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Oxidation of dimethyl sulfide by various aromatic compound oxygenases from bacteria

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Abstract

As a result of the determination of dimethyl sulfide (DMS) oxidizing activity of bacterial aromatic compound oxygenases, multicomponent monooxygenases (DmpKLMNOP from Pseudomonas sp. CF600, AphKLMNOP from Comamonas testosteroni TA441, and TodABCDEF from Pseudomonas sp. JS150), single component monooxygenases (TfdB from Pseudomonas putida EST4011 and XylMA from Pseudomonas putida mt-2), and dioxygenases (CumA1A2A3A4 from Pseudomonas fluorescens IP01 and PahAaAbAcAd from Pseudomonas putida OUS82) showed DMS-oxidizing activity, while CarAaAcAd from Pseudomonas sp. CA10 and SoxC from Rhodococcus sp. IGTS8 did not. These results indicate the possibilities that these oxygenases might oxidize DMS to DMSO under the natural condition in the environment.

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Authors and Affiliations

  1. Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan

    Takako Yoshida, Hideaki Nojiri, Hisakazu Yamane & Toshio Omori

Authors
  1. Masae Horinouchi
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  2. Takako Yoshida
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  3. Hideaki Nojiri
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  4. Hisakazu Yamane
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  5. Toshio Omori
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Present address: Laboratory of Microbiology, The Institute of Physical and Chemical Research (RIKEN), 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan

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Horinouchi, M., Yoshida, T., Nojiri, H. et al. Oxidation of dimethyl sulfide by various aromatic compound oxygenases from bacteria. Biotechnology Letters 21, 929–933 (1999). https://doi.org/10.1023/A:1005679622067

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  • DOI: https://doi.org/10.1023/A:1005679622067

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