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

Authors
Liu, JQ Odani, M Dairi, T Itoh, N Shimizu, S Yamada, H
Citation
Jq. Liu et al., 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, APPL MICR B, 51(5), 1999, pp. 586-591
Citations number
22
Categorie Soggetti
Biotecnology & Applied Microbiology",Microbiology
Journal title
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
ISSN journal
01757598 → ACNP
Volume
51
Issue
5
Year of publication
1999
Pages
586 - 591
Database
ISI
SICI code
0175-7598(199905)51:5<586:ANRTLA>2.0.ZU;2-7
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-sp ecificity D-threonine aldolase from Arthrobacter sp. DK-38. Chemically synt hesized DL-threo-MTPS was efficiently resolved with either the purified enz yme or the intact recombinant Escherichia coli cells overproducing the enzy me. Under the optimized experimental conditions, 100 mM (22.8 g l(-1)) L-th reo-MTPS was obtained from 200 mM (45.5 g l(-1)) DL-threo-MTPS, with a mola r yield of 50% and a 99.6% enantiomeric excess.