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

被引：54
|
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).
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页码：881 / 886
页数：6
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