Isolation and Characterization of an Alcohol Dehydrogenase Gene from the Octylphenol Polyethoxylate Degrader Pseudomonas putida S-5

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Octylphenol polyethoxylate (OPEO<SUB>n</SUB>) biodegradation by <I>Pseudomonas putida</I> S-5 under aerobic conditions is initiated by the oxidation of its terminal alcohol group by alcohol dehydrogenase. A DNA fragment, containing an alcohol dehydrogenase gene (<I>adh1</I>), was isolated using a combination of degenerate PCR and inverse PCR. The predicted translation product of <I>adh1</I> showed significant sequence similarity to bacterial alcohol dehydrogenases. Furthermore, a flavin-binding motif and signature patterns conserved in type III FAD-dependent alcohol oxidases were detected. Two open reading frames (ORFs) were found upstream of <I>adh1</I>, encoding a putative acyl-CoA synthetase and a putative esterase. Downstream of <I>adh1</I> and located on the opposite strand was an ORF encoding a putative aldehyde dehydrogenase. Transcription analysis using RT-PCR showed that <I>adh1</I> is cotranscribed with the putative acyl-CoA synthetase and esterase genes during growth on OPEO<SUB>n</SUB>. ADH1 overproduced in <I>Escherichia coli</I> exhibited activity not only toward various alcohols, including OPEO<SUB>n</SUB>s, but also toward primary aliphatic and aromatic aldehydes.

収録刊行物

  • Bioscience, biotechnology, and biochemistry  

    Bioscience, biotechnology, and biochemistry 70(8), 1855-1863, 2006-08-23 

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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各種コード

  • NII論文ID(NAID)
    10018527959
  • NII書誌ID(NCID)
    AA10824164
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    09168451
  • NDL 記事登録ID
    8040150
  • NDL 雑誌分類
    ZR7(科学技術--農林水産--農産) // ZR2(科学技術--生物学--生化学) // ZP1(科学技術--化学・化学工業)
  • NDL 請求記号
    Z53-G223
  • データ提供元
    CJP書誌  CJP引用  NDL  J-STAGE 
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