Purification and Properties of a Carbonyl Reductase Useful for Production of Ethyl (S)-4-Chloro-3-hydroxybutanoate from Kluyveromyces lactis | Zendy

Hiroaki Yamamoto | Zendy; Norihiro Kimoto | Zendy; Akinobu Matsuyama | Zendy; Yoshinori Kobayashi | Zendy

Open Access

Purification and Properties of a Carbonyl Reductase Useful for Production of Ethyl (S)-4-Chloro-3-hydroxybutanoate from Kluyveromyces lactis

Author(s) -

Hiroaki Yamamoto,

Norihiro Kimoto,

Akinobu Matsuyama,

Yoshinori Kobayashi

Publication year - 2002

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.66.1775

Subject(s) - kluyveromyces lactis , kluyveromyces , reductase , chemistry , catalysis , biochemistry , protein subunit , yeast , enzyme , stereochemistry , saccharomyces cerevisiae , gene

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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