PURIFICATION AND CHARACTERIZATION OF D-2-HALOACID DEHALOGENASE FROM PSEUDOMONAS-PUTIDA STRAIN AJ1/23

被引：55

作者：

SMITH, JM

HARRISON, K

COLBY, J

机构：

来源：

JOURNAL OF GENERAL MICROBIOLOGY | 1990年 / 136卷

关键词：

D O I：

10.1099/00221287-136-5-881

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

A D-2 haloacid dehalogenase was isolated and purified to homogeneity from Pseudomonas putida strain AJ1/23. The enzyme catalysed the stereospecific dehalogenation of the D-isomer of 2-chloropropionate. Using a new ion-chromatograph assay, the enzyme was found to catalyse the dehalogenation of short-chain 2-halocarboxylic acids. Maximum enzyme activity occurred at pH 9.5 and 50°C and the enzyme was insensitive to most -SH reagents. The enzyme has an M(r) of about 135000 and appears to be composed of four subunits of identical M(r).

引用

页码：881 / 886

页数：6

共 19 条

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