1887

Abstract

A -2-haloacid dehalogenase was isolated and purified to homogeneity from strain AJ1/23. The enzyme catalysed the stereospecific dehalogenation of the -isomer of 2-chloropropionate. Using a new ionchromatograph 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 of about 135000 and appears to be composed of four subunits of identical .

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1990-05-01
2021-10-19
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