CRYSTALLINE 3-METHYLASPARTASE FROM A FACULTATIVE ANAEROBE, ESCHERICHIA-COLI STRAIN YG1002

被引：8

作者：

ASANO, Y

KATO, Y

机构：

[1] Biotechnology Research Center, Faculty of Engineering, Toyama Prefectural University, Kosugi, Toyama

来源：

FEMS MICROBIOLOGY LETTERS | 1994年 / 118卷 / 03期

关键词：

3-METHYLASPARTASE; ESCHERICHIA COLI;

D O I：

10.1111/j.1574-6968.1994.tb06837.x

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Crystalline 3-methylaspartase (EC 4.3.1.2) from Escherichia coli strain YG1002 that had been isolated from soil was characterized. The enzyme activity was induced when the organism was grown statically on medium containing (S)-glutamic acid. Its molecular mass is about 84 kDa, and it may be composed of two identical subunits of 42 kDa. The enzyme requires both divalent and monovalent cations such as Mg2+ and K+, respectively. The enzyme catalyzes reversible amination-deamination between mesaconic acid and (2S,3S)-methylaspartic acid, which is the best substrate.

引用

页码：255 / 258

页数：4

共 23 条

[1] ENANTIOSPECIFIC SYNTHESIS OF 3-SUBSTITUTED ASPARTIC ACIDS VIA ENZYMIC AMINATION OF SUBSTITUTED FUMARIC ACIDS [J].