Enzymatic properties of cytochrome P450 catalyzing 3′-hydroxylation of naringenin from the white-rot fungus Phanerochaete chrysosporium
Enzymatic properties of cytochrome P450 catalyzing 3′-hydroxylation of naringenin from the white-rot fungus Phanerochaete chrysosporium
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DOI：
10.1016/j.bbrc.2009.06.134
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发表时间：
2009-09-11
影响因子：
3.1
通讯作者：
Sakaki, Toshiyuki
中科院分区：
文献类型：
--
作者：
Kasai, Noriyuki;Ikushiro, Shin-ichi;Sakaki, Toshiyuki
我们克隆了130多个黄孢原毛平革菌细胞色素P450（P450）的全长cDNA，并利用黄孢原毛平革菌P450和酵母NADPH-P450还原酶共表达系统在酿酒酵母中成功表达了70个P450亚型。在这些P450中，被命名为PcCYP 65 a2的微粒体P450由626个氨基酸残基组成，分子量为68.3 kDa。PcCYP 65 a2和人CYP 1A 2的序列比对揭示了PcCYP 65 a2的独特结构。利用重组S.酿酒酵母细胞证明，该11450催化柚皮素的3 ′-羟基化以产生圣草酚，圣草酚具有多种生物学和药理学性质。此外，重组S.表达PcCYP 65 a2的酿酒酵母细胞代谢诸如二苯并-p-二恶英（DD）、2-一氯DD、联苯和萘的多环芳香族化合物。这些结果表明PcCYP 65 a2在生物转化和生物修复中具有实用价值。(C)2009 Elsevier Inc. All rights reserved.
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 11450 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. (C) 2009 Elsevier Inc. All rights reserved.