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

Noriyuki Kasai, Shin ichi Ikushiro, Shinji Hirosue, Akira Arisawa, Hirofumi Ichinose, Hiroyuki Wariishi, Miho Ohta, Toshiyuki Sakaki

研究成果: ジャーナルへの寄稿記事

18 引用 (Scopus)

抄録

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.

元の言語英語
ページ(範囲)103-108
ページ数6
ジャーナルBiochemical and Biophysical Research Communications
387
発行部数1
DOI
出版物ステータス出版済み - 9 11 2009

Fingerprint

Phanerochaete
Hydroxylation
Fungi
Yeast
Cytochrome P-450 Enzyme System
Saccharomyces cerevisiae
Cytochrome P-450 CYP1A2
NADPH-Ferrihemoprotein Reductase
Environmental Biodegradation
Sequence Alignment
Cytochromes
Bioconversion
Functional analysis
Bioremediation
Protein Isoforms
Molecular mass
Complementary DNA
Yeasts
Pharmacology
Amino Acids

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Enzymatic properties of cytochrome P450 catalyzing 3′-hydroxylation of naringenin from the white-rot fungus Phanerochaete chrysosporium. / Kasai, Noriyuki; Ikushiro, Shin ichi; Hirosue, Shinji; Arisawa, Akira; Ichinose, Hirofumi; Wariishi, Hiroyuki; Ohta, Miho; Sakaki, Toshiyuki.

:: Biochemical and Biophysical Research Communications, 巻 387, 番号 1, 11.09.2009, p. 103-108.

研究成果: ジャーナルへの寄稿記事

Kasai, Noriyuki ; Ikushiro, Shin ichi ; Hirosue, Shinji ; Arisawa, Akira ; Ichinose, Hirofumi ; Wariishi, Hiroyuki ; Ohta, Miho ; Sakaki, Toshiyuki. / Enzymatic properties of cytochrome P450 catalyzing 3′-hydroxylation of naringenin from the white-rot fungus Phanerochaete chrysosporium. :: Biochemical and Biophysical Research Communications. 2009 ; 巻 387, 番号 1. pp. 103-108.
@article{8c3b44adcf684423b2a60a720eb4f1ef,
title = "Enzymatic properties of cytochrome P450 catalyzing 3′-hydroxylation of naringenin from the white-rot fungus Phanerochaete chrysosporium",
abstract = "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.",
author = "Noriyuki Kasai and Ikushiro, {Shin ichi} and Shinji Hirosue and Akira Arisawa and Hirofumi Ichinose and Hiroyuki Wariishi and Miho Ohta and Toshiyuki Sakaki",
year = "2009",
month = "9",
day = "11",
doi = "10.1016/j.bbrc.2009.06.134",
language = "English",
volume = "387",
pages = "103--108",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Enzymatic properties of cytochrome P450 catalyzing 3′-hydroxylation of naringenin from the white-rot fungus Phanerochaete chrysosporium

AU - Kasai, Noriyuki

AU - Ikushiro, Shin ichi

AU - Hirosue, Shinji

AU - Arisawa, Akira

AU - Ichinose, Hirofumi

AU - Wariishi, Hiroyuki

AU - Ohta, Miho

AU - Sakaki, Toshiyuki

PY - 2009/9/11

Y1 - 2009/9/11

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=67651030007&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=67651030007&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2009.06.134

DO - 10.1016/j.bbrc.2009.06.134

M3 - Article

C2 - 19576179

AN - SCOPUS:67651030007

VL - 387

SP - 103

EP - 108

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -