Functional characterization of cytochromes P450 2B from the desert woodrat Neotoma lepida.

@article{Wilderman2014FunctionalCO,
  title={Functional characterization of cytochromes P450 2B from the desert woodrat Neotoma lepida.},
  author={P Ross Wilderman and Hyun-Hee Jang and Jael R. Malenke and Mariam Nader Salib and Elisabeth Angermeier and Sonia Lamime and M. Denise Dearing and James R. Halpert},
  journal={Toxicology and applied pharmacology},
  year={2014},
  volume={274 3},
  pages={
          393-401
        }
}
Mammalian detoxification processes have been the focus of intense research, but little is known about how wild herbivores process plant secondary compounds, many of which have medicinal value or are drugs. cDNA sequences that code for three enzymes of the cytochrome P450 (CYP) 2B subfamily, here termed 2B35, 2B36, and 2B37 have been recently identified from a wild rodent, the desert woodrat (Malenke et al., 2012). Two variant clones of each enzyme were engineered to increase protein solubility… CONTINUE READING
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