Purification and properties of a plasmid-encoded 2,4-dichlorophenol hydroxylase.

@article{Liu1984PurificationAP,
  title={Purification and properties of a plasmid-encoded 2,4-dichlorophenol hydroxylase.},
  author={T Liu and Peter J. Chapman},
  journal={FEBS letters},
  year={1984},
  volume={173 2},
  pages={314-8}
}
2,4-Dichlorophenol hydroxylase, an enzyme involved in the bacterial degradation of the herbicide 2,4-dichlorophenoxyacetate (2,4-D) was purified from two bacterial strains that harbored the same 2,4-D plasmid, pJP4. The purified enzymes (Mr 224 000) from the two transconjugants were indistinguishable; they contained FAD and were composed of non-identical subunits, Mr 67 000 and 45 000, respectively. Various substituted phenols were hydroxylated, using either NADH or NADPH. The amino acid… CONTINUE READING

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