Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:flavin adenine dinucleotide oxidoreductase (TftC) of Burkholderia cepacia AC1100.

@article{Gisi2003CharacterizationOC,
  title={Characterization of chlorophenol 4-monooxygenase (TftD) and NADH:flavin adenine dinucleotide oxidoreductase (TftC) of Burkholderia cepacia AC1100.},
  author={Michelle R Gisi and Luying Xun},
  journal={Journal of bacteriology},
  year={2003},
  volume={185 9},
  pages={
          2786-92
        }
}
Burkholderia cepacia AC1100 uses 2,4,5-trichlorophenoxyacetic acid, an environmental pollutant, as a sole carbon and energy source. Chlorophenol 4-monooxygenase is a key enzyme in the degradation of 2,4,5-trichlorophenoxyacetic acid, and it was originally characterized as a two-component enzyme (TftC and TftD). Sequence analysis suggests that they are separate enzymes. The two proteins were separately produced in Escherichia coli, purified, and characterized. TftC was an NADH:flavin adenine… CONTINUE READING

Citations

Publications citing this paper.
SHOWING 1-10 OF 33 CITATIONS

References

Publications referenced by this paper.
SHOWING 1-10 OF 48 REFERENCES

Similar Papers

Loading similar papers…