Structural comparison of cytochromes P450 2A6, 2A13, and 2E1 with pilocarpine.

@article{DeVore2012StructuralCO,
  title={Structural comparison of cytochromes P450 2A6, 2A13, and 2E1 with pilocarpine.},
  author={Natasha M. DeVore and Kathleen M. Meneely and Aaron G Bart and Eva S. Stephens and Kevin P. Battaile and Emily E Scott},
  journal={The FEBS journal},
  year={2012},
  volume={279 9},
  pages={1621-31}
}
Human xenobiotic-metabolizing cytochrome P450 (CYP) enzymes can each bind and monooxygenate a diverse set of substrates, including drugs, often producing a variety of metabolites. Additionally, a single ligand can interact with multiple CYP enzymes, but often the protein structural similarities and differences that mediate such overlapping selectivity are not well understood. Even though the CYP superfamily has a highly canonical global protein fold, there are large variations in the active… CONTINUE READING
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