Discovery and characterization of new O-methyltransferase from the genome of the lignin-degrading fungus Phanerochaete chrysosporium for enhanced lignin degradation.
Identifieur interne : 000232 ( Main/Curation ); précédent : 000231; suivant : 000233Discovery 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
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pubmed:26672450Le document en format XML
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<term>Coriolaceae (enzymology)</term>
<term>DNA, Fungal (genetics)</term>
<term>Escherichia coli (MeSH)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (isolation & purification)</term>
<term>Fungal Proteins (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>
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<term>Phanerochaete (enzymology)</term>
<term>Phanerochaete (genetics)</term>
<term>Phenols (metabolism)</term>
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<term>Recombinant Fusion Proteins (metabolism)</term>
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<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>
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<term>Spécificité du substrat (MeSH)</term>
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<term>Fungal Proteins</term>
<term>Methyltransferases</term>
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<term>Phanerochaete</term>
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<term>Phanerochaete</term>
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<term>Methyltransferases</term>
<term>Phanerochaete</term>
<term>Protéines fongiques</term>
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<term>Methyltransferases</term>
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<term>Protéines fongiques</term>
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<term>Lignin</term>
<term>Methyltransferases</term>
<term>Phenols</term>
<term>Recombinant Fusion Proteins</term>
<term>S-Adenosylmethionine</term>
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<term>Lignine</term>
<term>Methyltransferases</term>
<term>Phénols</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines fongiques</term>
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<term>Cloning, Molecular</term>
<term>Escherichia coli</term>
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<term>Substrate Specificity</term>
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<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>
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<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>
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<ArticleTitle>Discovery and characterization of new O-methyltransferase from the genome of the lignin-degrading fungus Phanerochaete chrysosporium for enhanced lignin degradation.</ArticleTitle>
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<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>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Thanh Mai Pham</LastName>
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<ForeName>Yong Hwan</ForeName>
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<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>
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