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 |
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| Authors: | J Q Liu M Odani T Dairi N Itoh S Shimizu H Yamada |
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| Institution: | (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: +81-766-562498, JP;(2) Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Japan, JP |
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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.
Received: 2 September 1998 / Received revision: 27 October 1998 / Accepted: 29 November 1998 |
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