{"type": "FeatureCollection", "features": [{"id": "10.1002/cbic.202000051", "type": "Feature", "geometry": null, "properties": {"updated": "2026-04-13T16:14:06Z", "type": "Journal Article", "created": "2020-01-31", "title": "An Engineered E.\u2005coli Strain for Direct in Vivo Fluorination", "description": "Abstract<p>Selectively fluorinated compounds are found frequently in pharmaceutical and agrochemical products where currently 25\uffe2\uff80\uff9330\uffe2\uff80\uff89% of optimised compounds emerge from development containing at least one fluorine atom. There are many methods for the site\uffe2\uff80\uff90specific introduction of fluorine, but all are chemical and they often use environmentally challenging reagents. Biochemical processes for C\uffe2\uff88\uff92F bond formation are attractive, but they are extremely rare. In this work, the fluorinase enzyme, originally identified from the actinomycete bacterium Streptomyces cattleya, is engineered into Escherichia coli in such a manner that the organism is able to produce 5\uffe2\uff80\uffb2\uffe2\uff80\uff90fluorodeoxyadenosine (5\uffe2\uff80\uffb2\uffe2\uff80\uff90FDA) from S\uffe2\uff80\uff90adenosyl\uffe2\uff80\uff90l\uffe2\uff80\uff90methionine (SAM) and fluoride in live E.\uffe2\uff80\uff85coli cells. Success required the introduction of a SAM transporter and deletion of the endogenous fluoride efflux capacity in order to generate an E.\uffe2\uff80\uff85coli host that has the potential for future engineering of more elaborate fluorometabolites.</p>", "keywords": ["SAM transporters", "0301 basic medicine", "570", "S-Adenosylmethionine", "0303 health sciences", "Deoxyadenosines", "Halogenation", "DAS", "Fluorine", "Halogenations", "540", "QD Chemistry", "Streptomyces", "3. Good health", "03 medical and health sciences", "Bacterial Proteins", "Isomerism", "Escherichia coli", "QD", "Fluoride channels", "Genetic Engineering", "Oxidoreductases", "Fluorinases"]}, "links": [{"href": "https://onlinelibrary.wiley.com/doi/pdf/10.1002/cbic.202000051"}, {"href": "https://doi.org/10.1002/cbic.202000051"}, {"rel": "related", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items/ChemBioChem", "name": "related record", "description": "related record", "type": "application/json"}, {"rel": "self", "type": "application/geo+json", "title": "10.1002/cbic.202000051", "name": "item", "description": "10.1002/cbic.202000051", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items/10.1002/cbic.202000051"}, {"rel": "collection", "type": "application/json", "title": "Collection", "name": "collection", "description": "Collection", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main"}], "time": {"date": "2020-03-03T00:00:00Z"}}, {"id": "10.1038/s41598-023-49194-y", "type": "Feature", "geometry": null, "properties": {"updated": "2026-04-13T16:18:17Z", "type": "Journal Article", "created": "2023-12-13", "title": "Unraveling the genome of Bacillus velezensis MEP218, a strain producing fengycin homologs with broad antibacterial activity: comprehensive comparative genome analysis", "description": "Abstract<p>Bacillus sp. MEP218, a soil bacterium with high potential as a source of bioactive molecules, produces mostly C16\uffe2\uff80\uff93C17 fengycin and other cyclic lipopeptides (CLP) when growing under previously optimized culture conditions. This work addressed the elucidation of the genome sequence of MEP218 and its taxonomic classification. The genome comprises 3,944,892\uffc2\uffa0bp, with a total of 3474 coding sequences and a G\uffe2\uff80\uff89+\uffe2\uff80\uff89C content of 46.59%. Our phylogenetic analysis to determine the taxonomic position demonstrated that the assignment of the MEP218 strain to Bacillus velezensis species provides insights into its evolutionary context and potential functional attributes. The in silico genome analysis revealed eleven gene clusters involved in the synthesis of secondary metabolites, including non-ribosomal CLP (fengycins and surfactin), polyketides, terpenes, and bacteriocins. Furthermore, genes encoding phytase, involved in the release of phytic phosphate for plant and animal nutrition, or other enzymes such as cellulase, xylanase, and alpha 1\uffe2\uff80\uff934 glucanase were detected. In vitro antagonistic assays against Salmonella typhimurium, Acinetobacter baumanii, Escherichia coli, among others, demonstrated a broad spectrum of C16\uffe2\uff80\uff93C17 fengycin produced by MEP218. MEP218 genome sequence analysis expanded our understanding of the diversity and genetic relationships within the Bacillus genus and updated the Bacillus databases with its unique trait to produce antibacterial fengycins and its potential as a resource of biotechnologically useful enzymes.</p", "keywords": ["0301 basic medicine", "Bacillus", "Gene", "Agricultural and Biological Sciences", "https://purl.org/becyt/ford/1.6", "Phylogeny", "GC-content", "2. 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