M
Michihiko Kataoka
Researcher at Osaka Prefecture University
Publications - 140
Citations - 3451
Michihiko Kataoka is an academic researcher from Osaka Prefecture University. The author has contributed to research in topics: Reductase & Enzyme. The author has an hindex of 31, co-authored 139 publications receiving 3288 citations. Previous affiliations of Michihiko Kataoka include Kyoto University & Kaneka Corporation.
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Novel bioreduction system for the production of chiral alcohols
TL;DR: This review focuses on the establishment of a novel bioreduction system using an Escherichia coli transformant co-expressing genes for carbonyl reductase and cofactor-regeneration enzyme that could be useful as an all-purpose catalyst for asymmetric reduction reactions.
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Synthesis of optically pure ethyl (S)-4-chloro-3-hydroxybutanoate by Escherichia coli transformant cells coexpressing the carbonyl reductase and glucose dehydrogenase genes.
Noriyuki Kizaki,Yoshihiko Yasohara,Junzo Hasegawa,Masaru Wada,Michihiko Kataoka,Sakayu Shimizu +5 more
TL;DR: The aqueous system used for the reduction reaction involving E. coli HB101 cells carrying a plasmid containing the S1 and GDH genes as a catalyst is simple and highly advantageous for the practical synthesis of optically pure (S)-CHBE.
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Stereoselective reduction of ethyl 4-chloro-3-oxobutanoate by Escherichia coli transformant cells coexpressing the aldehyde reductase and glucose dehydrogenase genes.
Michihiko Kataoka,Kazuhiko Yamamoto,Hiroshi Kawabata,Masaru Wada,Keiko Kita,Hideshi Yanase,Sakayu Shimizu +6 more
TL;DR: The use of E. coli JM109 cells harboring pKAR and pACGD as a catalyst is highly advantageous for the practical synthesis of (R)-CHBE, and does not require the addition of GDH or the isolation of the enzymes.
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Gene cloning, biochemical characterization and physiological role of a thermostable low‐specificity L‐threonine aldolase from Escherichia coli
TL;DR: The ltaE gene encoding for a thermostable low-specificity L-threonine aldolase, which catalyzes the cleavage of L- Threonine/L-allo-threxine to glycine and acetaldehyde, was cloned from Escherichia coli GS245 by the polymerase chain reaction and characterized.
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Purification and Characterization of NADPH-Dependent Carbonyl Reductase, Involved in Stereoselective Reduction of Ethyl 4-Chloro-3-oxobutanoate, from Candida magnoliae
Masaru Wada,Michihiko Kataoka,Hiroshi Kawabata,Yoshihiko Yasohara,Noriyuki Kizaki,Junzo Hasegawa,Sakayu Shimizu +6 more
TL;DR: A NADPH-dependent carbonyl reductase was purified to homogeneity from Candida magnoliae AKU4643 through four steps, including Blue Sepharose affinity chromatography and the N-terminal amino acid sequence of the enzyme showed no apparent similarity with those of other oxidoreductases.