RT Journal Article SR Electronic(1) A1 Smith, Judith M. A1 Harrison, Karen A1 Colby, JohnYR 1990 T1 Purification and characterization of d-2-haloacid dehalogenase from Pseudomonas putida strain AJ1/23 JF Microbiology, VO 136 IS 5 SP 881 OP 886 DO https://doi.org/10.1099/00221287-136-5-881 PB Microbiology Society, SN 1465-2080, AB 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., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-136-5-881