Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites.
Identifieur interne : 000B38 ( Main/Exploration ); précédent : 000B37; suivant : 000B39Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites.
Auteurs : S. Camarero [Espagne] ; S. Sarkar ; F J Ruiz-Due As ; M J Martínez ; A T MartínezSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1999.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Chromatographie en phase liquide à haute performance (MeSH), Domaine catalytique (MeSH), Données de séquences moléculaires (MeSH), Lignine (métabolisme), Manganèse (métabolisme), Modèles moléculaires (MeSH), Peroxidases (isolement et purification), Peroxidases (métabolisme), Pleurotus (enzymologie), Séquence d'acides aminés (MeSH).
- MESH :
- enzymologie : Pleurotus.
- isolement et purification : Peroxidases.
- métabolisme : Lignine, Manganèse, Peroxidases.
- Alignement de séquences, Chromatographie en phase liquide à haute performance, Domaine catalytique, Données de séquences moléculaires, Modèles moléculaires, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Catalytic Domain (MeSH), Chromatography, High Pressure Liquid (MeSH), Lignin (metabolism), Manganese (metabolism), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Peroxidases (isolation & purification), Peroxidases (metabolism), Pleurotus (enzymology), Sequence Alignment (MeSH).
- MESH :
- chemical , isolation & purification : Peroxidases.
- chemical , metabolism : Lignin, Manganese, Peroxidases.
- enzymology : Pleurotus.
- Amino Acid Sequence, Catalytic Domain, Chromatography, High Pressure Liquid, Models, Molecular, Molecular Sequence Data, Sequence Alignment.
Abstract
Two major peroxidases are secreted by the fungus Pleurotus eryngii in lignocellulose cultures. One is similar to Phanerochaete chrysosporium manganese-dependent peroxidase. The second protein (PS1), although catalyzing the oxidation of Mn2+ to Mn3+ by H2O2, differs from the above enzymes by its manganese-independent activity enabling it to oxidize substituted phenols and synthetic dyes, as well as the lignin peroxidase (LiP) substrate veratryl alcohol. This is by a mechanism similar to that reported for LiP, as evidenced by p-dimethoxybenzene oxidation yielding benzoquinone. The apparent kinetic constants showed high activity on Mn2+, but methoxyhydroquinone was the natural substrate with the highest enzyme affinity (this and other phenolic substrates are not efficiently oxidized by the P. chrysosporium peroxidases). A three-dimensional model was built using crystal models from four fungal peroxidase as templates. The model suggests high structural affinity of this versatile peroxidase with LiP but shows a putative Mn2+ binding site near the internal heme propionate, involving Glu36, Glu40, and Asp181. A specific substrate interaction site for Mn2+ is supported by kinetic data showing noncompetitive inhibition with other peroxidase substrates. Moreover, residues reported as involved in LiP interaction with veratryl alcohol and other aromatic substrates are present in peroxidase PS1 such as His82 at the heme-channel opening, which is remarkably similar to that of P. chrysosporium LiP, and Trp170 at the protein surface. These residues could be involved in two different hypothetical long range electron transfer pathways from substrate (His82-Ala83-Asn84-His47-heme and Trp170-Leu171-heme) similar to those postulated for LiP.
DOI: 10.1074/jbc.274.15.10324
PubMed: 10187820
Affiliations:
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Sarkar</name></author><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></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="1999">1999</date><idno type="RBID">pubmed:10187820</idno><idno type="pmid">10187820</idno><idno type="doi">10.1074/jbc.274.15.10324</idno><idno type="wicri:Area/Main/Corpus">000B49</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000B49</idno><idno type="wicri:Area/Main/Curation">000B49</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000B49</idno><idno type="wicri:Area/Main/Exploration">000B49</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites.</title><author><name sortKey="Camarero, S" sort="Camarero, S" uniqKey="Camarero S" first="S" last="Camarero">S. Camarero</name><affiliation wicri:level="2"><nlm:affiliation>Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Velázquez 144, E-28006 Madrid, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Velázquez 144, E-28006 Madrid</wicri:regionArea><placeName><region nuts="2" type="communauté">Communauté de Madrid</region></placeName></affiliation></author><author><name sortKey="Sarkar, S" sort="Sarkar, S" uniqKey="Sarkar S" first="S" last="Sarkar">S. Sarkar</name></author><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></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">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Catalytic Domain (MeSH)</term><term>Chromatography, High Pressure Liquid (MeSH)</term><term>Lignin (metabolism)</term><term>Manganese (metabolism)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Peroxidases (isolation & purification)</term><term>Peroxidases (metabolism)</term><term>Pleurotus (enzymology)</term><term>Sequence Alignment (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Chromatographie en phase liquide à haute performance (MeSH)</term><term>Domaine catalytique (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Lignine (métabolisme)</term><term>Manganèse (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Peroxidases (isolement et purification)</term><term>Peroxidases (métabolisme)</term><term>Pleurotus (enzymologie)</term><term>Séquence d'acides aminés (MeSH)</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>Lignin</term><term>Manganese</term><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="isolement et purification" xml:lang="fr"><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Lignine</term><term>Manganèse</term><term>Peroxidases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Catalytic Domain</term><term>Chromatography, High Pressure Liquid</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Sequence Alignment</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Chromatographie en phase liquide à haute performance</term><term>Domaine catalytique</term><term>Données de séquences moléculaires</term><term>Modèles moléculaires</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Two major peroxidases are secreted by the fungus Pleurotus eryngii in lignocellulose cultures. One is similar to Phanerochaete chrysosporium manganese-dependent peroxidase. The second protein (PS1), although catalyzing the oxidation of Mn2+ to Mn3+ by H2O2, differs from the above enzymes by its manganese-independent activity enabling it to oxidize substituted phenols and synthetic dyes, as well as the lignin peroxidase (LiP) substrate veratryl alcohol. This is by a mechanism similar to that reported for LiP, as evidenced by p-dimethoxybenzene oxidation yielding benzoquinone. The apparent kinetic constants showed high activity on Mn2+, but methoxyhydroquinone was the natural substrate with the highest enzyme affinity (this and other phenolic substrates are not efficiently oxidized by the P. chrysosporium peroxidases). A three-dimensional model was built using crystal models from four fungal peroxidase as templates. The model suggests high structural affinity of this versatile peroxidase with LiP but shows a putative Mn2+ binding site near the internal heme propionate, involving Glu36, Glu40, and Asp181. A specific substrate interaction site for Mn2+ is supported by kinetic data showing noncompetitive inhibition with other peroxidase substrates. Moreover, residues reported as involved in LiP interaction with veratryl alcohol and other aromatic substrates are present in peroxidase PS1 such as His82 at the heme-channel opening, which is remarkably similar to that of P. chrysosporium LiP, and Trp170 at the protein surface. These residues could be involved in two different hypothetical long range electron transfer pathways from substrate (His82-Ala83-Asn84-His47-heme and Trp170-Leu171-heme) similar to those postulated for LiP.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10187820</PMID><DateCompleted><Year>1999</Year><Month>05</Month><Day>03</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>274</Volume><Issue>15</Issue><PubDate><Year>1999</Year><Month>Apr</Month><Day>09</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites.</ArticleTitle><Pagination><MedlinePgn>10324-30</MedlinePgn></Pagination><Abstract><AbstractText>Two major peroxidases are secreted by the fungus Pleurotus eryngii in lignocellulose cultures. One is similar to Phanerochaete chrysosporium manganese-dependent peroxidase. The second protein (PS1), although catalyzing the oxidation of Mn2+ to Mn3+ by H2O2, differs from the above enzymes by its manganese-independent activity enabling it to oxidize substituted phenols and synthetic dyes, as well as the lignin peroxidase (LiP) substrate veratryl alcohol. This is by a mechanism similar to that reported for LiP, as evidenced by p-dimethoxybenzene oxidation yielding benzoquinone. The apparent kinetic constants showed high activity on Mn2+, but methoxyhydroquinone was the natural substrate with the highest enzyme affinity (this and other phenolic substrates are not efficiently oxidized by the P. chrysosporium peroxidases). A three-dimensional model was built using crystal models from four fungal peroxidase as templates. The model suggests high structural affinity of this versatile peroxidase with LiP but shows a putative Mn2+ binding site near the internal heme propionate, involving Glu36, Glu40, and Asp181. A specific substrate interaction site for Mn2+ is supported by kinetic data showing noncompetitive inhibition with other peroxidase substrates. Moreover, residues reported as involved in LiP interaction with veratryl alcohol and other aromatic substrates are present in peroxidase PS1 such as His82 at the heme-channel opening, which is remarkably similar to that of P. chrysosporium LiP, and Trp170 at the protein surface. These residues could be involved in two different hypothetical long range electron transfer pathways from substrate (His82-Ala83-Asn84-His47-heme and Trp170-Leu171-heme) similar to those postulated for LiP.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Camarero</LastName><ForeName>S</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Velázquez 144, E-28006 Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sarkar</LastName><ForeName>S</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Ruiz-Dueñas</LastName><ForeName>F J</ForeName><Initials>FJ</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><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>AF175710</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>42Z2K6ZL8P</RegistryNumber><NameOfSubstance UI="D008345">Manganese</NameOfSubstance></Chemical><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="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008345" MajorTopicYN="N">Manganese</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</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="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020076" MajorTopicYN="N">Pleurotus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1999</Year><Month>4</Month><Day>3</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1999</Year><Month>4</Month><Day>3</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1999</Year><Month>4</Month><Day>3</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10187820</ArticleId><ArticleId IdType="doi">10.1074/jbc.274.15.10324</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Espagne</li></country><region><li>Communauté de Madrid</li></region></list><tree><noCountry><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="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><name sortKey="Sarkar, S" sort="Sarkar, S" uniqKey="Sarkar S" first="S" last="Sarkar">S. Sarkar</name></noCountry><country name="Espagne"><region name="Communauté de Madrid"><name sortKey="Camarero, S" sort="Camarero, S" uniqKey="Camarero S" first="S" last="Camarero">S. Camarero</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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