Engineering the substrate specificity of Bacillus megaterium cytochrome P-450 BM3: hydroxylation of alkyl trimethylammonium compounds.

  title={Engineering the substrate specificity of Bacillus megaterium cytochrome P-450 BM3: hydroxylation of alkyl trimethylammonium compounds.},
  author={Catherine F. Oliver and Sandeep P. Modi and William Ure Primrose and Lu Yun. Lian and Gordon C. K. Roberts},
  journal={The Biochemical journal},
  volume={327 ( Pt 2)},
Oligonucleotide-directed mutagenesis has been used to replace arginine-47 with glutamate in cytochrome P-450 BM3 from Bacillus megaterium and in its haem domain. The mutant has been characterized by sequencing, mass spectrometry, steady-state kinetics and by optical and NMR measurements of substrate binding. The mutant retains significant catalytic activity towards C12-C16 fatty acids, catalysing hydroxylation in the same (omega-1, omega-2, omega-3) positions with kcat/Km values a factor of 14… 

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Cytochrome P-450
ing species placed symmetrically between the endo and exo hydrogens could result in a G value of I, with subsequent asymmetric placement of the oxygen atom selectively at the exo face. The
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