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

Author: Grafiati

Published: 25 May 2024

Last updated: 31 July 2025

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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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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11

Willetts, Andrew, Ian Joint, Jack A. Gilbert, William Trimble, and Martin Mühling. "Isolation and initial characterization of a novel type of Baeyer-Villiger monooxygenase activity from a marine microorganism." Microbial Biotechnology 5, no. 4 (2012): 549–59. http://dx.doi.org/10.1111/j.1751-7915.2012.00337.x.

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12

Zhang, Chunyan, Huaran Zhang, and Jianhua Ju. "On-PKS Baeyer–Villiger-Type O-Atom Insertion Catalyzed by Luciferase-Like Monooxygenase OvmO during Olimycin Biosynthesis." Organic Letters 22, no. 5 (2020): 1780–84. http://dx.doi.org/10.1021/acs.orglett.0c00076.

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13

Dudek, Hanna M., Gonzalo de Gonzalo, Daniel E. Torres Pazmiño, et al. "Mapping the Substrate Binding Site of Phenylacetone Monooxygenase from Thermobifida fusca by Mutational Analysis." Applied and Environmental Microbiology 77, no. 16 (2011): 5730–38. http://dx.doi.org/10.1128/aem.00687-11.

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ABSTRACTBaeyer-Villiger monooxygenases catalyze oxidations that are of interest for biocatalytic applications. Among these enzymes, phenylacetone monooxygenase (PAMO) fromThermobifida fuscais the only protein showing remarkable stability. While related enzymes often present a broad substrate scope, PAMO accepts only a limited number of substrates. Due to the absence of a substrate in the elucidated crystal structure of PAMO, the substrate binding site of this protein has not yet been defined. In this study, a structural model of cyclopentanone monooxygenase, which acts on a broad range of comp

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14

Leisch, Hannes, Rong Shi, Stephan Grosse та ін. "Cloning, Baeyer-Villiger Biooxidations, and Structures of the Camphor Pathway 2-Oxo-Δ3-4,5,5-Trimethylcyclopentenylacetyl-Coenzyme A Monooxygenase of Pseudomonas putida ATCC 17453". Applied and Environmental Microbiology 78, № 7 (2012): 2200–2212. http://dx.doi.org/10.1128/aem.07694-11.

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ABSTRACTA dimeric Baeyer-Villiger monooxygenase (BVMO) catalyzing the lactonization of 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-coenzyme A (CoA), a key intermediate in the metabolism of camphor byPseudomonas putidaATCC 17453, had been initially characterized in 1983 by Ougham and coworkers (H. J. Ougham, D. G. Taylor, and P. W. Trudgill, J. Bacteriol. 153:140–152, 1983). Here we cloned and overexpressed the 2-oxo-Δ3-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase (OTEMO) inEscherichia coliand determined its three-dimensional structure with bound flavin adenine dinucleotide (FAD) at a 1

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15

Mansouri, Hamid R., Marko D. Mihovilovic, and Florian Rudroff. "Investigation of a New Type I Baeyer–Villiger Monooxygenase from Amycolatopsis thermoflava Revealed High Thermodynamic but Limited Kinetic Stability." ChemBioChem 21, no. 7 (2020): 971–77. http://dx.doi.org/10.1002/cbic.201900501.

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16

González, Carolina, Sebastián Rodríguez, José Pablo Reyes-Godoy, Valeria Razmilic, and Irene Martínez. "Recombinant Expression and Characterization of a Novel Type I Baeyer–Villiger Monooxygenase from a Streptomyces Strain Isolated from the Rhizosphere of the Atacama Desert Lupinus oreophilus." International Journal of Molecular Sciences 26, no. 13 (2025): 5940. https://doi.org/10.3390/ijms26135940.

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The Atacama Desert is emerging as an unexpected source of microbial life and, thus, a source of bioactive compounds and novel enzymes. Baeyer–Villiger monooxygenases (BVMOs), a subclass of flavin-dependent monooxygenases (FPMOs), have gained attention as promising biocatalysts for the biosynthesis of industrially relevant molecules for a wide range of applications, such as pharmaceuticals and polymers, among others. BVMOs catalyze the oxidation of ketones and cyclic ketones to esters and lactones, respectively, by using molecular oxygen and NAD(P)H. BVMOs may also catalyze heteroatoms oxidatio

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17

Weiss, Michael, Karin Denger, Thomas Huhn, and David Schleheck. "Two Enzymes of a Complete Degradation Pathway for Linear Alkylbenzenesulfonate (LAS) Surfactants: 4-Sulfoacetophenone Baeyer-Villiger Monooxygenase and 4-Sulfophenylacetate Esterase in Comamonas testosteroni KF-1." Applied and Environmental Microbiology 78, no. 23 (2012): 8254–63. http://dx.doi.org/10.1128/aem.02412-12.

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ABSTRACTComplete biodegradation of the surfactant linear alkylbenzenesulfonate (LAS) is accomplished by complex bacterial communities in two steps. First, all LAS congeners are degraded into about 50 sulfophenylcarboxylates (SPC), one of which is 3-(4-sulfophenyl)butyrate (3-C4-SPC). Second, these SPCs are mineralized. 3-C4-SPC is mineralized byComamonas testosteroniKF-1 in a process involving 4-sulfoacetophenone (SAP) as a metabolite and an unknown inducible Baeyer-Villiger monooxygenase (BVMO) to yield 4-sulfophenyl acetate (SPAc) from SAP (SAPMO enzyme); hydrolysis of SPAc to 4-sulfophenol

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18

Landry, Zachary, Brandon K. Swan, Gerhard J. Herndl, Ramunas Stepanauskas, and Stephen J. Giovannoni. "SAR202 Genomes from the Dark Ocean Predict Pathways for the Oxidation of Recalcitrant Dissolved Organic Matter." mBio 8, no. 2 (2017). http://dx.doi.org/10.1128/mbio.00413-17.

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ABSTRACTDeep-ocean regions beyond the reach of sunlight contain an estimated 615 Pg of dissolved organic matter (DOM), much of which persists for thousands of years. It is thought that bacteria oxidize DOM until it is too dilute or refractory to support microbial activity. We analyzed five single-amplified genomes (SAGs) from the abundant SAR202 clade of dark-ocean bacterioplankton and found they encode multiple families of paralogous enzymes involved in carbon catabolism, including several families of oxidative enzymes that we hypothesize participate in the degradation of cyclic alkanes. The

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19

Bunyat-zada, Amir R., Stephan E. Ducharme, Maria E. Cleveland, Esther R. Hoffman, and Graeme Howe. "Genome mining leads to the identification of a stable and promiscuous Baeyer‐Villiger monooxygenase from a thermophilic microorganism." ChemBioChem, July 11, 2024. http://dx.doi.org/10.1002/cbic.202400443.

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Baeyer‐Villiger monooxygenases (BVMOs) are NAD(P)H‐dependent flavoproteins that convert ketones to esters and lactones. While these enzymes offer an appealing alternative to traditional Baeyer‐Villiger oxidations, these proteins tend to be either too unstable or exhibit too narrow of a substrate scope for implementation as industrial biocatalysts. Here, sequence similarity networks were used to search for novel BVMOs that are both stable and promiscuous. Our genome mining led to the identification of an enzyme from Chloroflexota bacterium (strain G233) dubbed ssnBVMO that exhibits i) the highe

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20

Ceccoli, Romina D., Dario A. Bianchi, Michael J. Fink, Marko D. Mihovilovic, and Daniela V. Rial. "Cloning and characterization of the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa." AMB Express 7, no. 1 (2017). http://dx.doi.org/10.1186/s13568-017-0390-5.

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21

Zhang, Yan, Feng Liu, Na Xu, et al. "Discovery of Two Native Baeyer-Villiger Monooxygenases for Asymmetric Synthesis of Bulky Chiral Sulfoxides." Applied and Environmental Microbiology 84, no. 14 (2018). http://dx.doi.org/10.1128/aem.00638-18.

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ABSTRACT Two Baeyer-Villiger monooxygenases (BVMOs), designated Bo BVMO and Am BVMO, were discovered from Bradyrhizobium oligotrophicum and Aeromicrobium marinum , respectively. Both monooxygenases displayed novel features for catalyzing the asymmetric sulfoxidation of bulky and pharmaceutically relevant thioethers. Evolutionary relationship and sequence analysis revealed that the two BVMOs belong to the family of typical type I BVMOs and the subtype ethionamide monooxygenase. Both BVMOs are active toward medium- and long-chain aliphatic ketones as well as various thioether substrates but are

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22

Bornscheuer, Uwe, Thomas Oiffer, Friedemann Leipold, et al. "Chemo‐Enzymatic Depolymerization of Functionalized Low‐Molecular‐Weight Polyethylene." Angewandte Chemie, September 24, 2024. http://dx.doi.org/10.1002/ange.202415012.

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Polyethylene (PE) is the most commonly used plastic type in the world, contributing significantly to the plastic waste crisis. Microbial degradation of PE in natural environments is unlikely due to its inert saturated carbon‐carbon backbones, which are difficult to break down by enzymes, challenging the development of a biocatalytic recycling method for PE waste. Here, we demonstrated the depolymerization of low‐molecular‐weight (LMW) PE using an enzyme cascade that included a catalase‐peroxidase, an alcohol dehydrogenase, a Baeyer Villiger monooxygenase, and a lipase after the polymer was che

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23

Bornscheuer, Uwe, Thomas Oiffer, Friedemann Leipold, et al. "Chemo‐Enzymatic Depolymerization of Functionalized Low‐Molecular‐Weight Polyethylene." Angewandte Chemie International Edition, September 24, 2024. http://dx.doi.org/10.1002/anie.202415012.

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Polyethylene (PE) is the most commonly used plastic type in the world, contributing significantly to the plastic waste crisis. Microbial degradation of PE in natural environments is unlikely due to its inert saturated carbon‐carbon backbones, which are difficult to break down by enzymes, challenging the development of a biocatalytic recycling method for PE waste. Here, we demonstrated the depolymerization of low‐molecular‐weight (LMW) PE using an enzyme cascade that included a catalase‐peroxidase, an alcohol dehydrogenase, a Baeyer Villiger monooxygenase, and a lipase after the polymer was che

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24

Qin, Peng, Xin‐Yi Lu, Jian‐He Xu, and Hui‐Lei Yu. "Directed evolution of Baeyer–Villiger monooxygenase for highly secretory expressed in Pichia pastoris and efficient preparation of chiral pyrazole sulfoxide." Biotechnology and Bioengineering, December 13, 2023. http://dx.doi.org/10.1002/bit.28617.

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AbstractThe methylotrophic yeast Pichia pastoris (Komagataella phaffii) is a highly distinguished expression platform for the excellent synthesis of various heterologous proteins in recent years. With the advantages of high‐density fermentation, P. pastoris can produce gram amounts of recombinant proteins. While not every protein of interest can be expressed to such high titers, such as Baeyer–Villiger monooxygenase (BVMO) (AcPSMO) which is responsible for pyrazole sulfide asymmetric oxidation. In this work, an excellent yeast expression system was established to facilitate efficient AcPSMO ex

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