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Initial characterisation of 4-chlorobenzoate dehalogenase from Pseudomonas sp. CBS3
Affiliation:1. Department of Chemistry and Biochemistry, Loyola University Chicago, Chicago, Illinois, USA;2. Department of Chemistry, Marquette University, Milwaukee, Wisconsin, USA;3. Department of Physics, Marquette University, Milwaukee, Wisconsin, USA;4. Department of Chemistry, Colorado School of Mines, Golden, Colorado, USA
Abstract:Extracts of Pseudomonas sp. CBS3 converted 4-chlorobenzoate into 4-hydroxybenzoate. The enzyme responsible for this conversion was enriched by ammonium sulphate fractionation (30–60% saturation, 1.3-fold). The optimum conditions for the reaction were 30–35°C and pH 7–7.5. The enzyme was activated by Mn2+ (1 mM final concentration) up to 120-fold, and by Co2+ (1 mM final concentration) up to 60-fold. Other divalent ions had no effect. EDTA inhibited the enzyme. 4-Bromobenzoate and 4-iodobenzoate were substrates for the enzyme, but 4-fluorobenzoate was not converted.
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