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  • Title: Purification and characterization of 2,4-dichlorophenol hydroxylase isolated from a bacterium of the alpha-2 subgroup of the Proteobacteria.
    Author: Makdessi K, Lechner U.
    Journal: FEMS Microbiol Lett; 1997 Dec 01; 157(1):95-101. PubMed ID: 9418244.
    Abstract:
    2,4-Dichlorophenol hydroxylase (EC 1.14.13.20) was purified to apparent homogeneity from the bacterial strain S1, a member of the alpha-2 subgroup of the Proteobacteria. The molecular masses of the native enzyme and the subunit were determined to be 256 and 64 kDa, respectively, suggesting a homotetrameric structure. The enzyme converted 2,4-dichlorophenol to 3,5-dichlorocatechol. The apparent K(m) values for 2,4-dichlorophenol, NADPH and NADH were 3, 240 and 420 microM, respectively. The enzyme hydroxylated a broad range of halogenated phenols. 3-Chloro-, 2,6-dichloro- and 2,4,6-trichlorophenol acted as 'non-substrate' effectors. The N-terminal sequence revealed 72% identity with the amino acid sequence deduced from the pJP4-encoded tfdB gene.
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