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 Escherichia coli 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.
CITATION STYLE
Liu, J. Q., Odani, M., Dairi, T., Itoh, N., Shimizu, S., & Yamada, H. (1999). 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. Applied Microbiology and Biotechnology, 51(5), 586–591. https://doi.org/10.1007/s002530051436
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