Production and characterization of the recombinant Sphingomonas chlorophenolica pentachlorophenol 4-monooxygenase.

@article{Wang2001ProductionAC,
  title={Production and characterization of the recombinant Sphingomonas chlorophenolica pentachlorophenol 4-monooxygenase.},
  author={Hong Wang and Marja Annika Tiirola and Jaakko A. Puhakka and Markku S. Kulomaa},
  journal={Biochemical and biophysical research communications},
  year={2001},
  volume={289 1},
  pages={161-6}
}
Pentachlorophenol 4-monooxygenase (PCP4MO) from Sphingomonas chlorophenolica is a flavoprotein that hydroxylates PCP in the presence of NADPH and oxygen. In order to investigate the structure and function of active site, recombinant PCP4MO (rePCP4MO) was produced in Escherichia coli as a glutathione S-transferase (GST) fusion protein. Moreover, a tobacco etch virus (TEV) protease cleavage site (EKLYFQG) was introduced into GST-PCP4MO and a his-tagged TEV protease was employed. Hence, a two-step… CONTINUE READING