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One Enzyme, Three Metabolites : Shewanella algae Controls Siderophore Production via the Cellular Substrate Pool

One Enzyme, Three Metabolites : Shewanella algae Controls Siderophore Production via the Cellular Substrate Pool

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RÜTSCHLIN, Sina, Sandra GUNESCH, Thomas BÖTTCHER, 2017. One Enzyme, Three Metabolites : Shewanella algae Controls Siderophore Production via the Cellular Substrate Pool. In: Cell Chemical Biology. 24(5), pp. 598-604. ISSN 2451-9456. eISSN 2451-9456

@article{Rutschlin2017-05-18Enzym-39422, title={One Enzyme, Three Metabolites : Shewanella algae Controls Siderophore Production via the Cellular Substrate Pool}, year={2017}, doi={10.1016/j.chembiol.2017.03.017}, number={5}, volume={24}, issn={2451-9456}, journal={Cell Chemical Biology}, pages={598--604}, author={Rütschlin, Sina and Gunesch, Sandra and Böttcher, Thomas}, note={Anhang: Seiten e1-e10} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/39422"> <dc:contributor>Böttcher, Thomas</dc:contributor> <dc:creator>Rütschlin, Sina</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-06-27T09:42:49Z</dcterms:available> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/39422"/> <dcterms:title>One Enzyme, Three Metabolites : Shewanella algae Controls Siderophore Production via the Cellular Substrate Pool</dcterms:title> <dcterms:abstract xml:lang="eng">Shewanella algae B516 produces avaroferrin, an asymmetric hydroxamate siderophore, which has been shown to inhibit swarming motility of Vibrio alginolyticus. We aimed to elucidate the biosynthesis of this siderophore and to investigate how S. algae coordinates the production of avaroferrin and its two symmetric counterparts. We reconstituted the reaction in vitro with the main enzyme AvbD and the putative biosynthetic precursors, and demonstrate that multispecificity of this enzyme results in the production of all three cyclic hydroxamate siderophores that were previously isolated as natural products from S. algae. Surprisingly, purified AvbD exhibited a clear preference for the larger cadaverine-derived substrate. In live cells, however, siderophore ratios are maximized toward avaroferrin production, and we demonstrate that these siderophore ratios are the result of a regulation on substrate pool level, which may allow rapid evolutionary adaptation to environmental changes. Our results thereby give insights into a unique evolutionary strategy toward metabolite diversity.</dcterms:abstract> <dcterms:issued>2017-05-18</dcterms:issued> <dc:creator>Gunesch, Sandra</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-06-27T09:42:49Z</dc:date> <dc:contributor>Gunesch, Sandra</dc:contributor> <dc:language>eng</dc:language> <dc:creator>Böttcher, Thomas</dc:creator> <dc:contributor>Rütschlin, Sina</dc:contributor> </rdf:Description> </rdf:RDF>

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