A Novel NADH-Dependent Carbonyl Reductase from Kluyveromyces aestuarii and Comparison of NADH-Regeneration System for the Synthesis of Ethyl (S)-4-Chloro-3-hydroxybutanoate

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To compare NADH-regeneration systems for the synthesis of (<I>S</I>)-4-chloro-3-hydroxybutanoate (ECHB), a novel NADH-dependent carbonyl reductase (KaCR1), which reduced ethyl 4-chloroacetoacetate (ECAA) to form (<I>S</I>)-ECHB, was screened and purified from <I>Kluyveromyces aestuarii</I> and a gene encoding KaCR1 was cloned. Glucose dehydrogenase (GDH) and formate dehydrogenase (FDH) were compared as enzymes for NADH regeneration using <I>Escherichia coli</I> cells coexpressing each enzyme with KaCR1. <I>E. coli</I> cells coexpressing GDH produced 45.6 g/<I>l</I> of (<I>S</I>)-ECHB from 50 g/<I>l</I> of ECAA and <I>E. coli</I> cells coexpressing FDH, alternatively, produced only 19.0 g/<I>l</I>. The low productivity in the case of FDH was suggested to result from the low activity and instability of FDH.

収録刊行物

  • Bioscience, biotechnology, and biochemistry

    Bioscience, biotechnology, and biochemistry 68(3), 638-649, 2004-03-23

    公益社団法人 日本農芸化学会

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各種コード

  • NII論文ID(NAID)
    10013143016
  • 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
    6904380
  • 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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