Directed evolution of the fatty-acid hydroxylase P450 BM-3 into an indole-hydroxylating catalyst.

@article{Li2000DirectedEO,
  title={Directed evolution of the fatty-acid hydroxylase P450 BM-3 into an indole-hydroxylating catalyst.},
  author={Q. S. Li and U. Schwaneberg and P. Fischer and R. Schmid},
  journal={Chemistry},
  year={2000},
  volume={6 9},
  pages={
          1531-6
        }
}
The self-sufficient cytochrome P450 BM-3 enzyme from Bacillus megaterium catalyzes subterminal hydroxylation of saturated long-chain fatty acids and structurally related compounds. Since the primary structure of P450 BM-3 is homologous to that of mammalian P450 type II, it represents an excellent model for this family of enzymes. During studies on the directed evolution of P450 BM-3 into a medium-chain fatty-acid hydroxylase, several mutants, in particular the triple mutant Phe87Val, Leu188Gln… Expand
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