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An unexpected gene cluster for downstream degradation of alkylphenols in Sphingomonas sp. strain TTNP3

Kolvenbach, Boris ; Dobrowinski, Hyazinth ; Fousek, Jan ; Vlcek, Cestmir ; Schäffer, Andreas ; Gabriel, Frederic ; Kohler, Hans-Peter ; Corvini, Philippe

In: Applied Microbiology and Biotechnology, 2012, vol. 93, no. 3, p. 1315-1324

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    Titre
    • An unexpected gene cluster for downstream degradation of alkylphenols in Sphingomonas sp. strain TTNP3
    Auteur
    • Kolvenbach, Boris. Institute for Ecopreneurship, School of Life Sciences, University of Applied Sciences Northwestern Switzerland, Muttenz, Switzerland
    • Dobrowinski, Hyazinth. Institute for Ecopreneurship, School of Life Sciences, University of Applied Sciences Northwestern Switzerland, Muttenz, Switzerland
    • Fousek, Jan. Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic
    • Vlcek, Cestmir. Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic
    • Schäffer, Andreas. Institute for Environmental Research, Rheinisch-Westfälische Technische Hochschule, Aachen, Germany
    • Gabriel, Frederic. Institute of Clinical Chemistry and Laboratory Medicine, University of Rostock, Rostock, Germany
    • Kohler, Hans-Peter. Swiss Federal Institute of Aquatic Science and Technology, Dübendorf, Switzerland
    • Corvini, Philippe. Institute for Ecopreneurship, School of Life Sciences, University of Applied Sciences Northwestern Switzerland, Muttenz, Switzerland
    Type de document
    • Postprint
    Langue
    • Anglais
    Publié dans
    • Applied Microbiology and Biotechnology, 2012, vol. 93, no. 3, p. 1315-1324. Springer-Verlag
    Autre version électronique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:314302
    Summary
    In silico analysis of nucleotide sequences flanking the recently found hydroquinone dioxygenase in Sphingomonas sp. strain TTNP3 revealed a gene cluster that encodes a hydroquinone catabolic pathway. In addition to the two open-reading frames encoding the recently characterized hydroquinone dioxygenase, the cluster consisted of six open-reading frames. We were able to express the three open-reading frames, hqdC, hqdD, and hqdE, and demonstrated that the three gene products, HqdC, HqdD, and HqdE had 4-hydroxymuconic semialdehyde dehydrogenase, maleylacetate reductase, and intradiol dioxygenase activity, respectively. Surprisingly, the gene cluster showed similarities to functionally related clusters found in members of the β- and γ-proteobacteria rather than to those found in other members of the genus Sphingomonas sensu latu