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A monobromoacetate dehalogenase from Pseudomonas cepacia MBA4

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Abstract

Pseudomonas cepacia MBA4 able to utilize monobromoacetic acid as a sole source of carbon and energy was isolated from soil by enrichment culture. In batch culture the ability to utilize the substrate was conferred by a single halidohydrolase-type dehalogenase which demonstrated a high activity towards the enrichment substrate. The purified enzyme, designated as dehalogenase IVa by activity-stain polyacrylamide gel electrophoresis, had a relative molecular weight of 45,000 and was comprised of two electrophoretically identical subunits with relative molecular weights of 23,000. Dehalogenase IVa demonstrated isomer specificity, being active towards the L-isomer of 2-monochloropropionic acid only. The significance of activity-stain polyacrylamide gel electrophoresis in characterizing dehalogenases and their ubiquitous distribution among bacterial genera are discussed.

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Abbreviations

MCA:

Monochloroacetic acid

DCA:

dichloroacetic acid

MBA:

monobromoacetic acid

2MPCA:

2-monochloropropionic acid

2MBPA:

2-monobromopropionic acid

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Tsang, J.S.H., Sallis, P.J., Bull, A.T. et al. A monobromoacetate dehalogenase from Pseudomonas cepacia MBA4. Arch. Microbiol. 150, 441–446 (1988). https://doi.org/10.1007/BF00422284

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  • DOI: https://doi.org/10.1007/BF00422284

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