Regioselectivity of 7-O-methyltransferase of poplar to flavones.
Identifieur interne : 003E01 ( Main/Corpus ); précédent : 003E00; suivant : 003E02Regioselectivity of 7-O-methyltransferase of poplar to flavones.
Auteurs : Bong-Gyu Kim ; Hojung Kim ; Hor-Gil Hur ; Yoongho Lim ; Joong-Hoon AhnSource :
- Journal of biotechnology [ 0168-1656 ] ; 2006.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Flavones, Methyltransferases.
- enzymology : Populus.
- Substrate Specificity.
Abstract
POMT-7, an O-methyltransferase from poplar (Populus deltoids) was used to modify a variety of flavonoid compounds. POMT-7 was able to transfer a methyl group to several flavonoids containing a C-7 hydroxyl group. However, POMT-7 showed a higher affinity toward flavonol and flavone such as apigenin, kaempferol, luteolin, and quercetin than flavanone and isoflavone. Based on comparison of HPLC retention times with authentic compounds and corresponding nuclear magnetic resonance spectroscopy data, the methylation position of the reaction products was determined to be at the hydroxyl group of C-7. Biotransformation kinetics indicated that the enzyme converted more than 80% of the apigenin, kaempferol, luteolin and quercetin substrates, which were added at concentration of 70 microM, into corresponding 7-methoxy compounds within 24 h.
DOI: 10.1016/j.jbiotec.2006.04.019
PubMed: 16713650
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pubmed:16713650Le document en format XML
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POMT-7 was able to transfer a methyl group to several flavonoids containing a C-7 hydroxyl group. However, POMT-7 showed a higher affinity toward flavonol and flavone such as apigenin, kaempferol, luteolin, and quercetin than flavanone and isoflavone. Based on comparison of HPLC retention times with authentic compounds and corresponding nuclear magnetic resonance spectroscopy data, the methylation position of the reaction products was determined to be at the hydroxyl group of C-7. Biotransformation kinetics indicated that the enzyme converted more than 80% of the apigenin, kaempferol, luteolin and quercetin substrates, which were added at concentration of 70 microM, into corresponding 7-methoxy compounds within 24 h.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16713650</PMID><DateCompleted><Year>2006</Year><Month>12</Month><Day>13</Day></DateCompleted><DateRevised><Year>2006</Year><Month>10</Month><Day>18</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0168-1656</ISSN><JournalIssue CitedMedium="Print"><Volume>126</Volume><Issue>2</Issue><PubDate><Year>2006</Year><Month>Nov</Month><Day>01</Day></PubDate></JournalIssue><Title>Journal of biotechnology</Title><ISOAbbreviation>J Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Regioselectivity of 7-O-methyltransferase of poplar to flavones.</ArticleTitle><Pagination><MedlinePgn>241-7</MedlinePgn></Pagination><Abstract><AbstractText>POMT-7, an O-methyltransferase from poplar (Populus deltoids) was used to modify a variety of flavonoid compounds. POMT-7 was able to transfer a methyl group to several flavonoids containing a C-7 hydroxyl group. However, POMT-7 showed a higher affinity toward flavonol and flavone such as apigenin, kaempferol, luteolin, and quercetin than flavanone and isoflavone. Based on comparison of HPLC retention times with authentic compounds and corresponding nuclear magnetic resonance spectroscopy data, the methylation position of the reaction products was determined to be at the hydroxyl group of C-7. Biotransformation kinetics indicated that the enzyme converted more than 80% of the apigenin, kaempferol, luteolin and quercetin substrates, which were added at concentration of 70 microM, into corresponding 7-methoxy compounds within 24 h.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Bong-Gyu</ForeName><Initials>BG</Initials><AffiliationInfo><Affiliation>Department of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University, Seoul 143-701, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Hojung</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Hur</LastName><ForeName>Hor-Gil</ForeName><Initials>HG</Initials></Author><Author ValidYN="Y"><LastName>Lim</LastName><ForeName>Yoongho</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Ahn</LastName><ForeName>Joong-Hoon</ForeName><Initials>JH</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>05</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>J Biotechnol</MedlineTA><NlmUniqueID>8411927</NlmUniqueID><ISSNLinking>0168-1656</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D047309">Flavones</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber><NameOfSubstance UI="D008780">Methyltransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber><NameOfSubstance UI="C110900">isoflavone 7-O-methyltransferase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D047309" MajorTopicYN="N">Flavones</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008780" MajorTopicYN="N">Methyltransferases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year><Month>01</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2006</Year><Month>03</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2006</Year><Month>04</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>5</Month><Day>23</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>12</Month><Day>14</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>5</Month><Day>23</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16713650</ArticleId><ArticleId IdType="pii">S0168-1656(06)00333-6</ArticleId><ArticleId IdType="doi">10.1016/j.jbiotec.2006.04.019</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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