Purification and properties of a carbonyl reductase useful for production of ethyl (S)-4-chloro-3-hydroxybutanoate from Kluyveromyces lactis |
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Authors: | Yamamoto Hiroaki Kimoto Norihiro Matsuyama Akinobu Kobayashi Yoshinori |
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Affiliation: | Life Science Development Center, CPI Company, Daicel Chemical Industries, Ltd., Tsukuba, Ibaraki, Japan. h-yamamoto@daicel.co.jp |
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Abstract: | A novel carbonyl reductase (KLCR1) that reduced ethyl 4-chloroacetoacetate (ECAA) to synthesize ethyl (S)-4-chloro-3-hydroxybutanoate ((S)-ECHB) was purified from Kluyveromyces lactis. KLCR1 catalyzed the NADPH-dependent reduction of ECAA enantioselectively but not the oxidation of (S)-ECHB. From partial amino acid sequences, KLCR1 was suggested to be an alpha subunit of fatty acid synthase (FAS) but did not have FAS activity. |
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