A new versatile peroxidase from Pleurotus.
Identifieur interne : 000A60 ( Main/Exploration ); précédent : 000A59; suivant : 000A61A new versatile peroxidase from Pleurotus.
Auteurs : F J Ruiz-Due As [Espagne] ; S. Camarero ; M. Pérez-Boada ; M J Martínez ; A T MartínezSource :
- Biochemical Society transactions [ 0300-5127 ] ; 2001.
Descripteurs français
- KwdFr :
- Clonage moléculaire (MeSH), Conformation des protéines (MeSH), Lignine (métabolisme), Modèles moléculaires (MeSH), Oxydoréduction (MeSH), Peroxidases (composition chimique), Peroxidases (génétique), Peroxidases (métabolisme), Pleurotus (enzymologie), Pleurotus (génétique), Pleurotus (métabolisme), Sites de fixation (MeSH), Spécificité du substrat (MeSH).
- MESH :
- composition chimique : Peroxidases.
- enzymologie : Pleurotus.
- génétique : Peroxidases, Pleurotus.
- métabolisme : Lignine, Peroxidases, Pleurotus.
- Clonage moléculaire, Conformation des protéines, Modèles moléculaires, Oxydoréduction, Sites de fixation, Spécificité du substrat.
English descriptors
- KwdEn :
- Binding Sites (MeSH), Cloning, Molecular (MeSH), Lignin (metabolism), Models, Molecular (MeSH), Oxidation-Reduction (MeSH), Peroxidases (chemistry), Peroxidases (genetics), Peroxidases (metabolism), Pleurotus (enzymology), Pleurotus (genetics), Pleurotus (metabolism), Protein Conformation (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , chemistry : Peroxidases.
- chemical , genetics : Peroxidases.
- chemical , metabolism : Lignin, Peroxidases.
- enzymology : Pleurotus.
- genetics : Pleurotus.
- metabolism : Pleurotus.
- Binding Sites, Cloning, Molecular, Models, Molecular, Oxidation-Reduction, Protein Conformation, Substrate Specificity.
Abstract
Lignin peroxidase (LiP) and manganese peroxidase (MnP) have been investigated in Phanerochaete chrysosporium. A third ligninolytic peroxidase has been described in Pleurotus and Bjerkandera. Two of these versatile peroxidases (VPs) have been cloned, sequenced and characterized. They have high affinity for Mn(2+), hydroquinones and dyes, and also oxidize veratryl alcohol, dimethoxybenzene and lignin dimers. The deduced sequences show higher identity with Ph. chrysosporium LiP than MnP, but the molecular models obtained include a Mn(2+)-binding site. Concerning aromatic substrate oxidation, Pl. eryngii VP shows a putative long-range electron transfer pathway from an exposed trytophan to haem. Mutagenesis and chemical modification of this tryptophan and the acidic residues forming the Mn(2+)-binding site confirmed their role in catalysis. The existence of several substrate oxidation sites is supported further by biochemical evidence. Residue conservation in other fungal peroxidases is discussed.
DOI: 10.1042/0300-5127:0290116
PubMed: 11356138
Affiliations:
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Pérez-Boada</name></author><author><name sortKey="Martinez, M J" sort="Martinez, M J" uniqKey="Martinez M" first="M J" last="Martínez">M J Martínez</name></author><author><name sortKey="Martinez, A T" sort="Martinez, A T" uniqKey="Martinez A" first="A T" last="Martínez">A T Martínez</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2001">2001</date><idno type="RBID">pubmed:11356138</idno><idno type="pmid">11356138</idno><idno type="doi">10.1042/0300-5127:0290116</idno><idno type="wicri:Area/Main/Corpus">000A53</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000A53</idno><idno type="wicri:Area/Main/Curation">000A53</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000A53</idno><idno type="wicri:Area/Main/Exploration">000A53</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">A new versatile peroxidase from Pleurotus.</title><author><name sortKey="Ruiz Due As, F J" sort="Ruiz Due As, F J" uniqKey="Ruiz Due As F" first="F J" last="Ruiz-Due As">F J Ruiz-Due As</name><affiliation wicri:level="2"><nlm:affiliation>Centro de Investigaciones Biológicas, CSIC, Velázquez 144, E-28006 Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Centro de Investigaciones Biológicas, CSIC, Velázquez 144, E-28006 Madrid</wicri:regionArea><placeName><region nuts="2" type="communauté">Communauté de Madrid</region></placeName></affiliation></author><author><name sortKey="Camarero, S" sort="Camarero, S" uniqKey="Camarero S" first="S" last="Camarero">S. Camarero</name></author><author><name sortKey="Perez Boada, M" sort="Perez Boada, M" uniqKey="Perez Boada M" first="M" last="Pérez-Boada">M. Pérez-Boada</name></author><author><name sortKey="Martinez, M J" sort="Martinez, M J" uniqKey="Martinez M" first="M J" last="Martínez">M J Martínez</name></author><author><name sortKey="Martinez, A T" sort="Martinez, A T" uniqKey="Martinez A" first="A T" last="Martínez">A T Martínez</name></author></analytic><series><title level="j">Biochemical Society transactions</title><idno type="ISSN">0300-5127</idno><imprint><date when="2001" type="published">2001</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Lignin (metabolism)</term><term>Models, Molecular (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (chemistry)</term><term>Peroxidases (genetics)</term><term>Peroxidases (metabolism)</term><term>Pleurotus (enzymology)</term><term>Pleurotus (genetics)</term><term>Pleurotus (metabolism)</term><term>Protein Conformation (MeSH)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Clonage moléculaire (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Lignine (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (composition chimique)</term><term>Peroxidases (génétique)</term><term>Peroxidases (métabolisme)</term><term>Pleurotus (enzymologie)</term><term>Pleurotus (génétique)</term><term>Pleurotus (métabolisme)</term><term>Sites de fixation (MeSH)</term><term>Spécificité du substrat (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lignin</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>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Peroxidases</term><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Lignine</term><term>Peroxidases</term><term>Pleurotus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Cloning, Molecular</term><term>Models, Molecular</term><term>Oxidation-Reduction</term><term>Protein Conformation</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Clonage moléculaire</term><term>Conformation des protéines</term><term>Modèles moléculaires</term><term>Oxydoréduction</term><term>Sites de fixation</term><term>Spécificité du substrat</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lignin peroxidase (LiP) and manganese peroxidase (MnP) have been investigated in Phanerochaete chrysosporium. A third ligninolytic peroxidase has been described in Pleurotus and Bjerkandera. Two of these versatile peroxidases (VPs) have been cloned, sequenced and characterized. They have high affinity for Mn(2+), hydroquinones and dyes, and also oxidize veratryl alcohol, dimethoxybenzene and lignin dimers. The deduced sequences show higher identity with Ph. chrysosporium LiP than MnP, but the molecular models obtained include a Mn(2+)-binding site. Concerning aromatic substrate oxidation, Pl. eryngii VP shows a putative long-range electron transfer pathway from an exposed trytophan to haem. Mutagenesis and chemical modification of this tryptophan and the acidic residues forming the Mn(2+)-binding site confirmed their role in catalysis. The existence of several substrate oxidation sites is supported further by biochemical evidence. Residue conservation in other fungal peroxidases is discussed.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11356138</PMID><DateCompleted><Year>2001</Year><Month>09</Month><Day>06</Day></DateCompleted><DateRevised><Year>2019</Year><Month>07</Month><Day>07</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0300-5127</ISSN><JournalIssue CitedMedium="Print"><Volume>29</Volume><Issue>Pt 2</Issue><PubDate><Year>2001</Year><Month>May</Month></PubDate></JournalIssue><Title>Biochemical Society transactions</Title><ISOAbbreviation>Biochem Soc Trans</ISOAbbreviation></Journal><ArticleTitle>A new versatile peroxidase from Pleurotus.</ArticleTitle><Pagination><MedlinePgn>116-22</MedlinePgn></Pagination><Abstract><AbstractText>Lignin peroxidase (LiP) and manganese peroxidase (MnP) have been investigated in Phanerochaete chrysosporium. A third ligninolytic peroxidase has been described in Pleurotus and Bjerkandera. Two of these versatile peroxidases (VPs) have been cloned, sequenced and characterized. They have high affinity for Mn(2+), hydroquinones and dyes, and also oxidize veratryl alcohol, dimethoxybenzene and lignin dimers. The deduced sequences show higher identity with Ph. chrysosporium LiP than MnP, but the molecular models obtained include a Mn(2+)-binding site. Concerning aromatic substrate oxidation, Pl. eryngii VP shows a putative long-range electron transfer pathway from an exposed trytophan to haem. Mutagenesis and chemical modification of this tryptophan and the acidic residues forming the Mn(2+)-binding site confirmed their role in catalysis. The existence of several substrate oxidation sites is supported further by biochemical evidence. Residue conservation in other fungal peroxidases is discussed.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ruiz-Dueñas</LastName><ForeName>F J</ForeName><Initials>FJ</Initials><AffiliationInfo><Affiliation>Centro de Investigaciones Biológicas, CSIC, Velázquez 144, E-28006 Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Camarero</LastName><ForeName>S</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Pérez-Boada</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Martínez</LastName><ForeName>M J</ForeName><Initials>MJ</Initials></Author><Author ValidYN="Y"><LastName>Martínez</LastName><ForeName>A T</ForeName><Initials>AT</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></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biochem Soc Trans</MedlineTA><NlmUniqueID>7506897</NlmUniqueID><ISSNLinking>0300-5127</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020076" MajorTopicYN="N">Pleurotus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList><NumberOfReferences>50</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2001</Year><Month>5</Month><Day>18</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>9</Month><Day>8</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2001</Year><Month>5</Month><Day>18</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11356138</ArticleId><ArticleId IdType="doi">10.1042/0300-5127:0290116</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Espagne</li></country><region><li>Communauté de Madrid</li></region></list><tree><noCountry><name sortKey="Camarero, S" sort="Camarero, S" uniqKey="Camarero S" first="S" last="Camarero">S. Camarero</name><name sortKey="Martinez, A T" sort="Martinez, A T" uniqKey="Martinez A" first="A T" last="Martínez">A T Martínez</name><name sortKey="Martinez, M J" sort="Martinez, M J" uniqKey="Martinez M" first="M J" last="Martínez">M J Martínez</name><name sortKey="Perez Boada, M" sort="Perez Boada, M" uniqKey="Perez Boada M" first="M" last="Pérez-Boada">M. Pérez-Boada</name></noCountry><country name="Espagne"><region name="Communauté de Madrid"><name sortKey="Ruiz Due As, F J" sort="Ruiz Due As, F J" uniqKey="Ruiz Due As F" first="F J" last="Ruiz-Due As">F J Ruiz-Due As</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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