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.
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.
Liu
J Q
JQ
Laboratory of Biocatalytic Chemistry, Toyama Prefectural University, Japan.
Odani
M
M
Dairi
T
T
Itoh
N
N
Shimizu
S
S
Yamada
H
H
D000900:Anti-Bacterial Agents / Q000096:biosynthesis*; D003001:Cloning, Molecular; D004926:Escherichia coli; D012696:Glycine Hydroxymethyltransferase / Q000235:genetics / Q000378:metabolism*; D011401:Promoter Regions, Genetic; D012694:Serine / Q000031:analogs & derivatives* / Q000378:metabolism; D013839:Thiamphenicol / Q000031:analogs & derivatives / Q000378:metabolism
C120473:3-(4-(methylthio)phenylserine); D000900:Anti-Bacterial Agents; D012694:Serine; C035534:florfenicol; D012696:Glycine Hydroxymethyltransferase; D013839:Thiamphenicol