Enzymatic properties of cytochrome P450 catalyzing 3′-hydroxylation of naringenin from the white-rot fungus Phanerochaete chrysosporium
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- 作者：Noriyuki Kasai ; Shin-ichi Ikushiro ; Shinji Hirosue ; Akira Arisawa ; Hirofumi Ichinose ; Hiroyuki Wariishi ; Miho Ohta ; Toshiyuki Sakaki
- 关键词：Cytochrome P450 ; P. chrysosporium ; Naringenin hydroxylation ; Dioxin
- 刊名：Biochemical and Biophysical Research Communications
- 出版年：2009
- 出版时间：11 September 2009
- 年：2009
- 卷：387
- 期：1
- 页码：103-108
- 全文大小：322 K
文摘
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 68.3 kDa. Sequence alignment of PcCYP65a2 and human CYP1A2 revealed a unique structure of PcCYP65a2. Functional analysis of PcCYP65a2 using the recombinant S. cerevisiae cells demonstrated that this P450 catalyzes 3′-hydroxylation of naringenin to yield eriodictyol, which has various biological and pharmacological properties. In addition, the recombinant S. cerevisiae cells expressing PcCYP65a2 metabolized such polyaromatic compounds as dibenzo-p-dioxin (DD), 2-monochloroDD, biphenyl, and naphthalene. These results suggest that PcCYP65a2 is practically useful for both bioconversion and bioremediation.