Stereoselective Reduction of Carbonyl Compounds with Actinomycete: Purification and Characterization of Three .ALPHA.-Keto Ester Reductases from Streptomyces avermitilis

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  • ISHIHARA Kohji
    Department of Life Science, Okayama University of Science Graduate School of Science, Okayama University of Science
  • KATO Chiaki
    Graduate School of Science, Okayama University of Science
  • YAMAGUCHI Hitomi
    Research and Development Center, Nagase & Co., Ltd.
  • IWAI Rieko
    Graduate School of Science, Okayama University of Science
  • YOSHIDA Momoko
    Department of Life Science, Okayama University of Science
  • IKEDA Natsumi
    Department of Life Science, Okayama University of Science
  • HAMADA Hiroki
    Department of Life Science, Okayama University of Science Graduate School of Science, Okayama University of Science
  • MASUOKA Noriyoshi
    Department of Life Science, Okayama University of Science Graduate School of Science, Okayama University of Science
  • NAKAJIMA Nobuyoshi
    Graduate School of Health and Welfare, Okayama Prefectural University

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Other Title
  • Stereoselective reduction of carbonyl compounds with actinomycete: purification and characterization of three α-keto ester reductases from Streptomyces avermitilis
  • Stereoselective reduction of carbonyl compounds with actinomycete purification and characterization of three a keto ester reductases from Streptomyces avermitilis
  • Stereoselective Reduction of Carbonyl Compounds with Actinomycete: Purification and Characterization of Three α-Keto Ester Reductases from<i>Streptomyces avermitilis</i>

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Abstract

We achieved the purification of three α-keto ester reductases (Streptomyces avermitilis keto ester reductase, SAKERs-I, -II, and -III) from Streptomyces avermitilis NBRC14893 whole cells. The molecular masses of the native SAKERs-I, -II, and -III were estimated to be 72, 38, and 36 kDa, respectively, by gel filtration chromatography. The subunit molecular masses of SAKERs-I, -II, and -III were also estimated to be 32, 32, and 34 kDa, respectively, by SDS-polyacrylamide gel electrophoresis. The purified SAKERs-II and -III showed a reducing activity for α-keto esters (in particular, for ethyl pyruvate). SAKER-I showed a high reducing activity not only toward the α- and β-keto esters, but also toward α-keto acid. The N-terminal region amino acid sequences of SAKERs-I, -II, and -III were identical to that of a putative oxidoreductase, SAV2750, a putative oxidoreductase, SAV1849, and a putative oxidoreductase, SAV4117, respectively, hypothetical proteins coded on the S. avermitilis genome.

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