ORIGINAL PAPER

Applied Microbiology and Biotechnology

, Volume 51, Issue 5, pp 586-591

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. LiuAffiliated withLaboratory 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: +81-766-562498
  • , M. OdaniAffiliated withLaboratory 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: +81-766-562498
  • , T. DairiAffiliated withLaboratory 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: +81-766-562498
  • , N. ItohAffiliated withLaboratory 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: +81-766-562498
  • , S. ShimizuAffiliated withDivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Japan
  • , H. YamadaAffiliated withLaboratory 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: +81-766-562498

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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.