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The sulfonated osmolyte N-methyltaurine is dissimilated by Alcaligenes faecalis and by Paracoccus versutus with release of methylamine

The sulfonated osmolyte N-methyltaurine is dissimilated by Alcaligenes faecalis and by Paracoccus versutus with release of methylamine

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WEINITSCHKE, Sonja, Karin DENGER, Theo H. M. SMITS, Klaus HOLLEMEYER, Alasdair M. COOK, 2006. The sulfonated osmolyte N-methyltaurine is dissimilated by Alcaligenes faecalis and by Paracoccus versutus with release of methylamine. In: Microbiology. 152(4), pp. 1179-1186. ISSN 1350-0872. eISSN 1465-2080

@article{Weinitschke2006sulfo-8203, title={The sulfonated osmolyte N-methyltaurine is dissimilated by Alcaligenes faecalis and by Paracoccus versutus with release of methylamine}, year={2006}, doi={10.1099/mic.0.28622-0}, number={4}, volume={152}, issn={1350-0872}, journal={Microbiology}, pages={1179--1186}, author={Weinitschke, Sonja and Denger, Karin and Smits, Theo H. M. and Hollemeyer, Klaus and Cook, Alasdair M.} }

<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/123456789/8203"> <dc:format>application/pdf</dc:format> <dcterms:abstract xml:lang="eng">Selective enrichments yielded bacterial cultures able to utilize the osmolyte N-methyltaurine as sole source of carbon and energy or as sole source of fixed nitrogen for aerobic growth. Strain MT1, which degraded N-methyltaurine as a sole source of carbon concomitantly with growth, was identified as a strain of Alcaligenes faecalis. Stoichiometric amounts of methylamine, whose identity was confirmed by matrix-assisted, laser-desorption ionization time-of-flight mass spectrometry, and of sulfate were released during growth. Inducible N-methyltaurine dehydrogenase, sulfoacetaldehyde acetyltransferase (Xsc) and a sulfite dehydrogenase could be detected. Taurine dehydrogenase was also present and it was hypothesized that taurine dehydrogenase has a substrate range that includes N-methyltaurine. Partial sequences of a tauY-like gene (encoding the putative large component of taurine dehydrogenase) and an xsc gene were obtained by PCR with degenerate primers. Strain N-MT utilized N-methyltaurine as a sole source of fixed nitrogen for growth and could also utilize the compound as sole source of carbon. This bacterium was identified as a strain of Paracoccus versutus. This organism also expressed inducible (N-methyl)taurine dehydrogenase, Xsc and a sulfite dehydrogenase. The presence of a gene cluster with high identity to a larger cluster from Paracoccus pantotrophus NKNCYSA, which is now known to dissimilate N-methyltaurine via Xsc, allowed most of the overall pathway, including transport and excretion, to be defined. N-Methyltaurine is thus another compound whose catabolism is channelled directly through sulfoacetaldehyde.</dcterms:abstract> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:41:23Z</dc:date> <dcterms:issued>2006</dcterms:issued> <dc:rights>deposit-license</dc:rights> <dc:creator>Cook, Alasdair M.</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:41:23Z</dcterms:available> <dcterms:title>The sulfonated osmolyte N-methyltaurine is dissimilated by Alcaligenes faecalis and by Paracoccus versutus with release of methylamine</dcterms:title> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8203"/> <dc:contributor>Denger, Karin</dc:contributor> <dc:creator>Hollemeyer, Klaus</dc:creator> <dc:creator>Weinitschke, Sonja</dc:creator> <dc:creator>Smits, Theo H. M.</dc:creator> <dc:language>eng</dc:language> <dc:creator>Denger, Karin</dc:creator> <dc:contributor>Smits, Theo H. M.</dc:contributor> <dc:contributor>Cook, Alasdair M.</dc:contributor> <dc:contributor>Hollemeyer, Klaus</dc:contributor> <dcterms:bibliographicCitation>First publ. in: Microbiology 152 (2006), pp. 1179-1186</dcterms:bibliographicCitation> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:contributor>Weinitschke, Sonja</dc:contributor> </rdf:Description> </rdf:RDF>

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