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Novel Dehalogenase Mechanism for 2,3-Dichloro-1-Propanol Utilization in Pseudomonas putida Strain MC4

Arif, M. I., Samin, G., van Leeuwen, J. G. E., Oppentocht, J. & Janssen, D. B., Sep-2012, In : Applied and environmental microbiology. 78, 17, p. 6128-6136 9 p.

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DOI

A Pseudomonas putida strain (MC4) that can utilize 2,3-dichloro-1-propanol (DCP) and several aliphatic haloacids and haloalcohols as sole carbon and energy source for growth was isolated from contaminated soil. Degradation of DCP was found to start with oxidation and concomitant dehalogenation catalyzed by a 72-kDa monomeric protein (DppA) that was isolated from cell lysate. The dppA gene was cloned from a cosmid library and appeared to encode a protein equipped with a signal peptide and that possessed high similarity to quinohemoprotein alcohol dehydrogenases (ADHs), particularly ADH IIB and ADH IIG from Pseudomonas putida HK. This novel dehalogenating dehydrogenase has a broad substrate range, encompassing a number of nonhalogenated alcohols and haloalcohols. With DCP, DppA exhibited a k(cat) of 17s(-1). H-1 nuclear magnetic resonance experiments indicated that DCP oxidation by DppA in the presence of 2,6-dichlorophenolindophenol (DCPIP) and potassium ferricyanide [K3Fe(CN)(6)] yielded 2-chloroacrolein, which was oxidized to 2-chloroacrylic acid.

Original languageEnglish
Pages (from-to)6128-6136
Number of pages9
JournalApplied and environmental microbiology
Volume78
Issue number17
Publication statusPublished - Sep-2012

    Keywords

  • QUINOHEMOPROTEIN ALCOHOL-DEHYDROGENASE, QUINOPROTEIN ETHANOL DEHYDROGENASE, DEPENDENT ALDEHYDE DEHYDROGENASE, XANTHOBACTER-AUTOTROPHICUS GJ10, HALOALCOHOL DEHALOGENASE, MOLECULAR CHARACTERIZATION, HETEROLOGOUS EXPRESSION, HALOALKANE DEHALOGENASE, COMAMONAS-TESTOSTERONI, ANGSTROM RESOLUTION

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