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Applied Microbiology and Biotechnology

, Volume 51, Issue 5, pp 586–591 | Cite as

A new route to l-threo-3-[4-(methylthio)phenylserine], a key intermediate for the synthesis of antibiotics: recombinant low-specificity d-threonine aldolase-catalyzed stereospecific resolution

  • J. Q. Liu
  • M. Odani
  • T. Dairi
  • N. Itoh
  • S. Shimizu
  • H. Yamada
ORIGINAL PAPER

Abstract

A new enzymatic resolution process was established for the production of l-threo-3-[4-(methylthio)phenylserine] (MTPS), an intermediate for synthesis of antibiotics, florfenicol and thiamphenicol, using the recombinant low-specificity d-threonine aldolase from Arthrobacter sp. DK-38. Chemically synthesized dl-threo-MTPS was efficiently resolved with either the purified enzyme or the intact recombinant Escherichiacoli cells overproducing the enzyme. Under the optimized experimental conditions, 100 mM (22.8 g l−1) l-threo-MTPS was obtained from 200 mM (45.5 g l−1) dl-threo-MTPS, with a molar yield of 50% and a 99.6% enantiomeric excess.

Keywords

Enzyme Escherichiacoli Aldolase Arthrobacter Enantiomeric Excess 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1999

Authors and Affiliations

  • J. Q. Liu
    • 1
  • M. Odani
    • 1
  • T. Dairi
    • 1
  • N. Itoh
    • 1
  • S. Shimizu
    • 2
  • H. Yamada
    • 1
  1. 1.Laboratory of Biocatalytic Chemistry, Biotechnology Research Center, Toyama Prefectural University, Kurokawa 5180, Kosugi-Machi, Toyama, 939-0398 Japan e-mail: ryu@putoyama.ac.jp Tel.: +81-766-567500 Fax: +81-766-562498JP
  2. 2.Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, JapanJP

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