Global incorporation of norleucine in place of methionine in cytochrome P450 BM‐3 heme domain increases peroxygenase activity

@article{Cirino2003GlobalIO,
  title={Global incorporation of norleucine in place of methionine in cytochrome P450 BM‐3 heme domain increases peroxygenase activity},
  author={Patrick C Cirino and Yi Tang and Katsuyuki Takahashi and David A. Tirrell and Frances H. Arnold},
  journal={Biotechnology and Bioengineering},
  year={2003},
  volume={83}
}
In this study we have replaced all 13 methionine residues in the cytochrome P450 BM‐3 heme domain (463 amino acids) with the isosteric methionine analog norleucine. This experiment has provided a means of testing the functional limits of globally incorporating into an enzyme an unnatural amino acid in place of its natural analog, and also an efficient way to test whether inactivation during peroxide‐driven P450 catalysis involves methionine oxidation. Although there was no increase in the… 
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