Enzymatic properties of cytochrome P450 catalyzing 3'-hydroxylation of naringenin from the white-rot fungus Phanerochaete chrysosporium.
Identifieur interne : 000634 ( Main/Exploration ); précédent : 000633; suivant : 000635Enzymatic properties of cytochrome P450 catalyzing 3'-hydroxylation of naringenin from the white-rot fungus Phanerochaete chrysosporium.
Auteurs : Noriyuki Kasai [Japon] ; Shin-Ichi Ikushiro ; Shinji Hirosue ; Akira Arisawa ; Hirofumi Ichinose ; Hiroyuki Wariishi ; Miho Ohta ; Toshiyuki SakakiSource :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2009.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Catalyse (MeSH), Clonage moléculaire (MeSH), Cytochrome P-450 enzyme system (composition chimique), Cytochrome P-450 enzyme system (génétique), Cytochrome P-450 enzyme system (métabolisme), Données de séquences moléculaires (MeSH), Dépollution biologique de l'environnement (MeSH), Flavanones (métabolisme), Humains (MeSH), Hydroxylation (MeSH), Isoenzymes (génétique), Isoenzymes (métabolisme), Phanerochaete (enzymologie), Phanerochaete (génétique), Polluants environnementaux (métabolisme), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (génétique), Structure secondaire des protéines (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Cytochrome P-450 enzyme system, Protéines recombinantes.
- enzymologie : Phanerochaete, Saccharomyces cerevisiae.
- génétique : Cytochrome P-450 enzyme system, Isoenzymes, Phanerochaete, Protéines recombinantes, Saccharomyces cerevisiae.
- métabolisme : Cytochrome P-450 enzyme system, Flavanones, Isoenzymes, Polluants environnementaux, Protéines recombinantes.
- Alignement de séquences, Catalyse, Clonage moléculaire, Données de séquences moléculaires, Dépollution biologique de l'environnement, Humains, Hydroxylation, Structure secondaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Biodegradation, Environmental (MeSH), Catalysis (MeSH), Cloning, Molecular (MeSH), Cytochrome P-450 Enzyme System (chemistry), Cytochrome P-450 Enzyme System (genetics), Cytochrome P-450 Enzyme System (metabolism), Environmental Pollutants (metabolism), Flavanones (metabolism), Humans (MeSH), Hydroxylation (MeSH), Isoenzymes (genetics), Isoenzymes (metabolism), Molecular Sequence Data (MeSH), Phanerochaete (enzymology), Phanerochaete (genetics), Protein Structure, Secondary (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Sequence Alignment (MeSH).
- MESH :
- chemical , chemistry : Cytochrome P-450 Enzyme System, Recombinant Proteins.
- chemical , genetics : Cytochrome P-450 Enzyme System, Isoenzymes, Recombinant Proteins.
- chemical , metabolism : Cytochrome P-450 Enzyme System, Environmental Pollutants, Flavanones, Isoenzymes, Recombinant Proteins.
- enzymology : Phanerochaete, Saccharomyces cerevisiae.
- genetics : Phanerochaete, Saccharomyces cerevisiae.
- Amino Acid Sequence, Biodegradation, Environmental, Catalysis, Cloning, Molecular, Humans, Hydroxylation, Molecular Sequence Data, Protein Structure, Secondary, Sequence Alignment.
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 68.3kDa. 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.
DOI: 10.1016/j.bbrc.2009.06.134
PubMed: 19576179
Affiliations:
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(MeSH)</term><term>Hydroxylation (MeSH)</term><term>Isoenzymes (génétique)</term><term>Isoenzymes (métabolisme)</term><term>Phanerochaete (enzymologie)</term><term>Phanerochaete (génétique)</term><term>Polluants environnementaux (métabolisme)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Saccharomyces cerevisiae (enzymologie)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Structure secondaire des protéines (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cytochrome P-450 Enzyme System</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cytochrome P-450 Enzyme System</term><term>Isoenzymes</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" 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aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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 68.3kDa. 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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19576179</PMID><DateCompleted><Year>2009</Year><Month>08</Month><Day>14</Day></DateCompleted><DateRevised><Year>2012</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1090-2104</ISSN><JournalIssue CitedMedium="Internet"><Volume>387</Volume><Issue>1</Issue><PubDate><Year>2009</Year><Month>Sep</Month><Day>11</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Enzymatic properties of cytochrome P450 catalyzing 3'-hydroxylation of naringenin from the white-rot fungus Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>103-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbrc.2009.06.134</ELocationID><Abstract><AbstractText>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 68.3kDa. 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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kasai</LastName><ForeName>Noriyuki</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Biotechnology, Faculty of Engineering, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ikushiro</LastName><ForeName>Shin-ichi</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Hirosue</LastName><ForeName>Shinji</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Arisawa</LastName><ForeName>Akira</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Ichinose</LastName><ForeName>Hirofumi</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Wariishi</LastName><ForeName>Hiroyuki</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Ohta</LastName><ForeName>Miho</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Sakaki</LastName><ForeName>Toshiyuki</ForeName><Initials>T</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2009</Year><Month>07</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004785">Environmental Pollutants</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D044950">Flavanones</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007527">Isoenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9035-51-2</RegistryNumber><NameOfSubstance UI="D003577">Cytochrome P-450 Enzyme System</NameOfSubstance></Chemical><Chemical><RegistryNumber>HN5425SBF2</RegistryNumber><NameOfSubstance UI="C005273">naringenin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001673" MajorTopicYN="N">Biodegradation, Environmental</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003577" MajorTopicYN="N">Cytochrome P-450 Enzyme System</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004785" MajorTopicYN="N">Environmental Pollutants</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D044950" MajorTopicYN="N">Flavanones</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006900" MajorTopicYN="N">Hydroxylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2009</Year><Month>06</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2009</Year><Month>06</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>7</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>7</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>8</Month><Day>15</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19576179</ArticleId><ArticleId IdType="pii">S0006-291X(09)01301-1</ArticleId><ArticleId IdType="doi">10.1016/j.bbrc.2009.06.134</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country></list><tree><noCountry><name sortKey="Arisawa, Akira" sort="Arisawa, Akira" uniqKey="Arisawa A" first="Akira" last="Arisawa">Akira Arisawa</name><name sortKey="Hirosue, Shinji" sort="Hirosue, Shinji" uniqKey="Hirosue S" first="Shinji" last="Hirosue">Shinji Hirosue</name><name sortKey="Ichinose, Hirofumi" sort="Ichinose, Hirofumi" uniqKey="Ichinose H" first="Hirofumi" last="Ichinose">Hirofumi Ichinose</name><name sortKey="Ikushiro, Shin Ichi" sort="Ikushiro, Shin Ichi" uniqKey="Ikushiro S" first="Shin-Ichi" last="Ikushiro">Shin-Ichi Ikushiro</name><name sortKey="Ohta, Miho" sort="Ohta, Miho" uniqKey="Ohta M" first="Miho" last="Ohta">Miho Ohta</name><name sortKey="Sakaki, Toshiyuki" sort="Sakaki, Toshiyuki" uniqKey="Sakaki T" first="Toshiyuki" last="Sakaki">Toshiyuki Sakaki</name><name sortKey="Wariishi, Hiroyuki" sort="Wariishi, Hiroyuki" uniqKey="Wariishi H" first="Hiroyuki" last="Wariishi">Hiroyuki Wariishi</name></noCountry><country name="Japon"><noRegion><name sortKey="Kasai, Noriyuki" sort="Kasai, Noriyuki" uniqKey="Kasai N" first="Noriyuki" last="Kasai">Noriyuki Kasai</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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