Characterization of two components of the 2-naphthoate monooxygenase system from Burkholderia sp. strain JT1500.

@article{Deng2007CharacterizationOT,
  title={Characterization of two components of the 2-naphthoate monooxygenase system from Burkholderia sp. strain JT1500.},
  author={Daiyong Deng and Xiaobo Li and Xiangping Fang and Guoping Sun},
  journal={FEMS microbiology letters},
  year={2007},
  volume={273 1},
  pages={22-7}
}
2-Naphthoate monooxygenase, a two-protein system, encoded by the nmoA and nmoB genes, was heterologously overexpressed in Escherichia coli. The proteins used for functional characterization were purified to over 90% homogeneity by affinity chromatography. The oxidative component EnmoA (47.9 kDa) lacked substrate catalysis capability on its own, and the reductive component EnmoB (33.4 kDa) and its truncated derivate EnmoB(T) (25 kDa) possessed nearly identical independent flavin reductase… CONTINUE READING