Characterization of bispecific caffeic acid/5-hydroxyferulic acid O-methyltransferase from aspen.
Identifieur interne : 004C24 ( Main/Exploration ); précédent : 004C23; suivant : 004C25Characterization of bispecific caffeic acid/5-hydroxyferulic acid O-methyltransferase from aspen.
Auteurs : R C Bugos ; V L Chiang ; W H CampbellSource :
- Phytochemistry [ 0031-9422 ] ; 1992.
Descripteurs français
- KwdFr :
- Acides caféiques (métabolisme), Acides coumariques (métabolisme), Données de séquences moléculaires (MeSH), Methyltransferases (immunologie), Methyltransferases (isolement et purification), Methyltransferases (métabolisme), Plantes (enzymologie), Spécificité du substrat (MeSH), Séquence d'acides aminés (MeSH), Technique de Western (MeSH).
- MESH :
- enzymologie : Plantes.
- immunologie : Methyltransferases.
- isolement et purification : Methyltransferases.
- métabolisme : Acides caféiques, Acides coumariques, Methyltransferases.
- Données de séquences moléculaires, Spécificité du substrat, Séquence d'acides aminés, Technique de Western.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Blotting, Western (MeSH), Caffeic Acids (metabolism), Coumaric Acids (metabolism), Methyltransferases (immunology), Methyltransferases (isolation & purification), Methyltransferases (metabolism), Molecular Sequence Data (MeSH), Plants (enzymology), Substrate Specificity (MeSH).
- MESH :
- chemical , immunology : Methyltransferases.
- chemical , isolation & purification : Methyltransferases.
- chemical , metabolism : Caffeic Acids, Coumaric Acids, Methyltransferases.
- enzymology : Plants.
- Amino Acid Sequence, Blotting, Western, Molecular Sequence Data, Substrate Specificity.
Abstract
Bispecific O-methyltransferase (OMT, EC 2.1.1.68) which catalyses the meta-specific methylation of caffeic acid and 5-hydroxyferulic acid was purified to homogeneity from the developing secondary xylem of aspen (Populus tremuloides). The enzyme was purified by conventional techniques and affinity chromatography on S-adenosyl-L-homocysteine agarose using substrate elution. The enzyme has a M(r) of 40,000 as determined by SDS-PAGE. Amino acid sequences of three peptides produced from a proteolytic digest of bispecific OMT were obtained by automated Edman degradation. Polyclonal antibodies raised against the purified OMT reacted strongly to OMT in both purified and unpurified fractions in western blots. Addition of an equal concentration of anti-OMT IgG to crude extract protein inhibited OMT activity by more than 70%.
DOI: 10.1016/0031-9422(92)83093-e
PubMed: 1368360
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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uniqKey="Chiang V" first="V L" last="Chiang">V L Chiang</name></author><author><name sortKey="Campbell, W H" sort="Campbell, W H" uniqKey="Campbell W" first="W H" last="Campbell">W H Campbell</name></author></analytic><series><title level="j">Phytochemistry</title><idno type="ISSN">0031-9422</idno><imprint><date when="1992" type="published">1992</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Blotting, Western (MeSH)</term><term>Caffeic Acids (metabolism)</term><term>Coumaric Acids (metabolism)</term><term>Methyltransferases (immunology)</term><term>Methyltransferases (isolation & purification)</term><term>Methyltransferases (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Plants (enzymology)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides caféiques (métabolisme)</term><term>Acides coumariques (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Methyltransferases (immunologie)</term><term>Methyltransferases (isolement et purification)</term><term>Methyltransferases (métabolisme)</term><term>Plantes (enzymologie)</term><term>Spécificité du substrat (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Technique de Western (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Methyltransferases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Methyltransferases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Caffeic Acids</term><term>Coumaric Acids</term><term>Methyltransferases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Plantes</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Plants</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Methyltransferases</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Methyltransferases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides caféiques</term><term>Acides coumariques</term><term>Methyltransferases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Blotting, Western</term><term>Molecular Sequence Data</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Données de séquences moléculaires</term><term>Spécificité du substrat</term><term>Séquence d'acides aminés</term><term>Technique de Western</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Bispecific O-methyltransferase (OMT, EC 2.1.1.68) which catalyses the meta-specific methylation of caffeic acid and 5-hydroxyferulic acid was purified to homogeneity from the developing secondary xylem of aspen (Populus tremuloides). The enzyme was purified by conventional techniques and affinity chromatography on S-adenosyl-L-homocysteine agarose using substrate elution. The enzyme has a M(r) of 40,000 as determined by SDS-PAGE. Amino acid sequences of three peptides produced from a proteolytic digest of bispecific OMT were obtained by automated Edman degradation. Polyclonal antibodies raised against the purified OMT reacted strongly to OMT in both purified and unpurified fractions in western blots. Addition of an equal concentration of anti-OMT IgG to crude extract protein inhibited OMT activity by more than 70%.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1368360</PMID><DateCompleted><Year>1992</Year><Month>09</Month><Day>02</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>27</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0031-9422</ISSN><JournalIssue CitedMedium="Print"><Volume>31</Volume><Issue>5</Issue><PubDate><Year>1992</Year><Month>May</Month></PubDate></JournalIssue><Title>Phytochemistry</Title><ISOAbbreviation>Phytochemistry</ISOAbbreviation></Journal><ArticleTitle>Characterization of bispecific caffeic acid/5-hydroxyferulic acid O-methyltransferase from aspen.</ArticleTitle><Pagination><MedlinePgn>1495-8</MedlinePgn></Pagination><Abstract><AbstractText>Bispecific O-methyltransferase (OMT, EC 2.1.1.68) which catalyses the meta-specific methylation of caffeic acid and 5-hydroxyferulic acid was purified to homogeneity from the developing secondary xylem of aspen (Populus tremuloides). The enzyme was purified by conventional techniques and affinity chromatography on S-adenosyl-L-homocysteine agarose using substrate elution. The enzyme has a M(r) of 40,000 as determined by SDS-PAGE. Amino acid sequences of three peptides produced from a proteolytic digest of bispecific OMT were obtained by automated Edman degradation. Polyclonal antibodies raised against the purified OMT reacted strongly to OMT in both purified and unpurified fractions in western blots. Addition of an equal concentration of anti-OMT IgG to crude extract protein inhibited OMT activity by more than 70%.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bugos</LastName><ForeName>R C</ForeName><Initials>RC</Initials><AffiliationInfo><Affiliation>Phytotechnology Research Center, School of Forestry and Wood Products, Michigan Technological University, Houghton 49931.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chiang</LastName><ForeName>V L</ForeName><Initials>VL</Initials></Author><Author ValidYN="Y"><LastName>Campbell</LastName><ForeName>W H</ForeName><Initials>WH</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Phytochemistry</MedlineTA><NlmUniqueID>0151434</NlmUniqueID><ISSNLinking>0031-9422</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002109">Caffeic Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003373">Coumaric Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>1782-55-4</RegistryNumber><NameOfSubstance UI="C071744">5-hydroxyferulic acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber><NameOfSubstance UI="D008780">Methyltransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.68</RegistryNumber><NameOfSubstance UI="C019608">caffeate O-methyltransferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>U2S3A33KVM</RegistryNumber><NameOfSubstance UI="C040048">caffeic acid</NameOfSubstance></Chemical></ChemicalList><CitationSubset>B</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015153" MajorTopicYN="N">Blotting, Western</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002109" MajorTopicYN="N">Caffeic Acids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003373" MajorTopicYN="N">Coumaric Acids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008780" MajorTopicYN="N">Methyltransferases</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010944" MajorTopicYN="N">Plants</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1992</Year><Month>5</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1992</Year><Month>5</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1992</Year><Month>5</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1368360</ArticleId><ArticleId IdType="pii">0031-9422(92)83093-E</ArticleId><ArticleId IdType="doi">10.1016/0031-9422(92)83093-e</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Bugos, R C" sort="Bugos, R C" uniqKey="Bugos R" first="R C" last="Bugos">R C Bugos</name><name sortKey="Campbell, W H" sort="Campbell, W H" uniqKey="Campbell W" first="W H" last="Campbell">W H Campbell</name><name sortKey="Chiang, V L" sort="Chiang, V L" uniqKey="Chiang V" first="V L" last="Chiang">V L Chiang</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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