Role of Tyr residues on the protein surface of cationic cell-wall-peroxidase (CWPO-C) from poplar: potential oxidation sites for oxidative polymerization of lignin.
Identifieur interne : 003825 ( Main/Exploration ); précédent : 003824; suivant : 003826Role of Tyr residues on the protein surface of cationic cell-wall-peroxidase (CWPO-C) from poplar: potential oxidation sites for oxidative polymerization of lignin.
Auteurs : Shinya Sasaki [Japon] ; Daisuke Nonaka ; Hiroyuki Wariishi ; Yuji Tsutsumi ; Ryuichiro KondoSource :
- Phytochemistry [ 0031-9422 ] ; 2008.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Cations (composition chimique), Données de séquences moléculaires (MeSH), Hème (composition chimique), Lignine (composition chimique), Lignine (métabolisme), Masse moléculaire (MeSH), Modèles moléculaires (MeSH), Oxydoréduction (MeSH), Paroi cellulaire (enzymologie), Peroxidases (composition chimique), Peroxidases (génétique), Peroxidases (métabolisme), Populus (enzymologie), Populus (génétique), Propriétés de surface (MeSH), Spécificité du substrat (MeSH), Structure moléculaire (MeSH), Tyrosine (génétique), Tyrosine (métabolisme).
- MESH :
- composition chimique : Cations, Hème, Lignine, Peroxidases.
- enzymologie : Paroi cellulaire, Populus.
- génétique : Peroxidases, Populus, Tyrosine.
- métabolisme : Lignine, Peroxidases, Tyrosine.
- Alignement de séquences, Données de séquences moléculaires, Masse moléculaire, Modèles moléculaires, Oxydoréduction, Propriétés de surface, Spécificité du substrat, Structure moléculaire.
English descriptors
- KwdEn :
- Cations (chemistry), Cell Wall (enzymology), Heme (chemistry), Lignin (chemistry), Lignin (metabolism), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Molecular Structure (MeSH), Molecular Weight (MeSH), Oxidation-Reduction (MeSH), Peroxidases (chemistry), Peroxidases (genetics), Peroxidases (metabolism), Populus (enzymology), Populus (genetics), Sequence Alignment (MeSH), Substrate Specificity (MeSH), Surface Properties (MeSH), Tyrosine (genetics), Tyrosine (metabolism).
- MESH :
- chemical , chemistry : Cations, Heme, Lignin, Peroxidases.
- enzymology : Cell Wall, Populus.
- chemical , genetics : Peroxidases, Populus, Tyrosine.
- chemical , metabolism : Lignin, Peroxidases, Tyrosine.
- Models, Molecular, Molecular Sequence Data, Molecular Structure, Molecular Weight, Oxidation-Reduction, Sequence Alignment, Substrate Specificity, Surface Properties.
Abstract
It was previously reported that an unique peroxidase isoenzyme, cationic cell-wall-bound peroxidase (CWPO-C), from poplar callus oxidizes sinapyl alcohol, ferrocytochrome c and synthetic lignin polymers, unlike other plant peroxidases. Here, the catalytic mechanism of CWPO-C was investigated using chemical modification and homology modeling. The simulated CWPO-C structure predicts that the entrance to the heme pocket of CWPO-C is the same size as those of other plant peroxidases, suggesting that ferrocytochrome c and synthetic lignin polymers cannot interact with the heme of CWPO-C. Since Trp and Tyr residues are redox-active, such residues located on the protein surface were predicted to be active sites for CWPO-C. Modification of CWPO-C Trp residues did not suppress its oxidation activities toward guaiacol and syringaldazine. On the other hand, modification of CWPO-C Tyr residues using tetranitromethane strongly suppressed its oxidation activities toward syringaldazine and 2,6-dimethoxyphenol by 90%, respectively, and also suppressed its guaiacol oxidation activity to a lesser extent. Ferrocytochrome c was not oxidized by Tyr-modified CWPO-C. These results indicate that the Tyr residues in CWPO-C mediate its oxidation of syringyl compounds and high-molecular-weight substrates. Homology modeling indicates that Tyr-177 and Tyr-74 are located near the heme and exposed on the protein surface of CWPO-C. These results suggest that Tyr residues on the protein surface are considered to be important for the oxidation activities of CWPO-C with a wide range of substrates, and potentially unique oxidation sites for the plant peroxidase family.
DOI: 10.1016/j.phytochem.2007.08.020
PubMed: 17910963
Affiliations:
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sortKey="Nonaka, Daisuke" sort="Nonaka, Daisuke" uniqKey="Nonaka D" first="Daisuke" last="Nonaka">Daisuke Nonaka</name></author><author><name sortKey="Wariishi, Hiroyuki" sort="Wariishi, Hiroyuki" uniqKey="Wariishi H" first="Hiroyuki" last="Wariishi">Hiroyuki Wariishi</name></author><author><name sortKey="Tsutsumi, Yuji" sort="Tsutsumi, Yuji" uniqKey="Tsutsumi Y" first="Yuji" last="Tsutsumi">Yuji Tsutsumi</name></author><author><name sortKey="Kondo, Ryuichiro" sort="Kondo, Ryuichiro" uniqKey="Kondo R" first="Ryuichiro" last="Kondo">Ryuichiro Kondo</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:17910963</idno><idno type="pmid">17910963</idno><idno type="doi">10.1016/j.phytochem.2007.08.020</idno><idno type="wicri:Area/Main/Corpus">003A56</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">003A56</idno><idno 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Kyūshū</orgName><placeName><settlement type="city">Fukuoka</settlement><region type="province">Kyūshū</region><region type="prefecture">Préfecture de Fukuoka</region></placeName></affiliation></author><author><name sortKey="Nonaka, Daisuke" sort="Nonaka, Daisuke" uniqKey="Nonaka D" first="Daisuke" last="Nonaka">Daisuke Nonaka</name></author><author><name sortKey="Wariishi, Hiroyuki" sort="Wariishi, Hiroyuki" uniqKey="Wariishi H" first="Hiroyuki" last="Wariishi">Hiroyuki Wariishi</name></author><author><name sortKey="Tsutsumi, Yuji" sort="Tsutsumi, Yuji" uniqKey="Tsutsumi Y" first="Yuji" last="Tsutsumi">Yuji Tsutsumi</name></author><author><name sortKey="Kondo, Ryuichiro" sort="Kondo, Ryuichiro" uniqKey="Kondo R" first="Ryuichiro" last="Kondo">Ryuichiro Kondo</name></author></analytic><series><title level="j">Phytochemistry</title><idno type="ISSN">0031-9422</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cations (chemistry)</term><term>Cell Wall (enzymology)</term><term>Heme (chemistry)</term><term>Lignin (chemistry)</term><term>Lignin (metabolism)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Molecular Structure (MeSH)</term><term>Molecular Weight (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (chemistry)</term><term>Peroxidases (genetics)</term><term>Peroxidases (metabolism)</term><term>Populus (enzymology)</term><term>Populus (genetics)</term><term>Sequence Alignment (MeSH)</term><term>Substrate Specificity (MeSH)</term><term>Surface Properties (MeSH)</term><term>Tyrosine (genetics)</term><term>Tyrosine (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Cations (composition chimique)</term><term>Données de séquences moléculaires (MeSH)</term><term>Hème (composition chimique)</term><term>Lignine (composition chimique)</term><term>Lignine (métabolisme)</term><term>Masse moléculaire (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Paroi cellulaire (enzymologie)</term><term>Peroxidases (composition chimique)</term><term>Peroxidases (génétique)</term><term>Peroxidases (métabolisme)</term><term>Populus (enzymologie)</term><term>Populus (génétique)</term><term>Propriétés de surface (MeSH)</term><term>Spécificité du substrat (MeSH)</term><term>Structure moléculaire (MeSH)</term><term>Tyrosine (génétique)</term><term>Tyrosine (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cations</term><term>Heme</term><term>Lignin</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cations</term><term>Hème</term><term>Lignine</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Paroi cellulaire</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Cell Wall</term><term>Populus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peroxidases</term><term>Populus</term><term>Tyrosine</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Peroxidases</term><term>Populus</term><term>Tyrosine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lignin</term><term>Peroxidases</term><term>Tyrosine</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Lignine</term><term>Peroxidases</term><term>Tyrosine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Molecular Structure</term><term>Molecular Weight</term><term>Oxidation-Reduction</term><term>Sequence Alignment</term><term>Substrate Specificity</term><term>Surface Properties</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Données de séquences moléculaires</term><term>Masse moléculaire</term><term>Modèles moléculaires</term><term>Oxydoréduction</term><term>Propriétés de surface</term><term>Spécificité du substrat</term><term>Structure moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">It was previously reported that an unique peroxidase isoenzyme, cationic cell-wall-bound peroxidase (CWPO-C), from poplar callus oxidizes sinapyl alcohol, ferrocytochrome c and synthetic lignin polymers, unlike other plant peroxidases. Here, the catalytic mechanism of CWPO-C was investigated using chemical modification and homology modeling. The simulated CWPO-C structure predicts that the entrance to the heme pocket of CWPO-C is the same size as those of other plant peroxidases, suggesting that ferrocytochrome c and synthetic lignin polymers cannot interact with the heme of CWPO-C. Since Trp and Tyr residues are redox-active, such residues located on the protein surface were predicted to be active sites for CWPO-C. Modification of CWPO-C Trp residues did not suppress its oxidation activities toward guaiacol and syringaldazine. On the other hand, modification of CWPO-C Tyr residues using tetranitromethane strongly suppressed its oxidation activities toward syringaldazine and 2,6-dimethoxyphenol by 90%, respectively, and also suppressed its guaiacol oxidation activity to a lesser extent. Ferrocytochrome c was not oxidized by Tyr-modified CWPO-C. These results indicate that the Tyr residues in CWPO-C mediate its oxidation of syringyl compounds and high-molecular-weight substrates. Homology modeling indicates that Tyr-177 and Tyr-74 are located near the heme and exposed on the protein surface of CWPO-C. These results suggest that Tyr residues on the protein surface are considered to be important for the oxidation activities of CWPO-C with a wide range of substrates, and potentially unique oxidation sites for the plant peroxidase family.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17910963</PMID><DateCompleted><Year>2008</Year><Month>05</Month><Day>07</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0031-9422</ISSN><JournalIssue CitedMedium="Print"><Volume>69</Volume><Issue>2</Issue><PubDate><Year>2008</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Phytochemistry</Title><ISOAbbreviation>Phytochemistry</ISOAbbreviation></Journal><ArticleTitle>Role of Tyr residues on the protein surface of cationic cell-wall-peroxidase (CWPO-C) from poplar: potential oxidation sites for oxidative polymerization of lignin.</ArticleTitle><Pagination><MedlinePgn>348-55</MedlinePgn></Pagination><Abstract><AbstractText>It was previously reported that an unique peroxidase isoenzyme, cationic cell-wall-bound peroxidase (CWPO-C), from poplar callus oxidizes sinapyl alcohol, ferrocytochrome c and synthetic lignin polymers, unlike other plant peroxidases. Here, the catalytic mechanism of CWPO-C was investigated using chemical modification and homology modeling. The simulated CWPO-C structure predicts that the entrance to the heme pocket of CWPO-C is the same size as those of other plant peroxidases, suggesting that ferrocytochrome c and synthetic lignin polymers cannot interact with the heme of CWPO-C. Since Trp and Tyr residues are redox-active, such residues located on the protein surface were predicted to be active sites for CWPO-C. Modification of CWPO-C Trp residues did not suppress its oxidation activities toward guaiacol and syringaldazine. On the other hand, modification of CWPO-C Tyr residues using tetranitromethane strongly suppressed its oxidation activities toward syringaldazine and 2,6-dimethoxyphenol by 90%, respectively, and also suppressed its guaiacol oxidation activity to a lesser extent. Ferrocytochrome c was not oxidized by Tyr-modified CWPO-C. These results indicate that the Tyr residues in CWPO-C mediate its oxidation of syringyl compounds and high-molecular-weight substrates. Homology modeling indicates that Tyr-177 and Tyr-74 are located near the heme and exposed on the protein surface of CWPO-C. These results suggest that Tyr residues on the protein surface are considered to be important for the oxidation activities of CWPO-C with a wide range of substrates, and potentially unique oxidation sites for the plant peroxidase family.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sasaki</LastName><ForeName>Shinya</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Forest and Forest Products Sciences, Kyushu University, 6-10-1, Hakozaki, Higashiku, Fukuoka 812-8581, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nonaka</LastName><ForeName>Daisuke</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Wariishi</LastName><ForeName>Hiroyuki</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Tsutsumi</LastName><ForeName>Yuji</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Kondo</LastName><ForeName>Ryuichiro</ForeName><Initials>R</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>10</Month><Day>29</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Phytochemistry</MedlineTA><NlmUniqueID>0151434</NlmUniqueID><ISSNLinking>0031-9422</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002412">Cations</NameOfSubstance></Chemical><Chemical><RegistryNumber>42HK56048U</RegistryNumber><NameOfSubstance UI="D014443">Tyrosine</NameOfSubstance></Chemical><Chemical><RegistryNumber>42VZT0U6YR</RegistryNumber><NameOfSubstance UI="D006418">Heme</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></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002412" MajorTopicYN="N">Cations</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002473" MajorTopicYN="N">Cell Wall</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006418" MajorTopicYN="N">Heme</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">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="D015394" MajorTopicYN="N">Molecular Structure</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="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013499" MajorTopicYN="N">Surface Properties</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014443" MajorTopicYN="N">Tyrosine</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year><Month>10</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2007</Year><Month>07</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2007</Year><Month>08</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>10</Month><Day>4</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>5</Month><Day>8</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>10</Month><Day>4</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17910963</ArticleId><ArticleId IdType="pii">S0031-9422(07)00507-9</ArticleId><ArticleId IdType="doi">10.1016/j.phytochem.2007.08.020</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Kyūshū</li><li>Préfecture de Fukuoka</li></region><settlement><li>Fukuoka</li></settlement><orgName><li>Université de Kyūshū</li></orgName></list><tree><noCountry><name sortKey="Kondo, Ryuichiro" sort="Kondo, Ryuichiro" uniqKey="Kondo R" first="Ryuichiro" last="Kondo">Ryuichiro Kondo</name><name sortKey="Nonaka, Daisuke" sort="Nonaka, Daisuke" uniqKey="Nonaka D" first="Daisuke" last="Nonaka">Daisuke Nonaka</name><name sortKey="Tsutsumi, Yuji" sort="Tsutsumi, Yuji" uniqKey="Tsutsumi Y" first="Yuji" last="Tsutsumi">Yuji Tsutsumi</name><name sortKey="Wariishi, Hiroyuki" sort="Wariishi, Hiroyuki" uniqKey="Wariishi H" first="Hiroyuki" last="Wariishi">Hiroyuki Wariishi</name></noCountry><country name="Japon"><region name="Kyūshū"><name sortKey="Sasaki, Shinya" sort="Sasaki, Shinya" uniqKey="Sasaki S" first="Shinya" last="Sasaki">Shinya Sasaki</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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