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

被引：28

作者：

Liu, JQ

Odani, M

Dairi, T

Itoh, N

Shimizu, S

Yamada, H

机构：

[1] Toyama Prefectural Univ, Biotechnol Res Ctr, Lab Biocatalyt Chem, Kosugi Machi, Toyama 9390398, Japan

[2] Kyoto Univ, Grad Sch Agr, Div Appl Life Sci, Kyoto, Japan

来源：

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY | 1999年 / 51卷 / 05期

关键词：

D O I：

10.1007/s002530051436

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

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.

引用

页码：586 / 591

页数：6

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