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

被引:27
作者
Kasai, Noriyuki [1 ]
Ikushiro, Shin-ichi [1 ]
Hirosue, Shinji [2 ]
Arisawa, Akira [2 ]
Ichinose, Hirofumi [3 ]
Wariishi, Hiroyuki [3 ]
Ohta, Miho [4 ]
Sakaki, Toshiyuki [1 ]
机构
[1] Toyama Prefectural Univ, Fac Engn, Dept Biotechnol, Toyama 9390398, Japan
[2] Mercian Corp, Bioresource Labs, Iwata, Shizuoka, Japan
[3] Kyushu Univ, Grad Sch Bioresource & Bioenvironm Sci, Dept Forest & Forest Prod Sci, Fukuoka 8128581, Japan
[4] Soai Univ, Suminoe Ku, Osaka 5590033, Japan
关键词
Cytochrome P450; P; chrysosporium; Naringenin hydroxylation; Dioxin; DIETARY FLAVONOIDS; IN-VITRO; ESTROGENIC FLAVONOIDS; CYP1A SUBFAMILY; RAT; ERIODICTYOL; METABOLISM; ANTIOXIDANTS; OXIDATION; ENZYMES;
D O I
10.1016/j.bbrc.2009.06.134
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:103 / 108
页数:6
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