Possibility of application of cytochrome P450 to bioremediation of dioxins.
Identifieur interne : 000349 ( Main/Exploration ); précédent : 000348; suivant : 000350Possibility of application of cytochrome P450 to bioremediation of dioxins.
Auteurs : Toshiyuki Sakaki [Japon] ; Keiko Yamamoto ; Shinichi IkushiroSource :
- Biotechnology and applied biochemistry [ 1470-8744 ]
Descripteurs français
- KwdFr :
- Animaux (MeSH), Bacillus megaterium (enzymologie), Bacillus megaterium (métabolisme), Cytochrome P-450 enzyme system (génétique), Cytochrome P-450 enzyme system (métabolisme), Dioxines (composition chimique), Dioxines (métabolisme), Dépollution biologique de l'environnement (MeSH), Humains (MeSH), Modèles moléculaires (MeSH), Mutagenèse dirigée (MeSH), Phanerochaete (enzymologie), Phanerochaete (métabolisme), Structure moléculaire (MeSH).
- MESH :
- composition chimique : Dioxines.
- enzymologie : Bacillus megaterium, Phanerochaete.
- génétique : Cytochrome P-450 enzyme system.
- métabolisme : Bacillus megaterium, Cytochrome P-450 enzyme system, Dioxines, Phanerochaete.
- Animaux, Dépollution biologique de l'environnement, Humains, Modèles moléculaires, Mutagenèse dirigée, Structure moléculaire.
English descriptors
- KwdEn :
- Animals (MeSH), Bacillus megaterium (enzymology), Bacillus megaterium (metabolism), Biodegradation, Environmental (MeSH), Cytochrome P-450 Enzyme System (genetics), Cytochrome P-450 Enzyme System (metabolism), Dioxins (chemistry), Dioxins (metabolism), Humans (MeSH), Models, Molecular (MeSH), Molecular Structure (MeSH), Mutagenesis, Site-Directed (MeSH), Phanerochaete (enzymology), Phanerochaete (metabolism).
- MESH :
- chemical , chemistry : Dioxins.
- chemical , genetics : Cytochrome P-450 Enzyme System.
- enzymology : Bacillus megaterium, Phanerochaete.
- metabolism : Bacillus megaterium, Cytochrome P-450 Enzyme System, Dioxins, Phanerochaete.
- Animals, Biodegradation, Environmental, Humans, Models, Molecular, Molecular Structure, Mutagenesis, Site-Directed.
Abstract
Dioxins, including polychlorinated dibenzo-p-dioxins (PCDDs), dibenzofurans, and coplanar polychlorinated biphenyls, are known to be metabolized by enzymes such as cytochrome (CYP) P450, angular dioxygenase, lignin peroxidase, and dehalogenase. It is noted that all of these enzymes have metal ions in their active centers, and the enzyme systems except for peroxidase each have a distinct electron transport chain. Among these enzyme systems, we have focused on cytochrome P450-dependent metabolism of dioxins from the viewpoint of practical use for bioremediation. Mammalian and fungal cytochromes P450 showed remarkable activity toward low-chlorinated PCDDs. In particular, mammalian cytochromes P450 belonging to the CYP1 family showed high activity. Rat CYP1A1 showed high activity toward 2,3,7-trichloro-dibenzo-p-dioxin but no detectable activity for 2,3,7,8-tetrachloro-dibenzo-p-dioxin (2,3,7,8-TCDD). On the basis of these results, we assumed that enlarging the space of the substrate-binding pocket of rat CYP1A1 might generate TCDD-metabolizing enzyme. Large-sized amino acids located at putative substrate-recognition sites and F-G loop were substituted for alanine by site-directed mutagenesis. Finally, we successfully generated 2,3,7,8-TCDD-metabolizing enzyme by site-directed mutagenesis of rat CYP1A1. We hope that recombinant microorganisms harboring genetically engineered cytochrome P450 will be used for bioremediation of soil contaminated with PCDDs, polychlorinated dibenzofurans, and coplanar polychlorinated biphenyls in the future.
DOI: 10.1002/bab.1067
PubMed: 23586993
Affiliations:
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Ikushiro</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013 Jan-Feb</date><idno type="RBID">pubmed:23586993</idno><idno type="pmid">23586993</idno><idno type="doi">10.1002/bab.1067</idno><idno type="wicri:Area/Main/Corpus">000370</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000370</idno><idno type="wicri:Area/Main/Curation">000370</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000370</idno><idno type="wicri:Area/Main/Exploration">000370</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Possibility of application of cytochrome P450 to bioremediation of dioxins.</title><author><name sortKey="Sakaki, Toshiyuki" sort="Sakaki, Toshiyuki" uniqKey="Sakaki T" first="Toshiyuki" last="Sakaki">Toshiyuki Sakaki</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biotechnology, Faculty of Engineering, Toyama Prefectural University, Imizu, Toyama, Japan. tsakaki@pu-toyama.ac.jp</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biotechnology, Faculty of Engineering, Toyama Prefectural University, Imizu, Toyama</wicri:regionArea><wicri:noRegion>Toyama</wicri:noRegion></affiliation></author><author><name sortKey="Yamamoto, Keiko" sort="Yamamoto, Keiko" uniqKey="Yamamoto K" first="Keiko" last="Yamamoto">Keiko Yamamoto</name></author><author><name sortKey="Ikushiro, Shinichi" sort="Ikushiro, Shinichi" uniqKey="Ikushiro S" first="Shinichi" last="Ikushiro">Shinichi Ikushiro</name></author></analytic><series><title level="j">Biotechnology and applied biochemistry</title><idno type="eISSN">1470-8744</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Bacillus megaterium (enzymology)</term><term>Bacillus megaterium (metabolism)</term><term>Biodegradation, Environmental (MeSH)</term><term>Cytochrome P-450 Enzyme System (genetics)</term><term>Cytochrome P-450 Enzyme System (metabolism)</term><term>Dioxins (chemistry)</term><term>Dioxins (metabolism)</term><term>Humans (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Molecular Structure (MeSH)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Phanerochaete (enzymology)</term><term>Phanerochaete (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Bacillus megaterium (enzymologie)</term><term>Bacillus megaterium (métabolisme)</term><term>Cytochrome P-450 enzyme system (génétique)</term><term>Cytochrome P-450 enzyme system (métabolisme)</term><term>Dioxines (composition chimique)</term><term>Dioxines (métabolisme)</term><term>Dépollution biologique de l'environnement (MeSH)</term><term>Humains (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Phanerochaete (enzymologie)</term><term>Phanerochaete (métabolisme)</term><term>Structure moléculaire (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Dioxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cytochrome P-450 Enzyme System</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Dioxines</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Bacillus megaterium</term><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Bacillus megaterium</term><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cytochrome P-450 enzyme system</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Bacillus megaterium</term><term>Cytochrome P-450 Enzyme System</term><term>Dioxins</term><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Bacillus megaterium</term><term>Cytochrome P-450 enzyme system</term><term>Dioxines</term><term>Phanerochaete</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Biodegradation, Environmental</term><term>Humans</term><term>Models, Molecular</term><term>Molecular Structure</term><term>Mutagenesis, Site-Directed</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Dépollution biologique de l'environnement</term><term>Humains</term><term>Modèles moléculaires</term><term>Mutagenèse dirigée</term><term>Structure moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Dioxins, including polychlorinated dibenzo-p-dioxins (PCDDs), dibenzofurans, and coplanar polychlorinated biphenyls, are known to be metabolized by enzymes such as cytochrome (CYP) P450, angular dioxygenase, lignin peroxidase, and dehalogenase. It is noted that all of these enzymes have metal ions in their active centers, and the enzyme systems except for peroxidase each have a distinct electron transport chain. Among these enzyme systems, we have focused on cytochrome P450-dependent metabolism of dioxins from the viewpoint of practical use for bioremediation. Mammalian and fungal cytochromes P450 showed remarkable activity toward low-chlorinated PCDDs. In particular, mammalian cytochromes P450 belonging to the CYP1 family showed high activity. Rat CYP1A1 showed high activity toward 2,3,7-trichloro-dibenzo-p-dioxin but no detectable activity for 2,3,7,8-tetrachloro-dibenzo-p-dioxin (2,3,7,8-TCDD). On the basis of these results, we assumed that enlarging the space of the substrate-binding pocket of rat CYP1A1 might generate TCDD-metabolizing enzyme. Large-sized amino acids located at putative substrate-recognition sites and F-G loop were substituted for alanine by site-directed mutagenesis. Finally, we successfully generated 2,3,7,8-TCDD-metabolizing enzyme by site-directed mutagenesis of rat CYP1A1. We hope that recombinant microorganisms harboring genetically engineered cytochrome P450 will be used for bioremediation of soil contaminated with PCDDs, polychlorinated dibenzofurans, and coplanar polychlorinated biphenyls in the future.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23586993</PMID><DateCompleted><Year>2014</Year><Month>08</Month><Day>19</Day></DateCompleted><DateRevised><Year>2013</Year><Month>04</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1470-8744</ISSN><JournalIssue CitedMedium="Internet"><Volume>60</Volume><Issue>1</Issue><PubDate><MedlineDate>2013 Jan-Feb</MedlineDate></PubDate></JournalIssue><Title>Biotechnology and applied biochemistry</Title><ISOAbbreviation>Biotechnol Appl Biochem</ISOAbbreviation></Journal><ArticleTitle>Possibility of application of cytochrome P450 to bioremediation of dioxins.</ArticleTitle><Pagination><MedlinePgn>65-70</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/bab.1067</ELocationID><Abstract><AbstractText>Dioxins, including polychlorinated dibenzo-p-dioxins (PCDDs), dibenzofurans, and coplanar polychlorinated biphenyls, are known to be metabolized by enzymes such as cytochrome (CYP) P450, angular dioxygenase, lignin peroxidase, and dehalogenase. It is noted that all of these enzymes have metal ions in their active centers, and the enzyme systems except for peroxidase each have a distinct electron transport chain. Among these enzyme systems, we have focused on cytochrome P450-dependent metabolism of dioxins from the viewpoint of practical use for bioremediation. Mammalian and fungal cytochromes P450 showed remarkable activity toward low-chlorinated PCDDs. In particular, mammalian cytochromes P450 belonging to the CYP1 family showed high activity. Rat CYP1A1 showed high activity toward 2,3,7-trichloro-dibenzo-p-dioxin but no detectable activity for 2,3,7,8-tetrachloro-dibenzo-p-dioxin (2,3,7,8-TCDD). On the basis of these results, we assumed that enlarging the space of the substrate-binding pocket of rat CYP1A1 might generate TCDD-metabolizing enzyme. Large-sized amino acids located at putative substrate-recognition sites and F-G loop were substituted for alanine by site-directed mutagenesis. Finally, we successfully generated 2,3,7,8-TCDD-metabolizing enzyme by site-directed mutagenesis of rat CYP1A1. We hope that recombinant microorganisms harboring genetically engineered cytochrome P450 will be used for bioremediation of soil contaminated with PCDDs, polychlorinated dibenzofurans, and coplanar polychlorinated biphenyls in the future.</AbstractText><CopyrightInformation>© 2013 International Union of Biochemistry and Molecular Biology, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sakaki</LastName><ForeName>Toshiyuki</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Biotechnology, Faculty of Engineering, Toyama Prefectural University, Imizu, Toyama, Japan. tsakaki@pu-toyama.ac.jp</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yamamoto</LastName><ForeName>Keiko</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Ikushiro</LastName><ForeName>Shinichi</ForeName><Initials>S</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>01</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biotechnol Appl Biochem</MedlineTA><NlmUniqueID>8609465</NlmUniqueID><ISSNLinking>0885-4513</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004147">Dioxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9035-51-2</RegistryNumber><NameOfSubstance UI="D003577">Cytochrome P-450 Enzyme System</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001410" MajorTopicYN="N">Bacillus megaterium</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001673" MajorTopicYN="N">Biodegradation, Environmental</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003577" MajorTopicYN="N">Cytochrome P-450 Enzyme System</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004147" MajorTopicYN="N">Dioxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015394" MajorTopicYN="N">Molecular Structure</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>10</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>11</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>4</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>4</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>8</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23586993</ArticleId><ArticleId IdType="doi">10.1002/bab.1067</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country></list><tree><noCountry><name sortKey="Ikushiro, Shinichi" sort="Ikushiro, Shinichi" uniqKey="Ikushiro S" first="Shinichi" last="Ikushiro">Shinichi Ikushiro</name><name sortKey="Yamamoto, Keiko" sort="Yamamoto, Keiko" uniqKey="Yamamoto K" first="Keiko" last="Yamamoto">Keiko Yamamoto</name></noCountry><country name="Japon"><noRegion><name sortKey="Sakaki, Toshiyuki" sort="Sakaki, Toshiyuki" uniqKey="Sakaki T" first="Toshiyuki" last="Sakaki">Toshiyuki Sakaki</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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