Makdessi K, Lechner U
Institut für Mikrobiologie, Martin-Luther-Universität Halle-Wittenberg, Halle, Germany.
FEMS Microbiol Lett. 1997 Dec 1;157(1):95-101. doi: 10.1111/j.1574-6968.1997.tb12758.x.
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.
