Relevant bibliographies by topics / Baeyer-Villiger monooxygenase de type II

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Academic literature on the topic 'Baeyer-Villiger monooxygenase de type II'

Author: Grafiati
Published: 25 May 2024
Last updated: 31 July 2025

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Journal articles on the topic "Baeyer-Villiger monooxygenase de type II"

1

Isupov, Michail N., Ewald Schröder, Robert P. Gibson, 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 (2015): 2344–53. http://dx.doi.org/10.1107/s1399004715017939.

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The three-dimensional structures of the native enzyme and the FMN complex of the overexpressed form of the oxygenating component of the type II Baeyer–Villiger 3,6-diketocamphane monooxygenase have been determined to 1.9 Å resolution. The structure of this dimeric FMN-dependent enzyme, which is encoded on the large CAM plasmid ofPseudomonas putida, has been solved by a combination of multiple anomalous dispersion from a bromine crystal soak and molecular replacement using a bacterial luciferase model. The orientation of the isoalloxazine ring of the FMN cofactor in the active site of this TIM-
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Isupov, Michail N., Ewald Schröder, Robert P. Gibson, 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 (2018): 379. http://dx.doi.org/10.1107/s205979831800150x.

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Löwe, 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.

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Riebel, 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 (2013): 1112–17. http://dx.doi.org/10.1002/cctc.201300550.

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Tanner, 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 (2000): 6565–69. http://dx.doi.org/10.1128/jb.182.23.6565-6569.2000.

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ABSTRACT An arylketone monooxygenase was purified from Pseudomonas putida JD1 by ion exchange and affinity chromatography. It had the characteristics of a Baeyer-Villiger-type monooxygenase and converted its substrate, 4-hydroxyacetophenone, into 4-hydroxyphenyl acetate with the consumption of one molecule of oxygen and oxidation of one molecule of NADPH per molecule of substrate. The enzyme was a monomer with an M r of about 70,000 and contained one molecule of flavin adenine dinucleotide (FAD). The enzyme was specific for NADPH as the electron donor, and spectral studies showed rapid reducti
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Niero, Mattia, Irene Righetto, Elisa Beneventi, et al. "Unique Features of a New Baeyer–Villiger Monooxygenase from a Halophilic Archaeon." Catalysts 10, no. 1 (2020): 128. http://dx.doi.org/10.3390/catal10010128.

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Type I Baeyer–Villiger monooxygenases (BVMOs) are flavin-dependent monooxygenases that catalyze the oxidation of ketones to esters or lactones, a reaction otherwise performed in chemical processes by employing hazardous and toxic peracids. Even though various BVMOs are extensively studied for their promising role in industrial biotechnology, there is still a demand for enzymes that are able to retain activity at high saline concentrations. To this aim, and based on comparative in silico analyses, we cloned HtBVMO from the extremely halophilic archaeon Haloterrigena turkmenica DSM 5511. When ex
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Iwaki, 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 (2002): 5671–84. http://dx.doi.org/10.1128/aem.68.11.5671-5684.2002.

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ABSTRACT Cyclopentanone 1,2-monooxygenase, a flavoprotein produced by Pseudomonas sp. strain NCIMB 9872 upon induction by cyclopentanol or cyclopentanone (M. Griffin and P. W. Trudgill, Biochem. J. 129:595-603, 1972), has been utilized as a biocatalyst in Baeyer-Villiger oxidations. To further explore this biocatalytic potential and to discover new genes, we have cloned and sequenced a 16-kb chromosomal locus of strain 9872 that is herein reclassified as belonging to the genus Comamonas. Sequence analysis revealed a cluster of genes and six potential open reading frames designated and grouped
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Kostichka, 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 (2001): 6478–86. http://dx.doi.org/10.1128/jb.183.21.6478-6486.2001.

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ABSTRACT Biological oxidation of cyclic ketones normally results in formation of the corresponding dicarboxylic acids, which are further metabolized in the cell. Rhodococcus ruber strain SC1 was isolated from an industrial wastewater bioreactor that was able to utilize cyclododecanone as the sole carbon source. A reverse genetic approach was used to isolate a 10-kb gene cluster containing all genes required for oxidative conversion of cyclododecanone to 1,12-dodecanedioic acid (DDDA). The genes required for cyclododecanone oxidation were only marginally similar to the analogous genes for cyclo
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9

Iwaki, Hiroaki, Shaozhao Wang, Stephan Grosse, et al. "Pseudomonad Cyclopentadecanone Monooxygenase Displaying an Uncommon Spectrum of Baeyer-Villiger Oxidations of Cyclic Ketones." Applied and Environmental Microbiology 72, no. 4 (2006): 2707–20. http://dx.doi.org/10.1128/aem.72.4.2707-2720.2006.

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ABSTRACT Baeyer-Villiger monooxygenases (BVMOs) are biocatalysts that offer the prospect of high chemo-, regio-, and enantioselectivity in the organic synthesis of lactones or esters from a variety of ketones. In this study, we have cloned, sequenced, and overexpressed in Escherichia coli a new BVMO, cyclopentadecanone monooxygenase (CpdB or CPDMO), originally derived from Pseudomonas sp. strain HI-70. The 601-residue primary structure of CpdB revealed only 29% to 50% sequence identity to those of known BVMOs. A new sequence motif, characterized by a cluster of charged residues, was identified
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10

Tolmie, 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 (2018): 521. http://dx.doi.org/10.3390/toxins10120521.

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Aflatoxins are carcinogenic mycotoxins that are produced by the filamentous fungus Aspergillus flavus, a contaminant of numerous food crops. Aflatoxins are synthesised via the aflatoxin biosynthesis pathway, with the enzymes involved encoded by the aflatoxin biosynthesis gene cluster. MoxY is a type I Baeyer–Villiger monooxygenase (BVMO), responsible for the conversion of hydroxyversicolorone (HVN) and versicolorone (VN) to versiconal hemiacetal acetate (VHA) and versiconol acetate (VOAc), respectively. Using mRNA data, an intron near the C-terminus was identified that is alternatively spliced
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Dissertations / Theses on the topic "Baeyer-Villiger monooxygenase de type II"

1

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.

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Type II polyketide synthase (PKS) produced natural products have proven to be an excellent source of pharmacologically relevant molecules due to their rich biological activities and chemical scaffolds. Type II-PKS manufactured polyketides share similar polycyclic aromatic backbones leaving their diversity to stem from various chemical additions and alterations facilitated by post-PKS tailoring enzymes. Evidence suggests that post-PKS tailoring enzymes form complexes in order to facilitate the highly orchestrated process of biosynthesis. Thus, protein-protein interactions between these enzymes
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Röllig, Robert. "Chemical hydride transfer for flavin dependent monooxygenases of two-component systems." Electronic Thesis or Diss., Aix-Marseille, 2021. http://www.theses.fr/2021AIXM0436.

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Le terme monooxygénases flavoprotéiques (flavoprotein monooxygenases FPMO) recouvre aussi bien des flavoenzymes formées d’une seule composante que de deux. L'indépendance fonctionnelle de la partie oxygénase de la 2,5-dicétocamphane 1,2-monooxygénase I (2,5-DKCMO), une Baeyer-Villiger monooxygénase de type II, FMN dépendante, de sa contrepartie réductase, ainsi que le mécanisme de transfert de la flavine par libre diffusion, ont été étudiés dans des réactions sans réductase mais où des analogues biomimétiques synthétiques de nicotinamide (NCB) ont été utilisés pour réduire le FMN. L'équilibre
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