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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 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 M r of about 135000 and appears to be composed of four subunits of identical M r.
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