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 Microbiol Biotechnol. 1999 May;51(5):586-91. doi: 10.1007/s002530051436.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / biosynthesis*
  • Cloning, Molecular
  • Escherichia coli
  • Glycine Hydroxymethyltransferase / genetics
  • Glycine Hydroxymethyltransferase / metabolism*
  • Promoter Regions, Genetic
  • Serine / analogs & derivatives*
  • Serine / metabolism
  • Thiamphenicol / analogs & derivatives
  • Thiamphenicol / metabolism


  • 3-(4-(methylthio)phenylserine)
  • Anti-Bacterial Agents
  • Serine
  • florfenicol
  • Glycine Hydroxymethyltransferase
  • Thiamphenicol