Structure of mammalian cytochrome P450 2C5 complexed with diclofenac at 2.1 A resolution: evidence for an induced fit model of substrate binding.

@article{Wester2003StructureOM,
  title={Structure of mammalian cytochrome P450 2C5 complexed with diclofenac at 2.1 A resolution: evidence for an induced fit model of substrate binding.},
  author={Michael R. Wester and Eric F Johnson and Cristina Marques-Soares and Sylvie Dijols and Patrick M Dansette and Daniel Mansuy and Charles David Stout},
  journal={Biochemistry},
  year={2003},
  volume={42 31},
  pages={9335-45}
}
The structure of the anti-inflammatory drug diclofenac bound in the active site of rabbit microsomal cytochrome P450 2C5/3LVdH was determined by X-ray crystallography to 2.1 A resolution. P450 2C5/3LVdH and the related enzyme 2C5dH catalyze the 4'-hydroxylation of diclofenac with apparent K(m) values of 80 and 57 microM and k(cat) values of 13 and 16 min(-1), respectively. Spectrally determined binding constants are similar to the K(m) values. The structure indicates that the pi-electron system… CONTINUE READING

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