Enhanced electron transfer and lauric acid hydroxylation by site-directed mutagenesis of CYP119.

@article{Koo2002EnhancedET,
  title={Enhanced electron transfer and lauric acid hydroxylation by site-directed mutagenesis of CYP119.},
  author={Laura S. Koo and Chad E. Immoos and Michael S Cohen and Patrick J Farmer and Paul R. Ortiz de Montellano},
  journal={Journal of the American Chemical Society},
  year={2002},
  volume={124 20},
  pages={
          5684-91
        }
}
CYP119, a cytochrome P450 from a thermophilic organism for which a crystal structure is available, is shown here to hydroxylate lauric acid in a reaction supported by putidaredoxin and putidaredoxin reductase. This fatty acid hydroxylation activity is increased 15-fold by T214V and D77R mutations. The T214V mutation increases the rate by facilitating substrate binding and enhancing the associated spin state change, whereas the D77R mutation improves binding of the heterologous redox partner… CONTINUE READING

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