Purification and characterization of D-2-haloacid dehalogenase from Pseudomonas putida strain AJ1/23.
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.
Smith
J M
JM
School of Biology, Sunderland Polytechnic, UK.
Harrison
K
K
Colby
J
J
D006843:Hydrocarbons, Chlorinated; D006863:Hydrogen-Ion Concentration; D006867:Hydrolases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D007526:Isoelectric Point; D007700:Kinetics; D008970:Molecular Weight; D011422:Propionates; D011549:Pseudomonas / Q000201:enzymology*; D013237:Stereoisomerism; D013379:Substrate Specificity; D013696:Temperature
D006843:Hydrocarbons, Chlorinated; D011422:Propionates; C021974:2-chloropropionic acid; D006867:Hydrolases; C034507:2-haloacid dehalogenase