Diversity of microbial threonine aldolases and their application

被引：55

作者：

Liu, JQ

Dairi, T

Itoh, N

Kataoka, M

Shimizu, S

Yamada, H

机构：

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

[2] Kyoto Univ, Grad Sch Agr, Div Appl Life Sci, Kyoto 6068502, Japan

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2000年 / 10卷 / 1-3期

关键词：

threonine aldolase; beta-hydroxy-alpha-amino acid; enzymatic resolution; stereoselective synthesis;

D O I：

10.1016/S1381-1177(00)00118-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Threonine aldolase catalyzes the reversible interconversion of certain beta-hydroxy-alpha-amino acids and glycine plus the corresponding aldehydes. Various microbial threonine aldolases with different stereospecificities were found on extensive screening, and the genes encoding the proteins were cloned and heterogeneously overexpressed in Escherichia coli. By using recombinant threonine aldolases, an enzymatic resolution process was established for the production of optically pure P-hydroxy-a-amino acids. In addition, the threonine aldolase-catalyzed direct synthesis of beta-hydroxy-alpha-amino acid from aldehyde and glycine is discussed. (C) 2000 Elsevier Science B.V. Al rights reserved.

引用

页码：107 / 115

页数：9

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[1] ISSUES IN SEARCHING MOLECULAR SEQUENCE DATABASES [J].