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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  • YAMAMOTO Hiroaki
    Life Science Development Center, CPI Company, Daicel Chemical Industries, Ltd., Tsukuba Research Center
  • MITSUHASHI Kazuya
    Life Science Development Center, CPI Company, Daicel Chemical Industries, Ltd., Tsukuba Research Center
  • KIMOTO Norihiro
    Life Science Development Center, CPI Company, Daicel Chemical Industries, Ltd., Tsukuba Research Center
  • MATSUYAMA Akinobu
    Corporate Development Center, Daicel Chemical Industries, Ltd., Tsukuba Research Center
  • ESAKI Nobuyoshi
    Institute for Chemical Research, Kyoto University
  • KOBAYASHI Yoshinori
    Life Science Development Center, CPI Company, Daicel Chemical Industries, Ltd., Tsukuba Research Center

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タイトル別名
  • A Novel NADH-Dependent Carbonyl Reductase from <I>Kluyveromyces aestuarii</I> and Comparison of NADH-Regeneration System for the Synthesis of Ethyl (<I>S</I>)-4-Chloro-3-hydroxybutanoate
  • Novel NADH Dependent Carbonyl Reductase from Kluyveromyces aestuarii and Comparison of NADH Regeneration System for the Synthesis of Ethyl S 4 Chloro 3 hydroxybutanoate
  • A novel NADH-dependent carbonyl reductase from Kluyveromyces aestuarii and comparison of NADH-regeneration system for the synthesis of ethyl (S)-4-chloro-3-oxobutanoate

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

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