The putative endoglucanase PcGH61D from Phanerochaete chrysosporium is a metal-dependent oxidative enzyme that cleaves cellulose.
Identifieur interne : 000480 ( Main/Exploration ); précédent : 000479; suivant : 000481The putative endoglucanase PcGH61D from Phanerochaete chrysosporium is a metal-dependent oxidative enzyme that cleaves cellulose.
Auteurs : Bj Rge Westereng [Norvège] ; Takuya Ishida ; Gustav Vaaje-Kolstad ; Miao Wu ; Vincent G H. Eijsink ; Kiyohiko Igarashi ; Masahiro Samejima ; Jerry St Hlberg ; Svein J. Horn ; Mats SandgrenSource :
- PloS one [ 1932-6203 ] ; 2011.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Analyse de séquence de protéine (MeSH), Cellulase (composition chimique), Cellulase (isolement et purification), Cellulase (métabolisme), Cellulose (métabolisme), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Ions (MeSH), Modèles moléculaires (MeSH), Métaux (pharmacologie), Oxydoréduction (effets des médicaments et des substances chimiques), Phanerochaete (effets des médicaments et des substances chimiques), Phanerochaete (enzymologie), Protéines recombinantes (métabolisme), Réducteurs (pharmacologie), Similitude structurale de protéines (MeSH), Spécificité du substrat (effets des médicaments et des substances chimiques), Séquence d'acides aminés (MeSH), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- composition chimique : Cellulase.
- effets des médicaments et des substances chimiques : Oxydoréduction, Phanerochaete, Spécificité du substrat.
- enzymologie : Phanerochaete.
- isolement et purification : Cellulase.
- métabolisme : Cellulase, Cellulose, Protéines recombinantes.
- pharmacologie : Métaux, Réducteurs.
- Alignement de séquences, Analyse de séquence de protéine, Clonage moléculaire, Données de séquences moléculaires, Ions, Modèles moléculaires, Similitude structurale de protéines, Séquence d'acides aminés, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Cellulase (chemistry), Cellulase (isolation & purification), Cellulase (metabolism), Cellulose (metabolism), Cloning, Molecular (MeSH), Electrophoresis, Polyacrylamide Gel (MeSH), Ions (MeSH), Metals (pharmacology), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (drug effects), Phanerochaete (drug effects), Phanerochaete (enzymology), Recombinant Proteins (metabolism), Reducing Agents (pharmacology), Sequence Alignment (MeSH), Sequence Analysis, Protein (MeSH), Structural Homology, Protein (MeSH), Substrate Specificity (drug effects).
- MESH :
- chemical , chemistry : Cellulase.
- chemical , isolation & purification : Cellulase.
- chemical , metabolism : Cellulase, Cellulose, Recombinant Proteins.
- chemical , pharmacology : Metals, Reducing Agents.
- drug effects : Oxidation-Reduction, Phanerochaete, Substrate Specificity.
- enzymology : Phanerochaete.
- Amino Acid Sequence, Cloning, Molecular, Electrophoresis, Polyacrylamide Gel, Ions, Models, Molecular, Molecular Sequence Data, Sequence Alignment, Sequence Analysis, Protein, Structural Homology, Protein.
Abstract
Many fungi growing on plant biomass produce proteins currently classified as glycoside hydrolase family 61 (GH61), some of which are known to act synergistically with cellulases. In this study we show that PcGH61D, the gene product of an open reading frame in the genome of Phanerochaete chrysosporium, is an enzyme that cleaves cellulose using a metal-dependent oxidative mechanism that leads to generation of aldonic acids. The activity of this enzyme and its beneficial effect on the efficiency of classical cellulases are stimulated by the presence of electron donors. Experiments with reduced cellulose confirmed the oxidative nature of the reaction catalyzed by PcGH61D and indicated that the enzyme may be capable of penetrating into the substrate. Considering the abundance of GH61-encoding genes in fungi and genes encoding their functional bacterial homologues currently classified as carbohydrate binding modules family 33 (CBM33), this enzyme activity is likely to turn out as a major determinant of microbial biomass-degrading efficiency.
DOI: 10.1371/journal.pone.0027807
PubMed: 22132148
PubMed Central: PMC3223205
Affiliations:
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In this study we show that PcGH61D, the gene product of an open reading frame in the genome of Phanerochaete chrysosporium, is an enzyme that cleaves cellulose using a metal-dependent oxidative mechanism that leads to generation of aldonic acids. The activity of this enzyme and its beneficial effect on the efficiency of classical cellulases are stimulated by the presence of electron donors. Experiments with reduced cellulose confirmed the oxidative nature of the reaction catalyzed by PcGH61D and indicated that the enzyme may be capable of penetrating into the substrate. Considering the abundance of GH61-encoding genes in fungi and genes encoding their functional bacterial homologues currently classified as carbohydrate binding modules family 33 (CBM33), this enzyme activity is likely to turn out as a major determinant of microbial biomass-degrading efficiency.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22132148</PMID><DateCompleted><Year>2012</Year><Month>04</Month><Day>02</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>6</Volume><Issue>11</Issue><PubDate><Year>2011</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>The putative endoglucanase PcGH61D from Phanerochaete chrysosporium is a metal-dependent oxidative enzyme that cleaves cellulose.</ArticleTitle><Pagination><MedlinePgn>e27807</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0027807</ELocationID><Abstract><AbstractText>Many fungi growing on plant biomass produce proteins currently classified as glycoside hydrolase family 61 (GH61), some of which are known to act synergistically with cellulases. In this study we show that PcGH61D, the gene product of an open reading frame in the genome of Phanerochaete chrysosporium, is an enzyme that cleaves cellulose using a metal-dependent oxidative mechanism that leads to generation of aldonic acids. The activity of this enzyme and its beneficial effect on the efficiency of classical cellulases are stimulated by the presence of electron donors. Experiments with reduced cellulose confirmed the oxidative nature of the reaction catalyzed by PcGH61D and indicated that the enzyme may be capable of penetrating into the substrate. Considering the abundance of GH61-encoding genes in fungi and genes encoding their functional bacterial homologues currently classified as carbohydrate binding modules family 33 (CBM33), this enzyme activity is likely to turn out as a major determinant of microbial biomass-degrading efficiency.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Westereng</LastName><ForeName>Bjørge</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, Ås, Norway.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ishida</LastName><ForeName>Takuya</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Vaaje-Kolstad</LastName><ForeName>Gustav</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Miao</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Eijsink</LastName><ForeName>Vincent G H</ForeName><Initials>VG</Initials></Author><Author ValidYN="Y"><LastName>Igarashi</LastName><ForeName>Kiyohiko</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Samejima</LastName><ForeName>Masahiro</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Ståhlberg</LastName><ForeName>Jerry</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Horn</LastName><ForeName>Svein J</ForeName><Initials>SJ</Initials></Author><Author ValidYN="Y"><LastName>Sandgren</LastName><ForeName>Mats</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>AB670125</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>11</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007477">Ions</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008670">Metals</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019163">Reducing Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>9004-34-6</RegistryNumber><NameOfSubstance UI="D002482">Cellulose</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.4</RegistryNumber><NameOfSubstance UI="D002480">Cellulase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002480" MajorTopicYN="N">Cellulase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002482" MajorTopicYN="N">Cellulose</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007477" MajorTopicYN="N">Ions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008670" MajorTopicYN="N">Metals</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019163" MajorTopicYN="N">Reducing Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020539" MajorTopicYN="N">Sequence Analysis, Protein</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D040681" MajorTopicYN="N">Structural Homology, Protein</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2011</Year><Month>09</Month><Day>12</Day></PubMedPubDate><PubMedPubDate 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Eijsink</name><name sortKey="Horn, Svein J" sort="Horn, Svein J" uniqKey="Horn S" first="Svein J" last="Horn">Svein J. Horn</name><name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</name><name sortKey="Ishida, Takuya" sort="Ishida, Takuya" uniqKey="Ishida T" first="Takuya" last="Ishida">Takuya Ishida</name><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name><name sortKey="Sandgren, Mats" sort="Sandgren, Mats" uniqKey="Sandgren M" first="Mats" last="Sandgren">Mats Sandgren</name><name sortKey="St Hlberg, Jerry" sort="St Hlberg, Jerry" uniqKey="St Hlberg J" first="Jerry" last="St Hlberg">Jerry St Hlberg</name><name sortKey="Vaaje Kolstad, Gustav" sort="Vaaje Kolstad, Gustav" uniqKey="Vaaje Kolstad G" first="Gustav" last="Vaaje-Kolstad">Gustav Vaaje-Kolstad</name><name sortKey="Wu, Miao" sort="Wu, Miao" uniqKey="Wu M" first="Miao" last="Wu">Miao Wu</name></noCountry><country name="Norvège"><noRegion><name sortKey="Westereng, Bj Rge" sort="Westereng, Bj Rge" uniqKey="Westereng B" first="Bj Rge" last="Westereng">Bj Rge Westereng</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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