Discovery and characterization of new O-methyltransferase from the genome of the lignin-degrading fungus Phanerochaete chrysosporium for enhanced lignin degradation.
Identifieur interne : 000216 ( Main/Exploration ); précédent : 000215; suivant : 000217Discovery and characterization of new O-methyltransferase from the genome of the lignin-degrading fungus Phanerochaete chrysosporium for enhanced lignin degradation.
Auteurs : Le Thanh Mai Pham [Corée du Sud] ; Yong Hwan Kim [Corée du Sud]Source :
- Enzyme and microbial technology [ 1879-0909 ] ; 2016.
Descripteurs français
- KwdFr :
- ADN fongique (génétique), Adémétionine (métabolisme), Clonage moléculaire (MeSH), Conformation des protéines (MeSH), Coriolaceae (enzymologie), Dépollution biologique de l'environnement (MeSH), Escherichia coli (MeSH), Gènes fongiques (MeSH), Lignine (métabolisme), Methyltransferases (génétique), Methyltransferases (isolement et purification), Methyltransferases (métabolisme), Modèles moléculaires (MeSH), Méthylation (MeSH), Phanerochaete (enzymologie), Phanerochaete (génétique), Phénols (métabolisme), Protéines de fusion recombinantes (métabolisme), Protéines fongiques (génétique), Protéines fongiques (isolement et purification), Protéines fongiques (métabolisme), Spécificité d'espèce (MeSH), Spécificité du substrat (MeSH).
- MESH :
- enzymologie : Coriolaceae, Phanerochaete.
- génétique : ADN fongique, Methyltransferases, Phanerochaete, Protéines fongiques.
- isolement et purification : Methyltransferases, Protéines fongiques.
- métabolisme : Adémétionine, Lignine, Methyltransferases, Phénols, Protéines de fusion recombinantes, Protéines fongiques.
- Clonage moléculaire, Conformation des protéines, Dépollution biologique de l'environnement, Escherichia coli, Gènes fongiques, Modèles moléculaires, Méthylation, Spécificité d'espèce, Spécificité du substrat.
English descriptors
- KwdEn :
- Biodegradation, Environmental (MeSH), Cloning, Molecular (MeSH), Coriolaceae (enzymology), DNA, Fungal (genetics), Escherichia coli (MeSH), Fungal Proteins (genetics), Fungal Proteins (isolation & purification), Fungal Proteins (metabolism), Genes, Fungal (MeSH), Lignin (metabolism), Methylation (MeSH), Methyltransferases (genetics), Methyltransferases (isolation & purification), Methyltransferases (metabolism), Models, Molecular (MeSH), Phanerochaete (enzymology), Phanerochaete (genetics), Phenols (metabolism), Protein Conformation (MeSH), Recombinant Fusion Proteins (metabolism), S-Adenosylmethionine (metabolism), Species Specificity (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , genetics : DNA, Fungal, Fungal Proteins, Methyltransferases.
- enzymology : Coriolaceae, Phanerochaete.
- genetics : Phanerochaete.
- chemical , isolation & purification : Fungal Proteins, Methyltransferases.
- chemical , metabolism : Fungal Proteins, Lignin, Methyltransferases, Phenols, Recombinant Fusion Proteins, S-Adenosylmethionine.
- Biodegradation, Environmental, Cloning, Molecular, Escherichia coli, Genes, Fungal, Methylation, Models, Molecular, Protein Conformation, Species Specificity, Substrate Specificity.
Abstract
Using bioinformatic homology search tools, this study utilized sequence phylogeny, gene organization and conserved motifs to identify members of the family of O-methyltransferases from lignin-degrading fungus Phanerochaete chrysosporium. The heterologous expression and characterization of O-methyltransferases from P. chrysosporium were studied. The expressed protein utilized S-(5'-adenosyl)-L-methionine p-toluenesulfonate salt (SAM) and methylated various free-hydroxyl phenolic compounds at both meta and para site. In the same motif, O-methyltransferases were also identified in other white-rot fungi including Bjerkandera adusta, Ceriporiopsis (Gelatoporia) subvermispora B, and Trametes versicolor. As free-hydroxyl phenolic compounds have been known as inhibitors for lignin peroxidase, the presence of O-methyltransferases in white-rot fungi suggested their biological functions in accelerating lignin degradation in white-rot basidiomycetes by converting those inhibitory groups into non-toxic methylated phenolic ones.
DOI: 10.1016/j.enzmictec.2015.08.016
PubMed: 26672450
Affiliations:
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(metabolism)</term><term>Genes, Fungal (MeSH)</term><term>Lignin (metabolism)</term><term>Methylation (MeSH)</term><term>Methyltransferases (genetics)</term><term>Methyltransferases (isolation & purification)</term><term>Methyltransferases (metabolism)</term><term>Models, Molecular (MeSH)</term><term>Phanerochaete (enzymology)</term><term>Phanerochaete (genetics)</term><term>Phenols (metabolism)</term><term>Protein Conformation (MeSH)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>S-Adenosylmethionine (metabolism)</term><term>Species Specificity (MeSH)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN fongique (génétique)</term><term>Adémétionine (métabolisme)</term><term>Clonage moléculaire (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Coriolaceae (enzymologie)</term><term>Dépollution biologique de l'environnement (MeSH)</term><term>Escherichia coli (MeSH)</term><term>Gènes fongiques (MeSH)</term><term>Lignine (métabolisme)</term><term>Methyltransferases (génétique)</term><term>Methyltransferases (isolement et purification)</term><term>Methyltransferases (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Méthylation (MeSH)</term><term>Phanerochaete (enzymologie)</term><term>Phanerochaete (génétique)</term><term>Phénols (métabolisme)</term><term>Protéines de fusion recombinantes (métabolisme)</term><term>Protéines fongiques (génétique)</term><term>Protéines fongiques (isolement et purification)</term><term>Protéines fongiques (métabolisme)</term><term>Spécificité d'espèce (MeSH)</term><term>Spécificité du substrat (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA, Fungal</term><term>Fungal Proteins</term><term>Methyltransferases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Coriolaceae</term><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Coriolaceae</term><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN fongique</term><term>Methyltransferases</term><term>Phanerochaete</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Fungal Proteins</term><term>Methyltransferases</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Methyltransferases</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fungal Proteins</term><term>Lignin</term><term>Methyltransferases</term><term>Phenols</term><term>Recombinant Fusion Proteins</term><term>S-Adenosylmethionine</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Adémétionine</term><term>Lignine</term><term>Methyltransferases</term><term>Phénols</term><term>Protéines de fusion recombinantes</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biodegradation, Environmental</term><term>Cloning, Molecular</term><term>Escherichia coli</term><term>Genes, Fungal</term><term>Methylation</term><term>Models, Molecular</term><term>Protein Conformation</term><term>Species Specificity</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Clonage moléculaire</term><term>Conformation des protéines</term><term>Dépollution biologique de l'environnement</term><term>Escherichia coli</term><term>Gènes fongiques</term><term>Modèles moléculaires</term><term>Méthylation</term><term>Spécificité d'espèce</term><term>Spécificité du substrat</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Using bioinformatic homology search tools, this study utilized sequence phylogeny, gene organization and conserved motifs to identify members of the family of O-methyltransferases from lignin-degrading fungus Phanerochaete chrysosporium. The heterologous expression and characterization of O-methyltransferases from P. chrysosporium were studied. The expressed protein utilized S-(5'-adenosyl)-L-methionine p-toluenesulfonate salt (SAM) and methylated various free-hydroxyl phenolic compounds at both meta and para site. In the same motif, O-methyltransferases were also identified in other white-rot fungi including Bjerkandera adusta, Ceriporiopsis (Gelatoporia) subvermispora B, and Trametes versicolor. As free-hydroxyl phenolic compounds have been known as inhibitors for lignin peroxidase, the presence of O-methyltransferases in white-rot fungi suggested their biological functions in accelerating lignin degradation in white-rot basidiomycetes by converting those inhibitory groups into non-toxic methylated phenolic ones.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26672450</PMID><DateCompleted><Year>2016</Year><Month>10</Month><Day>11</Day></DateCompleted><DateRevised><Year>2017</Year><Month>08</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0909</ISSN><JournalIssue CitedMedium="Internet"><Volume>82</Volume><PubDate><Year>2016</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Enzyme and microbial technology</Title><ISOAbbreviation>Enzyme Microb Technol</ISOAbbreviation></Journal><ArticleTitle>Discovery and characterization of new O-methyltransferase from the genome of the lignin-degrading fungus Phanerochaete chrysosporium for enhanced lignin degradation.</ArticleTitle><Pagination><MedlinePgn>66-73</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0141-0229(15)30051-X</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.enzmictec.2015.08.016</ELocationID><Abstract><AbstractText>Using bioinformatic homology search tools, this study utilized sequence phylogeny, gene organization and conserved motifs to identify members of the family of O-methyltransferases from lignin-degrading fungus Phanerochaete chrysosporium. The heterologous expression and characterization of O-methyltransferases from P. chrysosporium were studied. The expressed protein utilized S-(5'-adenosyl)-L-methionine p-toluenesulfonate salt (SAM) and methylated various free-hydroxyl phenolic compounds at both meta and para site. In the same motif, O-methyltransferases were also identified in other white-rot fungi including Bjerkandera adusta, Ceriporiopsis (Gelatoporia) subvermispora B, and Trametes versicolor. As free-hydroxyl phenolic compounds have been known as inhibitors for lignin peroxidase, the presence of O-methyltransferases in white-rot fungi suggested their biological functions in accelerating lignin degradation in white-rot basidiomycetes by converting those inhibitory groups into non-toxic methylated phenolic ones.</AbstractText><CopyrightInformation>Copyright © 2015 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Thanh Mai Pham</LastName><ForeName>Le</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Chemical Engineering, Kwangwoon University, 447-1, Wolgye-Dong, Nowon-Gu, Seoul 139-701, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Yong Hwan</ForeName><Initials>YH</Initials><AffiliationInfo><Affiliation>Department of Chemical Engineering, Kwangwoon University, 447-1, Wolgye-Dong, Nowon-Gu, Seoul 139-701, Republic of Korea. Electronic address: metalkim@kw.ac.kr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>08</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Enzyme Microb Technol</MedlineTA><NlmUniqueID>8003761</NlmUniqueID><ISSNLinking>0141-0229</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004271">DNA, Fungal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010636">Phenols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>7LP2MPO46S</RegistryNumber><NameOfSubstance UI="D012436">S-Adenosylmethionine</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber><NameOfSubstance UI="D008780">Methyltransferases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001673" MajorTopicYN="N">Biodegradation, Environmental</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055453" MajorTopicYN="N">Coriolaceae</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004271" MajorTopicYN="N">DNA, Fungal</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005800" MajorTopicYN="N">Genes, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008745" MajorTopicYN="N">Methylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008780" MajorTopicYN="N">Methyltransferases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</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="D010636" MajorTopicYN="N">Phenols</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012436" MajorTopicYN="N">S-Adenosylmethionine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013045" MajorTopicYN="N">Species Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Free-phenolic compounds</Keyword><Keyword MajorTopicYN="N">Lignin peroxidase</Keyword><Keyword MajorTopicYN="N">O-Methyltransferase</Keyword><Keyword MajorTopicYN="N">White-rot fungi</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>06</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>08</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>08</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>12</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>12</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>10</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26672450</ArticleId><ArticleId IdType="pii">S0141-0229(15)30051-X</ArticleId><ArticleId IdType="doi">10.1016/j.enzmictec.2015.08.016</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Corée du Sud</li></country><region><li>Région capitale de Séoul</li></region><settlement><li>Séoul</li></settlement></list><tree><country name="Corée du Sud"><region name="Région capitale de Séoul"><name sortKey="Thanh Mai Pham, Le" sort="Thanh Mai Pham, Le" uniqKey="Thanh Mai Pham L" first="Le" last="Thanh Mai Pham">Le Thanh Mai Pham</name></region><name sortKey="Kim, Yong Hwan" sort="Kim, Yong Hwan" uniqKey="Kim Y" first="Yong Hwan" last="Kim">Yong Hwan Kim</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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