Purification and characterization of peroxidases correlated with lignification in poplar xylem.
Identifieur interne : 004926 ( Main/Exploration ); précédent : 004925; suivant : 004927Purification and characterization of peroxidases correlated with lignification in poplar xylem.
Auteurs : J H Christensen [Belgique] ; G. Bauw ; K G Welinder ; M. Van Montagu ; W. BoerjanSource :
- Plant physiology [ 0032-0889 ] ; 1998.
Descripteurs français
- KwdFr :
- Acides aminés (analyse), Arbres (enzymologie), Arbres (génétique), Arbres (métabolisme), Données de séquences moléculaires (MeSH), Fragments peptidiques (génétique), Fragments peptidiques (isolement et purification), Glycosylation (MeSH), Isoenzymes (génétique), Isoenzymes (isolement et purification), Isoenzymes (métabolisme), Lignine (biosynthèse), Masse moléculaire (MeSH), Peroxidases (génétique), Peroxidases (isolement et purification), Peroxidases (métabolisme), Point isoélectrique (MeSH), Similitude de séquences d'acides aminés (MeSH), Spécificité du substrat (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- analyse : Acides aminés.
- biosynthèse : Lignine.
- enzymologie : Arbres.
- génétique : Arbres, Fragments peptidiques, Isoenzymes, Peroxidases.
- isolement et purification : Fragments peptidiques, Isoenzymes, Peroxidases.
- métabolisme : Arbres, Isoenzymes, Peroxidases.
- Données de séquences moléculaires, Glycosylation, Masse moléculaire, Point isoélectrique, Similitude de séquences d'acides aminés, Spécificité du substrat, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Amino Acids (analysis), Glycosylation (MeSH), Isoelectric Point (MeSH), Isoenzymes (genetics), Isoenzymes (isolation & purification), Isoenzymes (metabolism), Lignin (biosynthesis), Molecular Sequence Data (MeSH), Molecular Weight (MeSH), Peptide Fragments (genetics), Peptide Fragments (isolation & purification), Peroxidases (genetics), Peroxidases (isolation & purification), Peroxidases (metabolism), Sequence Homology, Amino Acid (MeSH), Substrate Specificity (MeSH), Trees (enzymology), Trees (genetics), Trees (metabolism).
- MESH :
- chemical , analysis : Amino Acids.
- chemical , biosynthesis : Lignin.
- chemical , genetics : Isoenzymes, Peptide Fragments, Peroxidases.
- chemical , isolation & purification : Isoenzymes, Peptide Fragments, Peroxidases.
- chemical , metabolism : Isoenzymes, Peroxidases.
- enzymology : Trees.
- genetics : Trees.
- metabolism : Trees.
- Amino Acid Sequence, Glycosylation, Isoelectric Point, Molecular Sequence Data, Molecular Weight, Sequence Homology, Amino Acid, Substrate Specificity.
Abstract
Lignin is an integral cell wall component of all vascular plants. Peroxidases are widely believed to catalyze the last enzymatic step in the biosynthesis of lignin, the dehydrogenation of the p-coumaryl alcohols. As the first stage in identifying lignin-specific peroxidase isoenzymes, the classical anionic peroxidases found in the xylem of poplar (Populus trichocarpa Trichobel) were purified and characterized. Five different poplar xylem peroxidases (PXP 1, PXP 2, PXP 3-4, PXP 5, and PXP 6) were isolated. All five peroxidases were strongly glycosylated (3.6% to 4.9% N-glucosamine), with apparent molecular masses between 46 and 54 kD and pI values between pH 3.1 and 3.8. Two of the five isolated peroxidases (PXP 3-4 and PXP 5) could oxidize the lignin monomer analog syringaldazine, an activity previously correlated with lignification in poplar. Because these isoenzymes were specifically or preferentially expressed in xylem, PXP 3-4 and PXP 5 are suggested to be involved in lignin polymerization.
DOI: 10.1104/pp.118.1.125
PubMed: 9733532
PubMed Central: PMC34849
Affiliations:
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Ledeganckstraat 35, B-9000 Gent, Belgium.</nlm:affiliation><country xml:lang="fr">Belgique</country><wicri:regionArea>Laboratorium voor Genetica, Departement Genetica, Vlaams Interuniversitair Instituut voor Biotechnologie, Universiteit Gent, K.L. Ledeganckstraat 35, B-9000 Gent</wicri:regionArea><orgName type="university">Université de Gand</orgName><placeName><settlement type="city">Gand</settlement><region>Région flamande</region><region type="district" nuts="2">Province de Flandre-Orientale</region></placeName></affiliation></author><author><name sortKey="Bauw, G" sort="Bauw, G" uniqKey="Bauw G" first="G" last="Bauw">G. Bauw</name></author><author><name sortKey="Welinder, K G" sort="Welinder, K G" uniqKey="Welinder K" first="K G" last="Welinder">K G Welinder</name></author><author><name sortKey="Van Montagu, M" sort="Van Montagu, M" uniqKey="Van Montagu M" first="M" last="Van Montagu">M. 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Peroxidases are widely believed to catalyze the last enzymatic step in the biosynthesis of lignin, the dehydrogenation of the p-coumaryl alcohols. As the first stage in identifying lignin-specific peroxidase isoenzymes, the classical anionic peroxidases found in the xylem of poplar (Populus trichocarpa Trichobel) were purified and characterized. Five different poplar xylem peroxidases (PXP 1, PXP 2, PXP 3-4, PXP 5, and PXP 6) were isolated. All five peroxidases were strongly glycosylated (3.6% to 4.9% N-glucosamine), with apparent molecular masses between 46 and 54 kD and pI values between pH 3.1 and 3.8. Two of the five isolated peroxidases (PXP 3-4 and PXP 5) could oxidize the lignin monomer analog syringaldazine, an activity previously correlated with lignification in poplar. Because these isoenzymes were specifically or preferentially expressed in xylem, PXP 3-4 and PXP 5 are suggested to be involved in lignin polymerization.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9733532</PMID><DateCompleted><Year>1998</Year><Month>11</Month><Day>18</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>14</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0032-0889</ISSN><JournalIssue CitedMedium="Print"><Volume>118</Volume><Issue>1</Issue><PubDate><Year>1998</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Plant physiology</Title><ISOAbbreviation>Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>Purification and characterization of peroxidases correlated with lignification in poplar xylem.</ArticleTitle><Pagination><MedlinePgn>125-35</MedlinePgn></Pagination><Abstract><AbstractText>Lignin is an integral cell wall component of all vascular plants. Peroxidases are widely believed to catalyze the last enzymatic step in the biosynthesis of lignin, the dehydrogenation of the p-coumaryl alcohols. As the first stage in identifying lignin-specific peroxidase isoenzymes, the classical anionic peroxidases found in the xylem of poplar (Populus trichocarpa Trichobel) were purified and characterized. Five different poplar xylem peroxidases (PXP 1, PXP 2, PXP 3-4, PXP 5, and PXP 6) were isolated. All five peroxidases were strongly glycosylated (3.6% to 4.9% N-glucosamine), with apparent molecular masses between 46 and 54 kD and pI values between pH 3.1 and 3.8. Two of the five isolated peroxidases (PXP 3-4 and PXP 5) could oxidize the lignin monomer analog syringaldazine, an activity previously correlated with lignification in poplar. Because these isoenzymes were specifically or preferentially expressed in xylem, PXP 3-4 and PXP 5 are suggested to be involved in lignin polymerization.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Christensen</LastName><ForeName>J H</ForeName><Initials>JH</Initials><AffiliationInfo><Affiliation>Laboratorium voor Genetica, Departement Genetica, Vlaams Interuniversitair Instituut voor Biotechnologie, Universiteit Gent, K.L. Ledeganckstraat 35, B-9000 Gent, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bauw</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Welinder</LastName><ForeName>K G</ForeName><Initials>KG</Initials></Author><Author ValidYN="Y"><LastName>Van Montagu</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Boerjan</LastName><ForeName>W</ForeName><Initials>W</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></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant Physiol</MedlineTA><NlmUniqueID>0401224</NlmUniqueID><ISSNLinking>0032-0889</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007527">Isoenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010446">Peptide Fragments</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="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006031" MajorTopicYN="N">Glycosylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007526" MajorTopicYN="N">Isoelectric Point</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010446" MajorTopicYN="N">Peptide Fragments</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014197" MajorTopicYN="N">Trees</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1998</Year><Month>9</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1998</Year><Month>9</Month><Day>11</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1998</Year><Month>9</Month><Day>11</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9733532</ArticleId><ArticleId IdType="pmc">PMC34849</ArticleId><ArticleId IdType="doi">10.1104/pp.118.1.125</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Biochem J. 1955 Jan;59(1):110-21</Citation><ArticleIdList><ArticleId IdType="pubmed">14351150</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1970 Aug 15;227(5259):680-5</Citation><ArticleIdList><ArticleId IdType="pubmed">5432063</ArticleId></ArticleIdList></Reference><Reference><Citation>Planta. 1980 Feb;147(5):467-70</Citation><ArticleIdList><ArticleId 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sort="Bauw, G" uniqKey="Bauw G" first="G" last="Bauw">G. Bauw</name><name sortKey="Boerjan, W" sort="Boerjan, W" uniqKey="Boerjan W" first="W" last="Boerjan">W. Boerjan</name><name sortKey="Van Montagu, M" sort="Van Montagu, M" uniqKey="Van Montagu M" first="M" last="Van Montagu">M. Van Montagu</name><name sortKey="Welinder, K G" sort="Welinder, K G" uniqKey="Welinder K" first="K G" last="Welinder">K G Welinder</name></noCountry><country name="Belgique"><region name="Région flamande"><name sortKey="Christensen, J H" sort="Christensen, J H" uniqKey="Christensen J" first="J H" last="Christensen">J H Christensen</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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