PhanerochaeteV1, Main, Exploration, bibRecord, 000205

Heterologous expression of fungal cytochromes P450 (CYP5136A1 and CYP5136A3) from the white-rot basidiomycete Phanerochaete chrysosporium: Functionalization with cytochrome b5 in Escherichia coli.

Identifieur interne : 000205 ( Main/Exploration ); précédent : 000204; suivant : 000206

Heterologous expression of fungal cytochromes P450 (CYP5136A1 and CYP5136A3) from the white-rot basidiomycete Phanerochaete chrysosporium: Functionalization with cytochrome b5 in Escherichia coli.

Auteurs : Mayumi Hatakeyama [Japon] ; Takuya Kitaoka [Japon] ; Hirofumi Ichinose [Japon]

Source :

Enzyme and microbial technology [ 1879-0909 ] ; 2016.

RBID : pubmed:27233123

Descripteurs français

English descriptors

KwdEn :
- Cytochrome P-450 Enzyme System (genetics), Cytochrome P-450 Enzyme System (metabolism), Cytochromes b5 (genetics), Cytochromes b5 (metabolism), Electron Transport (MeSH), Escherichia coli (genetics), Escherichia coli (metabolism), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Expression (MeSH), Genes, Fungal (MeSH), NADPH-Ferrihemoprotein Reductase (genetics), NADPH-Ferrihemoprotein Reductase (metabolism), Phanerochaete (enzymology), Phanerochaete (genetics), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Xenobiotics (metabolism).
MESH :
- chemical , genetics : Cytochrome P-450 Enzyme System, Cytochromes b5, Fungal Proteins, NADPH-Ferrihemoprotein Reductase, Recombinant Proteins.
- chemical , metabolism : Cytochrome P-450 Enzyme System, Cytochromes b5, Fungal Proteins, NADPH-Ferrihemoprotein Reductase, Recombinant Proteins, Xenobiotics.
- enzymology : Phanerochaete.
- genetics : Escherichia coli, Phanerochaete.
- metabolism : Escherichia coli.
- Electron Transport, Gene Expression, Genes, Fungal.

Abstract

Cytochromes P450 from the white-rot basidiomycete Phanerochaete chrysosporium, CYP5136A1 and CYP5136A3, are capable of catalyzing oxygenation reactions of a wide variety of exogenous compounds, implying their significant roles in the metabolism of xenobiotics by the fungus. It is therefore interesting to explore their biochemistry to better understand fungal biology and to enable the use of fungal enzymes in the biotechnology sector. In the present study, we developed heterologous expression systems for CYP5136A1 and CYP5136A3 using the T7 RNA polymerase/promoter system in Escherichia coli. Expression levels of recombinant P450s were dramatically improved by modifications and optimization of their N-terminal amino acid sequences. A CYP5136A1 reaction system was reconstructed in E. coli whole cells by coexpression of CYP5136A1 and a redox partner, NADPH-dependent P450 reductase (CPR). The catalytic activity of CYP5136A1 was significantly increased when cytochrome b5 (Cyt-b5) was further coexpressed with CPR, indicating that Cyt-b5 supports electron transfer reactions from NAD(P)H to CYP5136A1. Notably, P450 reaction occurred in E. coli cells that harbored CYP5136A1 and Cyt-b5 but not CPR, implying that the reducing equivalents required for the P450 catalytic cycle were transferred via a CPR-independent pathway. Such an "alternative" electron transfer system in CYP5136A1 reaction was also demonstrated using purified enzymes in vitro. The fungal P450 reaction system may be associated with sophisticated electron transfer pathways.

DOI: 10.1016/j.enzmictec.2016.03.004
PubMed: 27233123

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<term>Cytochromes b5 (genetics)</term>
<term>Cytochromes b5 (metabolism)</term>
<term>Electron Transport (MeSH)</term>
<term>Escherichia coli (genetics)</term>
<term>Escherichia coli (metabolism)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Gene Expression (MeSH)</term>
<term>Genes, Fungal (MeSH)</term>
<term>NADPH-Ferrihemoprotein Reductase (genetics)</term>
<term>NADPH-Ferrihemoprotein Reductase (metabolism)</term>
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<term>Cytochrome P-450 enzyme system (métabolisme)</term>
<term>Cytochromes b5 (génétique)</term>
<term>Cytochromes b5 (métabolisme)</term>
<term>Escherichia coli (génétique)</term>
<term>Escherichia coli (métabolisme)</term>
<term>Expression des gènes (MeSH)</term>
<term>Gènes fongiques (MeSH)</term>
<term>NADPH-ferrihemoprotéine reductase (génétique)</term>
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<term>Protéines fongiques (métabolisme)</term>
<term>Protéines recombinantes (génétique)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Transport d'électrons (MeSH)</term>
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<term>NADPH-Ferrihemoprotein Reductase</term>
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<term>Escherichia coli</term>
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<term>Phanerochaete</term>
<term>Protéines fongiques</term>
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<front><div type="abstract" xml:lang="en">Cytochromes P450 from the white-rot basidiomycete Phanerochaete chrysosporium, CYP5136A1 and CYP5136A3, are capable of catalyzing oxygenation reactions of a wide variety of exogenous compounds, implying their significant roles in the metabolism of xenobiotics by the fungus. It is therefore interesting to explore their biochemistry to better understand fungal biology and to enable the use of fungal enzymes in the biotechnology sector. In the present study, we developed heterologous expression systems for CYP5136A1 and CYP5136A3 using the T7 RNA polymerase/promoter system in Escherichia coli. Expression levels of recombinant P450s were dramatically improved by modifications and optimization of their N-terminal amino acid sequences. A CYP5136A1 reaction system was reconstructed in E. coli whole cells by coexpression of CYP5136A1 and a redox partner, NADPH-dependent P450 reductase (CPR). The catalytic activity of CYP5136A1 was significantly increased when cytochrome b5 (Cyt-b5) was further coexpressed with CPR, indicating that Cyt-b5 supports electron transfer reactions from NAD(P)H to CYP5136A1. Notably, P450 reaction occurred in E. coli cells that harbored CYP5136A1 and Cyt-b5 but not CPR, implying that the reducing equivalents required for the P450 catalytic cycle were transferred via a CPR-independent pathway. Such an "alternative" electron transfer system in CYP5136A1 reaction was also demonstrated using purified enzymes in vitro. The fungal P450 reaction system may be associated with sophisticated electron transfer pathways. </div>
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<Abstract><AbstractText>Cytochromes P450 from the white-rot basidiomycete Phanerochaete chrysosporium, CYP5136A1 and CYP5136A3, are capable of catalyzing oxygenation reactions of a wide variety of exogenous compounds, implying their significant roles in the metabolism of xenobiotics by the fungus. It is therefore interesting to explore their biochemistry to better understand fungal biology and to enable the use of fungal enzymes in the biotechnology sector. In the present study, we developed heterologous expression systems for CYP5136A1 and CYP5136A3 using the T7 RNA polymerase/promoter system in Escherichia coli. Expression levels of recombinant P450s were dramatically improved by modifications and optimization of their N-terminal amino acid sequences. A CYP5136A1 reaction system was reconstructed in E. coli whole cells by coexpression of CYP5136A1 and a redox partner, NADPH-dependent P450 reductase (CPR). The catalytic activity of CYP5136A1 was significantly increased when cytochrome b5 (Cyt-b5) was further coexpressed with CPR, indicating that Cyt-b5 supports electron transfer reactions from NAD(P)H to CYP5136A1. Notably, P450 reaction occurred in E. coli cells that harbored CYP5136A1 and Cyt-b5 but not CPR, implying that the reducing equivalents required for the P450 catalytic cycle were transferred via a CPR-independent pathway. Such an "alternative" electron transfer system in CYP5136A1 reaction was also demonstrated using purified enzymes in vitro. The fungal P450 reaction system may be associated with sophisticated electron transfer pathways. </AbstractText>
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<Keyword MajorTopicYN="N">Cytochrome b(5)</Keyword>
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<settlement><li>Fukuoka</li>
</settlement>
<orgName><li>Université de Kyūshū</li>
</orgName>
</list>
<tree><country name="Japon"><region name="Kyūshū"><name sortKey="Hatakeyama, Mayumi" sort="Hatakeyama, Mayumi" uniqKey="Hatakeyama M" first="Mayumi" last="Hatakeyama">Mayumi Hatakeyama</name>
</region>
<name sortKey="Ichinose, Hirofumi" sort="Ichinose, Hirofumi" uniqKey="Ichinose H" first="Hirofumi" last="Ichinose">Hirofumi Ichinose</name>
<name sortKey="Kitaoka, Takuya" sort="Kitaoka, Takuya" uniqKey="Kitaoka T" first="Takuya" last="Kitaoka">Takuya Kitaoka</name>
</country>
</tree>
</affiliations>
</record>

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   |wiki=    Bois
   |area=    PhanerochaeteV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:27233123
   |texte=   Heterologous expression of fungal cytochromes P450 (CYP5136A1 and CYP5136A3) from the white-rot basidiomycete Phanerochaete chrysosporium: Functionalization with cytochrome b5 in Escherichia coli.
}}

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	Serveur d'exploration sur le phanerochaete
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Serveur d'exploration sur le phanerochaete

Heterologous expression of fungal cytochromes P450 (CYP5136A1 and CYP5136A3) from the white-rot basidiomycete Phanerochaete chrysosporium: Functionalization with cytochrome b5 in Escherichia coli.

Heterologous expression of fungal cytochromes P450 (CYP5136A1 and CYP5136A3) from the white-rot basidiomycete Phanerochaete chrysosporium: Functionalization with cytochrome b5 in Escherichia coli.

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