Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases.
Identifieur interne : 000359 ( Main/Exploration ); précédent : 000358; suivant : 000360Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases.
Auteurs : Christiane Liers [Allemagne] ; Marek J. Pecyna ; Harald Kellner ; Anja Worrich ; Holger Zorn ; Kari T. Steffen ; Martin Hofrichter ; René UllrichSource :
- Applied microbiology and biotechnology [ 1432-0614 ] ; 2013.
Descripteurs français
- KwdFr :
- Agents colorants (métabolisme), Basidiomycota (enzymologie), Chromatographie en phase liquide (MeSH), Concentration en ions d'hydrogène (MeSH), Conformation des protéines (MeSH), Masse moléculaire (MeSH), Modèles moléculaires (MeSH), Oxydoréduction (MeSH), Peroxidases (composition chimique), Peroxidases (isolement et purification), Peroxidases (métabolisme), Similitude de séquences d'acides aminés (MeSH), Stabilité enzymatique (MeSH).
- MESH :
- composition chimique : Peroxidases.
- enzymologie : Basidiomycota.
- isolement et purification : Peroxidases.
- métabolisme : Agents colorants, Peroxidases.
- Chromatographie en phase liquide, Concentration en ions d'hydrogène, Conformation des protéines, Masse moléculaire, Modèles moléculaires, Oxydoréduction, Similitude de séquences d'acides aminés, Stabilité enzymatique.
English descriptors
- KwdEn :
- Basidiomycota (enzymology), Chromatography, Liquid (MeSH), Coloring Agents (metabolism), Enzyme Stability (MeSH), Hydrogen-Ion Concentration (MeSH), Models, Molecular (MeSH), Molecular Weight (MeSH), Oxidation-Reduction (MeSH), Peroxidases (chemistry), Peroxidases (isolation & purification), Peroxidases (metabolism), Protein Conformation (MeSH), Sequence Homology, Amino Acid (MeSH).
- MESH :
- chemical , chemistry : Peroxidases.
- chemical , isolation & purification : Peroxidases.
- chemical , metabolism : Coloring Agents, Peroxidases.
- enzymology : Basidiomycota.
- Chromatography, Liquid, Enzyme Stability, Hydrogen-Ion Concentration, Models, Molecular, Molecular Weight, Oxidation-Reduction, Protein Conformation, Sequence Homology, Amino Acid.
Abstract
Catalytic and physicochemical properties of representative fungal dye-decolorizing peroxidases (DyPs) of wood- (WRF) and litter-decomposing white-rot fungi (LDF) are summarized and compared, including one recombinant Mycetinis scorodonius DyP (rMscDyP; LDF), the wild-type Auricularia auricula-judae DyP (AauDyP; WRF), and two new DyPs secreted by the jelly fungi Exidia glandulosa (EglDyP; WRF) and Mycena epipterygia (MepDyP; LDF). Homogeneous preparations of these DyPs were obtained after different steps of fast protein liquid chromatography, and they increase the total number of characterized fungal DyP proteins to eight. The peptide sequences of AauDyP, MepDyP, and EglDyP showed highest homologies (52-56%) to the DyPs of M. scorodonius. Five out of the eight characterized fungal DyPs were used to evaluate their catalytic properties compared to classic fungal and plant heme peroxidases, namely lignin peroxidase of Phanerochaete chrysosporium (PchLiP; WRF), versatile peroxidase of Bjerkandera adusta (BadVP; WRF), and generic peroxidases of Coprinopsis cinerea (CiP) and Glycine max (soybean peroxidase=SBP). All DyPs tested possess unique properties regarding the stability at low pH values: 50-90% enzymatic activity remained after 4-h exposition at pH 2.5, and the oxidation of nonphenolic aromatic substrates (lignin model compounds) was optimal below pH 3. Furthermore, all DyPs efficiently oxidized recalcitrant dyes (e.g., Azure B) as well as the phenolic substrate 2,6-dimethoxyphenol. Thus, DyPs combine features of different peroxidases on the functional level and may be part of the biocatalytic system secreted by fungi for the oxidation of lignin and/or toxic aromatic compounds.
DOI: 10.1007/s00253-012-4521-2
PubMed: 23111597
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases.</title><author><name sortKey="Liers, Christiane" sort="Liers, Christiane" uniqKey="Liers C" first="Christiane" last="Liers">Christiane Liers</name><affiliation wicri:level="1"><nlm:affiliation>Department of Bio- and Environmental Sciences, International Graduate School of Zittau, Markt 23, 02763 Zittau, Germany. liers@ihi-zittau.de</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Bio- and Environmental Sciences, International Graduate School of Zittau, Markt 23, 02763 Zittau</wicri:regionArea><wicri:noRegion>02763 Zittau</wicri:noRegion><wicri:noRegion>02763 Zittau</wicri:noRegion><wicri:noRegion>02763 Zittau</wicri:noRegion></affiliation></author><author><name sortKey="Pecyna, Marek J" sort="Pecyna, Marek J" uniqKey="Pecyna M" first="Marek J" last="Pecyna">Marek J. Pecyna</name></author><author><name sortKey="Kellner, Harald" sort="Kellner, Harald" uniqKey="Kellner H" first="Harald" last="Kellner">Harald Kellner</name></author><author><name sortKey="Worrich, Anja" sort="Worrich, Anja" uniqKey="Worrich A" first="Anja" last="Worrich">Anja Worrich</name></author><author><name sortKey="Zorn, Holger" sort="Zorn, Holger" uniqKey="Zorn H" first="Holger" last="Zorn">Holger Zorn</name></author><author><name sortKey="Steffen, Kari T" sort="Steffen, Kari T" uniqKey="Steffen K" first="Kari T" last="Steffen">Kari T. Steffen</name></author><author><name sortKey="Hofrichter, Martin" sort="Hofrichter, Martin" uniqKey="Hofrichter M" first="Martin" last="Hofrichter">Martin Hofrichter</name></author><author><name sortKey="Ullrich, Rene" sort="Ullrich, Rene" uniqKey="Ullrich R" first="René" last="Ullrich">René Ullrich</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23111597</idno><idno type="pmid">23111597</idno><idno type="doi">10.1007/s00253-012-4521-2</idno><idno type="wicri:Area/Main/Corpus">000393</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000393</idno><idno type="wicri:Area/Main/Curation">000393</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000393</idno><idno type="wicri:Area/Main/Exploration">000393</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases.</title><author><name sortKey="Liers, Christiane" sort="Liers, Christiane" uniqKey="Liers C" first="Christiane" last="Liers">Christiane Liers</name><affiliation wicri:level="1"><nlm:affiliation>Department of Bio- and Environmental Sciences, International Graduate School of Zittau, Markt 23, 02763 Zittau, Germany. liers@ihi-zittau.de</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Bio- and Environmental Sciences, International Graduate School of Zittau, Markt 23, 02763 Zittau</wicri:regionArea><wicri:noRegion>02763 Zittau</wicri:noRegion><wicri:noRegion>02763 Zittau</wicri:noRegion><wicri:noRegion>02763 Zittau</wicri:noRegion></affiliation></author><author><name sortKey="Pecyna, Marek J" sort="Pecyna, Marek J" uniqKey="Pecyna M" first="Marek J" last="Pecyna">Marek J. Pecyna</name></author><author><name sortKey="Kellner, Harald" sort="Kellner, Harald" uniqKey="Kellner H" first="Harald" last="Kellner">Harald Kellner</name></author><author><name sortKey="Worrich, Anja" sort="Worrich, Anja" uniqKey="Worrich A" first="Anja" last="Worrich">Anja Worrich</name></author><author><name sortKey="Zorn, Holger" sort="Zorn, Holger" uniqKey="Zorn H" first="Holger" last="Zorn">Holger Zorn</name></author><author><name sortKey="Steffen, Kari T" sort="Steffen, Kari T" uniqKey="Steffen K" first="Kari T" last="Steffen">Kari T. Steffen</name></author><author><name sortKey="Hofrichter, Martin" sort="Hofrichter, Martin" uniqKey="Hofrichter M" first="Martin" last="Hofrichter">Martin Hofrichter</name></author><author><name sortKey="Ullrich, Rene" sort="Ullrich, Rene" uniqKey="Ullrich R" first="René" last="Ullrich">René Ullrich</name></author></analytic><series><title level="j">Applied microbiology and biotechnology</title><idno type="eISSN">1432-0614</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (enzymology)</term><term>Chromatography, Liquid (MeSH)</term><term>Coloring Agents (metabolism)</term><term>Enzyme Stability (MeSH)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Molecular Weight (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (chemistry)</term><term>Peroxidases (isolation & purification)</term><term>Peroxidases (metabolism)</term><term>Protein Conformation (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Agents colorants (métabolisme)</term><term>Basidiomycota (enzymologie)</term><term>Chromatographie en phase liquide (MeSH)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Masse moléculaire (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (composition chimique)</term><term>Peroxidases (isolement et purification)</term><term>Peroxidases (métabolisme)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Stabilité enzymatique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Coloring Agents</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Agents colorants</term><term>Peroxidases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography, Liquid</term><term>Enzyme Stability</term><term>Hydrogen-Ion Concentration</term><term>Models, Molecular</term><term>Molecular Weight</term><term>Oxidation-Reduction</term><term>Protein Conformation</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie en phase liquide</term><term>Concentration en ions d'hydrogène</term><term>Conformation des protéines</term><term>Masse moléculaire</term><term>Modèles moléculaires</term><term>Oxydoréduction</term><term>Similitude de séquences d'acides aminés</term><term>Stabilité enzymatique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Catalytic and physicochemical properties of representative fungal dye-decolorizing peroxidases (DyPs) of wood- (WRF) and litter-decomposing white-rot fungi (LDF) are summarized and compared, including one recombinant Mycetinis scorodonius DyP (rMscDyP; LDF), the wild-type Auricularia auricula-judae DyP (AauDyP; WRF), and two new DyPs secreted by the jelly fungi Exidia glandulosa (EglDyP; WRF) and Mycena epipterygia (MepDyP; LDF). Homogeneous preparations of these DyPs were obtained after different steps of fast protein liquid chromatography, and they increase the total number of characterized fungal DyP proteins to eight. The peptide sequences of AauDyP, MepDyP, and EglDyP showed highest homologies (52-56%) to the DyPs of M. scorodonius. Five out of the eight characterized fungal DyPs were used to evaluate their catalytic properties compared to classic fungal and plant heme peroxidases, namely lignin peroxidase of Phanerochaete chrysosporium (PchLiP; WRF), versatile peroxidase of Bjerkandera adusta (BadVP; WRF), and generic peroxidases of Coprinopsis cinerea (CiP) and Glycine max (soybean peroxidase=SBP). All DyPs tested possess unique properties regarding the stability at low pH values: 50-90% enzymatic activity remained after 4-h exposition at pH 2.5, and the oxidation of nonphenolic aromatic substrates (lignin model compounds) was optimal below pH 3. Furthermore, all DyPs efficiently oxidized recalcitrant dyes (e.g., Azure B) as well as the phenolic substrate 2,6-dimethoxyphenol. Thus, DyPs combine features of different peroxidases on the functional level and may be part of the biocatalytic system secreted by fungi for the oxidation of lignin and/or toxic aromatic compounds.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23111597</PMID><DateCompleted><Year>2013</Year><Month>12</Month><Day>27</Day></DateCompleted><DateRevised><Year>2013</Year><Month>06</Month><Day>18</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-0614</ISSN><JournalIssue CitedMedium="Internet"><Volume>97</Volume><Issue>13</Issue><PubDate><Year>2013</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Applied microbiology and biotechnology</Title><ISOAbbreviation>Appl Microbiol Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases.</ArticleTitle><Pagination><MedlinePgn>5839-49</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00253-012-4521-2</ELocationID><Abstract><AbstractText>Catalytic and physicochemical properties of representative fungal dye-decolorizing peroxidases (DyPs) of wood- (WRF) and litter-decomposing white-rot fungi (LDF) are summarized and compared, including one recombinant Mycetinis scorodonius DyP (rMscDyP; LDF), the wild-type Auricularia auricula-judae DyP (AauDyP; WRF), and two new DyPs secreted by the jelly fungi Exidia glandulosa (EglDyP; WRF) and Mycena epipterygia (MepDyP; LDF). Homogeneous preparations of these DyPs were obtained after different steps of fast protein liquid chromatography, and they increase the total number of characterized fungal DyP proteins to eight. The peptide sequences of AauDyP, MepDyP, and EglDyP showed highest homologies (52-56%) to the DyPs of M. scorodonius. Five out of the eight characterized fungal DyPs were used to evaluate their catalytic properties compared to classic fungal and plant heme peroxidases, namely lignin peroxidase of Phanerochaete chrysosporium (PchLiP; WRF), versatile peroxidase of Bjerkandera adusta (BadVP; WRF), and generic peroxidases of Coprinopsis cinerea (CiP) and Glycine max (soybean peroxidase=SBP). All DyPs tested possess unique properties regarding the stability at low pH values: 50-90% enzymatic activity remained after 4-h exposition at pH 2.5, and the oxidation of nonphenolic aromatic substrates (lignin model compounds) was optimal below pH 3. Furthermore, all DyPs efficiently oxidized recalcitrant dyes (e.g., Azure B) as well as the phenolic substrate 2,6-dimethoxyphenol. Thus, DyPs combine features of different peroxidases on the functional level and may be part of the biocatalytic system secreted by fungi for the oxidation of lignin and/or toxic aromatic compounds.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Liers</LastName><ForeName>Christiane</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Bio- and Environmental Sciences, International Graduate School of Zittau, Markt 23, 02763 Zittau, Germany. liers@ihi-zittau.de</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pecyna</LastName><ForeName>Marek J</ForeName><Initials>MJ</Initials></Author><Author ValidYN="Y"><LastName>Kellner</LastName><ForeName>Harald</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Worrich</LastName><ForeName>Anja</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Zorn</LastName><ForeName>Holger</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Steffen</LastName><ForeName>Kari T</ForeName><Initials>KT</Initials></Author><Author ValidYN="Y"><LastName>Hofrichter</LastName><ForeName>Martin</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Ullrich</LastName><ForeName>René</ForeName><Initials>R</Initials></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>2012</Year><Month>10</Month><Day>31</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Appl Microbiol Biotechnol</MedlineTA><NlmUniqueID>8406612</NlmUniqueID><ISSNLinking>0175-7598</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004396">Coloring Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002853" MajorTopicYN="N">Chromatography, Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004396" MajorTopicYN="N">Coloring Agents</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</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="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>07</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>10</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2012</Year><Month>10</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>11</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>11</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>12</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23111597</ArticleId><ArticleId IdType="doi">10.1007/s00253-012-4521-2</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Hofrichter, Martin" sort="Hofrichter, Martin" uniqKey="Hofrichter M" first="Martin" last="Hofrichter">Martin Hofrichter</name><name sortKey="Kellner, Harald" sort="Kellner, Harald" uniqKey="Kellner H" first="Harald" last="Kellner">Harald Kellner</name><name sortKey="Pecyna, Marek J" sort="Pecyna, Marek J" uniqKey="Pecyna M" first="Marek J" last="Pecyna">Marek J. Pecyna</name><name sortKey="Steffen, Kari T" sort="Steffen, Kari T" uniqKey="Steffen K" first="Kari T" last="Steffen">Kari T. Steffen</name><name sortKey="Ullrich, Rene" sort="Ullrich, Rene" uniqKey="Ullrich R" first="René" last="Ullrich">René Ullrich</name><name sortKey="Worrich, Anja" sort="Worrich, Anja" uniqKey="Worrich A" first="Anja" last="Worrich">Anja Worrich</name><name sortKey="Zorn, Holger" sort="Zorn, Holger" uniqKey="Zorn H" first="Holger" last="Zorn">Holger Zorn</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Liers, Christiane" sort="Liers, Christiane" uniqKey="Liers C" first="Christiane" last="Liers">Christiane Liers</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PhanerochaeteV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000359 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000359 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= PhanerochaeteV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:23111597
|texte= Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:23111597" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PhanerochaeteV1
| This area was generated with Dilib version V0.6.37. |  |