Molecular characterization of flavonol synthase from poplar and its application to the synthesis of 3-O-methylkaempferol.
Identifieur interne : 003190 ( Main/Exploration ); précédent : 003189; suivant : 003191Molecular characterization of flavonol synthase from poplar and its application to the synthesis of 3-O-methylkaempferol.
Auteurs : Bong-Gyu Kim [Corée du Sud] ; Eun Ji Joe ; Joong-Hoon AhnSource :
- Biotechnology letters [ 1573-6776 ] ; 2010.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Cinétique (MeSH), Données de séquences moléculaires (MeSH), Escherichia coli (génétique), Flavanones (métabolisme), Kaempférols (biosynthèse), Methyltransferases (génétique), Methyltransferases (métabolisme), Oxidoreductases (composition chimique), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Populus (enzymologie), Populus (génétique), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Protéines végétales (composition chimique), Protéines végétales (génétique), Protéines végétales (métabolisme), Spectrométrie de masse en tandem (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- biosynthèse : Kaempférols.
- composition chimique : Oxidoreductases, Protéines recombinantes, Protéines végétales.
- enzymologie : Populus.
- génétique : Escherichia coli, Methyltransferases, Oxidoreductases, Populus, Protéines recombinantes, Protéines végétales.
- métabolisme : Flavanones, Methyltransferases, Oxidoreductases, Protéines recombinantes, Protéines végétales.
- Alignement de séquences, Cinétique, Données de séquences moléculaires, Spectrométrie de masse en tandem, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Escherichia coli (genetics), Flavanones (metabolism), Kaempferols (biosynthesis), Kinetics (MeSH), Methyltransferases (genetics), Methyltransferases (metabolism), Molecular Sequence Data (MeSH), Oxidoreductases (chemistry), Oxidoreductases (genetics), Oxidoreductases (metabolism), Plant Proteins (chemistry), Plant Proteins (genetics), Plant Proteins (metabolism), Populus (enzymology), Populus (genetics), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Sequence Alignment (MeSH), Tandem Mass Spectrometry (MeSH).
- MESH :
- chemical , biosynthesis : Kaempferols.
- chemical , chemistry : Oxidoreductases, Plant Proteins, Recombinant Proteins.
- chemical , genetics : Methyltransferases, Oxidoreductases, Plant Proteins, Recombinant Proteins.
- chemical , metabolism : Flavanones, Methyltransferases, Oxidoreductases, Plant Proteins, Recombinant Proteins.
- enzymology : Populus.
- genetics : Escherichia coli, Populus.
- Amino Acid Sequence, Kinetics, Molecular Sequence Data, Sequence Alignment, Tandem Mass Spectrometry.
Abstract
Biosynthesis of flavonoid derivatives requires enzyme(s) having high reactivity as well as regioselectivity. We have synthesized 3-O-kaempferol from naringenin using two enzymes. The first reaction, in which naringenin is converted to kaempferol, is mediated by flavonol synthase (FLS). An FLS (PFLS) with strong catalytic activity was cloned and characterized from the genome sequence of the poplar (Populus deltoides). PFLS consists of a 1,008 bp ORF encoding a 38 kDa protein. PFLS was expressed in Escherichia coli with a glutathione-S-transferase (GST) tagging. The purified recombinant PFLS was characterized. Catalytically, it was more efficient than the previously characterized FLSs. A mixture of two E. coli transformants harboring either PFLS or ROMT9 (a kaempferol 3-O-methyltransferase) converted naringenin into 3-O-methylkaempferol.
DOI: 10.1007/s10529-009-0188-x
PubMed: 20033832
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Kaempferols</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Oxidoreductases</term><term>Plant Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Methyltransferases</term><term>Oxidoreductases</term><term>Plant Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Flavanones</term><term>Methyltransferases</term><term>Oxidoreductases</term><term>Plant Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Kaempférols</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Oxidoreductases</term><term>Protéines recombinantes</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" 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xml:lang="fr"><term>Alignement de séquences</term><term>Cinétique</term><term>Données de séquences moléculaires</term><term>Spectrométrie de masse en tandem</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Biosynthesis of flavonoid derivatives requires enzyme(s) having high reactivity as well as regioselectivity. We have synthesized 3-O-kaempferol from naringenin using two enzymes. The first reaction, in which naringenin is converted to kaempferol, is mediated by flavonol synthase (FLS). An FLS (PFLS) with strong catalytic activity was cloned and characterized from the genome sequence of the poplar (Populus deltoides). PFLS consists of a 1,008 bp ORF encoding a 38 kDa protein. PFLS was expressed in Escherichia coli with a glutathione-S-transferase (GST) tagging. The purified recombinant PFLS was characterized. Catalytically, it was more efficient than the previously characterized FLSs. A mixture of two E. coli transformants harboring either PFLS or ROMT9 (a kaempferol 3-O-methyltransferase) converted naringenin into 3-O-methylkaempferol.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20033832</PMID><DateCompleted><Year>2010</Year><Month>06</Month><Day>24</Day></DateCompleted><DateRevised><Year>2012</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1573-6776</ISSN><JournalIssue CitedMedium="Internet"><Volume>32</Volume><Issue>4</Issue><PubDate><Year>2010</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Biotechnology letters</Title><ISOAbbreviation>Biotechnol Lett</ISOAbbreviation></Journal><ArticleTitle>Molecular characterization of flavonol synthase from poplar and its application to the synthesis of 3-O-methylkaempferol.</ArticleTitle><Pagination><MedlinePgn>579-84</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s10529-009-0188-x</ELocationID><Abstract><AbstractText>Biosynthesis of flavonoid derivatives requires enzyme(s) having high reactivity as well as regioselectivity. We have synthesized 3-O-kaempferol from naringenin using two enzymes. The first reaction, in which naringenin is converted to kaempferol, is mediated by flavonol synthase (FLS). An FLS (PFLS) with strong catalytic activity was cloned and characterized from the genome sequence of the poplar (Populus deltoides). PFLS consists of a 1,008 bp ORF encoding a 38 kDa protein. PFLS was expressed in Escherichia coli with a glutathione-S-transferase (GST) tagging. The purified recombinant PFLS was characterized. Catalytically, it was more efficient than the previously characterized FLSs. A mixture of two E. coli transformants harboring either PFLS or ROMT9 (a kaempferol 3-O-methyltransferase) converted naringenin into 3-O-methylkaempferol.</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 143-901, Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Joe</LastName><ForeName>Eun Ji</ForeName><Initials>EJ</Initials></Author><Author ValidYN="Y"><LastName>Ahn</LastName><ForeName>Joong-Hoon</ForeName><Initials>JH</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>2009</Year><Month>12</Month><Day>24</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="C464826">3-methylkaempferol</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D044950">Flavanones</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D044949">Kaempferols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance 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MajorTopicYN="N">Kaempferols</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008780" MajorTopicYN="N">Methyltransferases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">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="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053719" MajorTopicYN="N">Tandem Mass Spectrometry</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2009</Year><Month>11</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2009</Year><Month>12</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2009</Year><Month>12</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>12</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>12</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>6</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20033832</ArticleId><ArticleId IdType="doi">10.1007/s10529-009-0188-x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Corée du Sud</li></country><region><li>Région capitale de Séoul</li></region><settlement><li>Séoul</li></settlement></list><tree><noCountry><name sortKey="Ahn, Joong Hoon" sort="Ahn, Joong Hoon" uniqKey="Ahn J" first="Joong-Hoon" last="Ahn">Joong-Hoon Ahn</name><name sortKey="Joe, Eun Ji" sort="Joe, Eun Ji" uniqKey="Joe E" first="Eun Ji" last="Joe">Eun Ji Joe</name></noCountry><country name="Corée du Sud"><region name="Région capitale de Séoul"><name sortKey="Kim, Bong Gyu" sort="Kim, Bong Gyu" uniqKey="Kim B" first="Bong-Gyu" last="Kim">Bong-Gyu Kim</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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