Enzymatic properties of cytochrome P450 catalyzing 3'-hydroxylation of naringenin from the white-rot fungus Phanerochaete chrysosporium.

@article{Kasai2009EnzymaticPO,
  title={Enzymatic properties of cytochrome P450 catalyzing 3'-hydroxylation of naringenin from the white-rot fungus Phanerochaete chrysosporium.},
  author={Noriyuki Kasai and Shin-ichi Ikushiro and Shinji Hirosue and Akira Arisawa and Hirofumi Ichinose and Hiroyuki Wariishi and Miho Ohta and Toshiyuki Sakaki},
  journal={Biochemical and biophysical research communications},
  year={2009},
  volume={387 1},
  pages={
          103-8
        }
}
We cloned full-length cDNAs of more than 130 cytochrome P450s (P450s) derived from Phanerochaete chrysosporium, and successfully expressed 70 isoforms using a co-expression system of P. chrysosporium P450 and yeast NADPH-P450 reductase in Saccharomyces cerevisiae. Of these P450s, a microsomal P450 designated as PcCYP65a2 consists of 626 amino acid residues with a molecular mass of 68.3kDa. Sequence alignment of PcCYP65a2 and human CYP1A2 revealed a unique structure of PcCYP65a2. Functional… CONTINUE READING

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