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Статті в журналах з теми "Baeyer-Villiger monooxygenase de type II"
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, no. 11 (October 31, 2015): 2344–53. http://dx.doi.org/10.1107/s1399004715017939.
Повний текст джерелаIsupov, 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, no. 4 (April 1, 2018): 379. http://dx.doi.org/10.1107/s205979831800150x.
Повний текст джерелаLöwe, Jana, Olga Blifernez-Klassen, Thomas Baier, Lutz Wobbe, Olaf Kruse, and 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 (March 2019): 81–87. http://dx.doi.org/10.1016/j.jbiotec.2019.01.011.
Повний текст джерелаRiebel, Anette, Michael J. Fink, Marko D. Mihovilovic, and 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, no. 4 (October 7, 2013): 1112–17. http://dx.doi.org/10.1002/cctc.201300550.
Повний текст джерелаTanner, Adam, and 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, no. 23 (December 1, 2000): 6565–69. http://dx.doi.org/10.1128/jb.182.23.6565-6569.2000.
Повний текст джерелаNiero, Mattia, Irene Righetto, Elisa Beneventi, Patrizia Polverino de Laureto, Marco Wilhelmus Fraaije, Francesco Filippini, and Elisabetta Bergantino. "Unique Features of a New Baeyer–Villiger Monooxygenase from a Halophilic Archaeon." Catalysts 10, no. 1 (January 16, 2020): 128. http://dx.doi.org/10.3390/catal10010128.
Повний текст джерелаIwaki, Hiroaki, Yoshie Hasegawa, Shaozhao Wang, Margaret M. Kayser, and 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, no. 11 (November 2002): 5671–84. http://dx.doi.org/10.1128/aem.68.11.5671-5684.2002.
Повний текст джерелаKostichka, Kristy, Stuart M. Thomas, Katharine J. Gibson, Vasantha Nagarajan, and Qiong Cheng. "Cloning and Characterization of a Gene Cluster for Cyclododecanone Oxidation in Rhodococcus ruber SC1." Journal of Bacteriology 183, no. 21 (November 1, 2001): 6478–86. http://dx.doi.org/10.1128/jb.183.21.6478-6486.2001.
Повний текст джерелаIwaki, Hiroaki, Shaozhao Wang, Stephan Grosse, Hélène Bergeron, Ayako Nagahashi, Jittiwud Lertvorachon, Jianzhong Yang, Yasuo Konishi, Yoshie Hasegawa, and Peter C. K. Lau. "Pseudomonad Cyclopentadecanone Monooxygenase Displaying an Uncommon Spectrum of Baeyer-Villiger Oxidations of Cyclic Ketones." Applied and Environmental Microbiology 72, no. 4 (April 2006): 2707–20. http://dx.doi.org/10.1128/aem.72.4.2707-2720.2006.
Повний текст джерелаTolmie, Carmien, Martha Smit, and Diederik Opperman. "Alternative Splicing of the Aflatoxin-Associated Baeyer–Villiger Monooxygenase from Aspergillus flavus: Characterisation of MoxY Isoforms." Toxins 10, no. 12 (December 5, 2018): 521. http://dx.doi.org/10.3390/toxins10120521.
Повний текст джерелаДисертації з теми "Baeyer-Villiger monooxygenase de type II"
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.
Повний текст джерелаRöllig, Robert. "Chemical hydride transfer for flavin dependent monooxygenases of two-component systems." Electronic Thesis or Diss., Aix-Marseille, 2021. http://www.theses.fr/2021AIXM0436.
Повний текст джерелаThe 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