Determination of a catalytic tyrosine in Trametes cervina lignin peroxidase with chemical modification techniques.
Identifieur interne : 000513 ( Main/Exploration ); précédent : 000512; suivant : 000514Determination of a catalytic tyrosine in Trametes cervina lignin peroxidase with chemical modification techniques.
Auteurs : Yuta Miki [Japon] ; Hirofumi Ichinose ; Hiroyuki WariishiSource :
- Biotechnology letters [ 1573-6776 ] ; 2011.
Descripteurs français
- KwdFr :
- Alcools benzyliques (métabolisme), Domaine catalytique (MeSH), Maturation post-traductionnelle des protéines (MeSH), Modèles moléculaires (MeSH), N-Bromo-succinimide (métabolisme), Peroxidases (composition chimique), Peroxidases (métabolisme), Phanerochaete (enzymologie), Structure tertiaire des protéines (MeSH), Trametes (enzymologie), Tyrosine (composition chimique), Tyrosine (métabolisme), Tétranitro-méthane (métabolisme).
- MESH :
- composition chimique : Peroxidases, Tyrosine.
- enzymologie : Phanerochaete, Trametes.
- métabolisme : Alcools benzyliques, N-Bromo-succinimide, Peroxidases, Tyrosine, Tétranitro-méthane.
- Domaine catalytique, Maturation post-traductionnelle des protéines, Modèles moléculaires, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Benzyl Alcohols (metabolism), Bromosuccinimide (metabolism), Catalytic Domain (MeSH), Models, Molecular (MeSH), Peroxidases (chemistry), Peroxidases (metabolism), Phanerochaete (enzymology), Protein Processing, Post-Translational (MeSH), Protein Structure, Tertiary (MeSH), Tetranitromethane (metabolism), Trametes (enzymology), Tyrosine (chemistry), Tyrosine (metabolism).
- MESH :
- chemical , chemistry : Peroxidases, Tyrosine.
- chemical , metabolism : Benzyl Alcohols, Bromosuccinimide, Peroxidases, Tetranitromethane, Tyrosine.
- enzymology : Phanerochaete, Trametes.
- Catalytic Domain, Models, Molecular, Protein Processing, Post-Translational, Protein Structure, Tertiary.
Abstract
Trametes cervina lignin peroxidase (LiP) lacks a catalytic tryptophan strictly conserved in other LiP and versatile peroxidases. It contains tyrosine(181) at the potential catalytic site. This protein and the well-characterized Phanerochaete chrysosporium LiP with the catalytic tryptophan(171) have been chemically modified: the tryptophan-specific modification with N-bromosuccinimide sufficiently disrupted oxidation of veratryl alcohol by P. chrysosporium LiP, whereas the activity of T. cervina LiP was not affected, suggesting no catalytic tryptophan in T. cervina LiP. On the other hand, the tyrosine-specific modification with tetranitromethane did not affect the activities of P. chrysosporium LiP lacking tyrosine but inactivated T. cervina LiP due to the nitration of tyrosine(181). These results strongly suggest that tyrosine(181) is at the catalytic site in T. cervina LiP.
DOI: 10.1007/s10529-011-0571-2
PubMed: 21373922
Affiliations:
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Ichinose</name></author><author><name sortKey="Wariishi, Hiroyuki" sort="Wariishi, Hiroyuki" uniqKey="Wariishi H" first="Hiroyuki" last="Wariishi">Hiroyuki Wariishi</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2011">2011</date><idno type="RBID">pubmed:21373922</idno><idno type="pmid">21373922</idno><idno type="doi">10.1007/s10529-011-0571-2</idno><idno type="wicri:Area/Main/Corpus">000508</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000508</idno><idno type="wicri:Area/Main/Curation">000508</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000508</idno><idno type="wicri:Area/Main/Exploration">000508</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Determination of a catalytic tyrosine in Trametes cervina lignin peroxidase with chemical modification techniques.</title><author><name sortKey="Miki, Yuta" sort="Miki, Yuta" uniqKey="Miki Y" first="Yuta" last="Miki">Yuta Miki</name><affiliation wicri:level="4"><nlm:affiliation>Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Higashi-ku, Fukuoka, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Higashi-ku, Fukuoka</wicri:regionArea><orgName type="university">Université de 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="Ichinose, Hirofumi" sort="Ichinose, Hirofumi" uniqKey="Ichinose H" first="Hirofumi" last="Ichinose">Hirofumi Ichinose</name></author><author><name sortKey="Wariishi, Hiroyuki" sort="Wariishi, Hiroyuki" uniqKey="Wariishi H" first="Hiroyuki" last="Wariishi">Hiroyuki Wariishi</name></author></analytic><series><title level="j">Biotechnology letters</title><idno 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(métabolisme)</term><term>Peroxidases (composition chimique)</term><term>Peroxidases (métabolisme)</term><term>Phanerochaete (enzymologie)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Trametes (enzymologie)</term><term>Tyrosine (composition chimique)</term><term>Tyrosine (métabolisme)</term><term>Tétranitro-méthane (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peroxidases</term><term>Tyrosine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Benzyl Alcohols</term><term>Bromosuccinimide</term><term>Peroxidases</term><term>Tetranitromethane</term><term>Tyrosine</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Peroxidases</term><term>Tyrosine</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term><term>Trametes</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term><term>Trametes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Alcools benzyliques</term><term>N-Bromo-succinimide</term><term>Peroxidases</term><term>Tyrosine</term><term>Tétranitro-méthane</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Catalytic Domain</term><term>Models, Molecular</term><term>Protein Processing, Post-Translational</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Domaine catalytique</term><term>Maturation post-traductionnelle des protéines</term><term>Modèles moléculaires</term><term>Structure tertiaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Trametes cervina lignin peroxidase (LiP) lacks a catalytic tryptophan strictly conserved in other LiP and versatile peroxidases. It contains tyrosine(181) at the potential catalytic site. This protein and the well-characterized Phanerochaete chrysosporium LiP with the catalytic tryptophan(171) have been chemically modified: the tryptophan-specific modification with N-bromosuccinimide sufficiently disrupted oxidation of veratryl alcohol by P. chrysosporium LiP, whereas the activity of T. cervina LiP was not affected, suggesting no catalytic tryptophan in T. cervina LiP. On the other hand, the tyrosine-specific modification with tetranitromethane did not affect the activities of P. chrysosporium LiP lacking tyrosine but inactivated T. cervina LiP due to the nitration of tyrosine(181). These results strongly suggest that tyrosine(181) is at the catalytic site in T. cervina LiP.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21373922</PMID><DateCompleted><Year>2011</Year><Month>10</Month><Day>04</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1573-6776</ISSN><JournalIssue CitedMedium="Internet"><Volume>33</Volume><Issue>7</Issue><PubDate><Year>2011</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Biotechnology letters</Title><ISOAbbreviation>Biotechnol Lett</ISOAbbreviation></Journal><ArticleTitle>Determination of a catalytic tyrosine in Trametes cervina lignin peroxidase with chemical modification techniques.</ArticleTitle><Pagination><MedlinePgn>1423-7</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s10529-011-0571-2</ELocationID><Abstract><AbstractText>Trametes cervina lignin peroxidase (LiP) lacks a catalytic tryptophan strictly conserved in other LiP and versatile peroxidases. It contains tyrosine(181) at the potential catalytic site. This protein and the well-characterized Phanerochaete chrysosporium LiP with the catalytic tryptophan(171) have been chemically modified: the tryptophan-specific modification with N-bromosuccinimide sufficiently disrupted oxidation of veratryl alcohol by P. chrysosporium LiP, whereas the activity of T. cervina LiP was not affected, suggesting no catalytic tryptophan in T. cervina LiP. On the other hand, the tyrosine-specific modification with tetranitromethane did not affect the activities of P. chrysosporium LiP lacking tyrosine but inactivated T. cervina LiP due to the nitration of tyrosine(181). These results strongly suggest that tyrosine(181) is at the catalytic site in T. cervina LiP.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Miki</LastName><ForeName>Yuta</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Higashi-ku, Fukuoka, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ichinose</LastName><ForeName>Hirofumi</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Wariishi</LastName><ForeName>Hiroyuki</ForeName><Initials>H</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>03</Month><Day>04</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biotechnol Lett</MedlineTA><NlmUniqueID>8008051</NlmUniqueID><ISSNLinking>0141-5492</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001592">Benzyl Alcohols</NameOfSubstance></Chemical><Chemical><RegistryNumber>42HK56048U</RegistryNumber><NameOfSubstance UI="D014443">Tyrosine</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>K1G7CKU98F</RegistryNumber><NameOfSubstance UI="D013774">Tetranitromethane</NameOfSubstance></Chemical><Chemical><RegistryNumber>K8G1F2UCJF</RegistryNumber><NameOfSubstance UI="D001974">Bromosuccinimide</NameOfSubstance></Chemical><Chemical><RegistryNumber>MB4T4A711H</RegistryNumber><NameOfSubstance UI="C042197">veratryl alcohol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001592" MajorTopicYN="N">Benzyl Alcohols</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001974" MajorTopicYN="N">Bromosuccinimide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" 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MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2011</Year><Month>01</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2011</Year><Month>02</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>3</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>3</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2011</Year><Month>10</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">21373922</ArticleId><ArticleId IdType="doi">10.1007/s10529-011-0571-2</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="Ichinose, Hirofumi" sort="Ichinose, Hirofumi" uniqKey="Ichinose H" first="Hirofumi" last="Ichinose">Hirofumi Ichinose</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="Miki, Yuta" sort="Miki, Yuta" uniqKey="Miki Y" first="Yuta" last="Miki">Yuta Miki</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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