Gotthard Kunze, Heidi Frenzel, Henning Schindler, Elke Hammer, Marie-Katherin Zühlke, Katharina Riedel, Frieder Schauer, Daniela Zühlke, Uwe T. Bornscheuer
Publikováno v:
Applied Microbiology and Biotechnology. 101:3743-3758
The biphenyl-degrading Gram-negative bacterium Cupriavidus basilensis (formerly Ralstonia sp.) SBUG 290 uses various aromatic compounds as carbon and energy sources and has a high capacity to transform bisphenol A (BPA), which is a hormonally active
Autor:
Anibal Cuetos, Juan Mangas Sanchez, Matthias Höhne, Gideon Grogan, Uwe T. Bornscheuer, Fabian Steffen-Munsberg, Amina Frese
Publikováno v:
ChemBioChem. 17:2308-2311
Pyridoxal-phosphate (PLP)-dependent enzymes catalyse a remarkable diversity of chemical reactions in nature. A1RDF1 from Arthrobacter aurescens TC1 is a fold type I, PLP-dependent enzyme in the class III transaminase (TA) subgroup. Despite sharing 28