2-Haloacid Dehalogenase from a 4-Chlorobenzoate-DegradingPseudomonas spec.CBS 3
Authors:
- Uwe KlagesUKUwe Klages
- Susanne KraussSKSusanne Krauss
- Franz LingensFLFranz Lingens
- 1 January 1983
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 364 (1) , 529-536
Abstract
Pseudomonas CBS 3 contains a 2-haloacid dehalogenase induced by chloroacetate. The enzyme was purified .apprx. 25-fold to electrophoretic homogeneity by ammonium sulfate fractionation, hydroxyapatite, DEAE-cellulose and gel filtration. The relative MW as determined by Sephadex G-75 gel filtration and dodecyl sulfate polyacrylamide gel electrophoresis, were 41,000 and 28,000, respectively. The enzyme dehalogenated all monohaloacetates, except fluoroacetate. Low activities were found against dichloroacetate and 2,2-dichloropropionate. The enzyme was inactive against trichloroacetate and 3-chloropropionate; it catalyzed the stereospecific dehalogenation of L-2-chloropropionate to D-lactate, the rate of dehalogenation being .apprx. 20% of the rate of chloroacetate dechlorination. The enzyme activity was not affected by chelating agents and thiol reagents.Keywords
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