Literatura científica selecionada sobre o tema "Type II Baeyer-Villiger monooxygenase"
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Artigos de revistas sobre o assunto "Type II Baeyer-Villiger monooxygenase"
Isupov, Michail N., Ewald Schröder, Robert P. Gibson, Jean Beecher, Giuliana Donadio, Vahid Saneei, Stephlina A. Dcunha et al. "The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid ofPseudomonas putida: the first crystal structure of a type II Baeyer–Villiger monooxygenase". Acta Crystallographica Section D Biological Crystallography 71, n.º 11 (31 de outubro de 2015): 2344–53. http://dx.doi.org/10.1107/s1399004715017939.
Texto completo da fonteIsupov, Michail N., Ewald Schröder, Robert P. Gibson, Jean Beecher, Giuliana Donadio, Vahid Saneei, Stephlina A. Dcunha et al. "The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid ofPseudomonas putida: the first crystal structure of a type II Baeyer–Villiger monooxygenase. Corrigendum". Acta Crystallographica Section D Structural Biology 74, n.º 4 (1 de abril de 2018): 379. http://dx.doi.org/10.1107/s205979831800150x.
Texto completo da fonteLöwe, Jana, Olga Blifernez-Klassen, Thomas Baier, Lutz Wobbe, Olaf Kruse e Harald Gröger. "Type II flavoprotein monooxygenase PsFMO_A from the bacterium Pimelobacter sp. Bb-B catalyzes enantioselective Baeyer-Villiger oxidations with a relaxed cofactor specificity". Journal of Biotechnology 294 (março de 2019): 81–87. http://dx.doi.org/10.1016/j.jbiotec.2019.01.011.
Texto completo da fonteRiebel, Anette, Michael J. Fink, Marko D. Mihovilovic e Marco W. Fraaije. "Type II Flavin-Containing Monooxygenases: A New Class of Biocatalysts that Harbors Baeyer-Villiger Monooxygenases with a Relaxed Coenzyme Specificity". ChemCatChem 6, n.º 4 (7 de outubro de 2013): 1112–17. http://dx.doi.org/10.1002/cctc.201300550.
Texto completo da fonteTanner, Adam, e David J. Hopper. "Conversion of 4-Hydroxyacetophenone into 4-Phenyl Acetate by a Flavin Adenine Dinucleotide-Containing Baeyer-Villiger-Type Monooxygenase". Journal of Bacteriology 182, n.º 23 (1 de dezembro de 2000): 6565–69. http://dx.doi.org/10.1128/jb.182.23.6565-6569.2000.
Texto completo da fonteNiero, Mattia, Irene Righetto, Elisa Beneventi, Patrizia Polverino de Laureto, Marco Wilhelmus Fraaije, Francesco Filippini e Elisabetta Bergantino. "Unique Features of a New Baeyer–Villiger Monooxygenase from a Halophilic Archaeon". Catalysts 10, n.º 1 (16 de janeiro de 2020): 128. http://dx.doi.org/10.3390/catal10010128.
Texto completo da fonteIwaki, Hiroaki, Yoshie Hasegawa, Shaozhao Wang, Margaret M. Kayser e Peter C. K. Lau. "Cloning and Characterization of a Gene Cluster Involved in Cyclopentanol Metabolism in Comamonas sp. Strain NCIMB 9872 and Biotransformations Effected by Escherichia coli-Expressed Cyclopentanone 1,2-Monooxygenase". Applied and Environmental Microbiology 68, n.º 11 (novembro de 2002): 5671–84. http://dx.doi.org/10.1128/aem.68.11.5671-5684.2002.
Texto completo da fonteKostichka, Kristy, Stuart M. Thomas, Katharine J. Gibson, Vasantha Nagarajan e Qiong Cheng. "Cloning and Characterization of a Gene Cluster for Cyclododecanone Oxidation in Rhodococcus ruber SC1". Journal of Bacteriology 183, n.º 21 (1 de novembro de 2001): 6478–86. http://dx.doi.org/10.1128/jb.183.21.6478-6486.2001.
Texto completo da fonteIwaki, Hiroaki, Shaozhao Wang, Stephan Grosse, Hélène Bergeron, Ayako Nagahashi, Jittiwud Lertvorachon, Jianzhong Yang, Yasuo Konishi, Yoshie Hasegawa e Peter C. K. Lau. "Pseudomonad Cyclopentadecanone Monooxygenase Displaying an Uncommon Spectrum of Baeyer-Villiger Oxidations of Cyclic Ketones". Applied and Environmental Microbiology 72, n.º 4 (abril de 2006): 2707–20. http://dx.doi.org/10.1128/aem.72.4.2707-2720.2006.
Texto completo da fonteTolmie, Carmien, Martha Smit e Diederik Opperman. "Alternative Splicing of the Aflatoxin-Associated Baeyer–Villiger Monooxygenase from Aspergillus flavus: Characterisation of MoxY Isoforms". Toxins 10, n.º 12 (5 de dezembro de 2018): 521. http://dx.doi.org/10.3390/toxins10120521.
Texto completo da fonteTeses / dissertações sobre o assunto "Type II Baeyer-Villiger monooxygenase"
Downey, Theresa E. "INVESTIGATING STRUCTURE AND PROTEIN-PROTEIN INTERACTIONS OF KEY POST-TYPE II PKS TAILORING ENZYMES". UKnowledge, 2014. http://uknowledge.uky.edu/pharmacy_etds/35.
Texto completo da fonteRöllig, Robert. "Chemical hydride transfer for flavin dependent monooxygenases of two-component systems". Electronic Thesis or Diss., Aix-Marseille, 2021. http://www.theses.fr/2021AIXM0436.
Texto completo da fonteThe term flavoprotein monooxygenases (FPMO) covers two different types of flavoenzymes: single and two component oxygenases. Two component FPMOs consist of a reductase and an oxygenating enzyme. The functional independence of the oxygenase part of 2,5-diketocamphane 1,2-monooxygenase I (2,5 DKCMO), an FMN dependent type II Baeyer-Villiger monooxygenase, from the reductase counterpart, as well as the mechanism of flavin transfer by free diffusion, was investigated in a reductase-free reaction, using synthetic nicotinamide biomimetics (NCBs) for the reduction of FMN. The balance of flavin reduction and enzymatic (re)oxidation was identified as the bottleneck of the system. Aiming for potentially cost efficient hydride donors for enzymatic redox reactions, nicotinamide coenzyme and nicotinamide biomimetic independent flavin reduction strategies were investigated. The capability of the pH and oxygen robust iridium III complex [Cp*Ir(bpy-OMe)H]+ (Ir* (H+)) to transfer hydrides for flavin reduction for the enzymatic reaction of respectively FMNH2 and FADH2 dependent monooxygenases, 2,5 DKCMO and styrene monooxygenase from Sphingopyxis fribergensis Kp.5.2 (SfStyA) was exploited. The Ir* (H+)/SfStyA approach outperformed the state of the art system by six-fold in terms of turn over number of the metal catalyst. Nevertheless, the robustness of the system remains challenging, and improvements are required to establish the approach as an efficient and versatile platform technology for flavoenzymes