| Literature DB >> 2380688 |
J M Smith1, K Harrison, J Colby.
Abstract
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 degrees C and the enzyme was insensitive to most -SH reagents. The enzyme has an Mr of about 135,000 and appears to be composed of four subunits of identical Mr.Entities:
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Year: 1990 PMID: 2380688 DOI: 10.1099/00221287-136-5-881
Source DB: PubMed Journal: J Gen Microbiol ISSN: 0022-1287