Monolignol pathway 4-coumaric acid:coenzyme A ligases in Populus trichocarpa: novel specificity, metabolic regulation, and simulation of coenzyme A ligation fluxes.
Identifieur interne : 002721 ( Main/Corpus ); précédent : 002720; suivant : 002722Monolignol pathway 4-coumaric acid:coenzyme A ligases in Populus trichocarpa: novel specificity, metabolic regulation, and simulation of coenzyme A ligation fluxes.
Auteurs : Hsi-Chuan Chen ; Jina Song ; Cranos M. Williams ; Christopher M. Shuford ; Jie Liu ; Jack P. Wang ; Quanzi Li ; Rui Shi ; Emine Gokce ; Joel Ducoste ; David C. Muddiman ; Ronald R. Sederoff ; Vincent L. ChiangSource :
- Plant physiology [ 1532-2548 ] ; 2013.
English descriptors
- KwdEn :
- Allosteric Regulation (drug effects), Binding Sites (MeSH), Biosynthetic Pathways (drug effects), Blotting, Western (MeSH), Caffeic Acids (pharmacology), Coenzyme A (metabolism), Coenzyme A Ligases (antagonists & inhibitors), Coenzyme A Ligases (metabolism), Computer Simulation (MeSH), Coumaric Acids (chemistry), Coumaric Acids (metabolism), Coumaric Acids (pharmacology), Kinetics (MeSH), Lignin (biosynthesis), Lignin (chemistry), Phenylpropionates (metabolism), Phosphoproteins (metabolism), Phosphorylation (drug effects), Plant Extracts (MeSH), Populus (drug effects), Populus (enzymology), Propionates (MeSH), Proteomics (MeSH), Recombinant Fusion Proteins (metabolism), Sequence Homology, Amino Acid (MeSH), Substrate Specificity (drug effects), Xylem (drug effects), Xylem (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Coenzyme A Ligases.
- chemical , biosynthesis : Lignin.
- chemical , chemistry : Coumaric Acids, Lignin.
- chemical , metabolism : Coenzyme A, Coenzyme A Ligases, Coumaric Acids, Phenylpropionates, Phosphoproteins, Recombinant Fusion Proteins.
- chemical , pharmacology : Caffeic Acids, Coumaric Acids.
- drug effects : Allosteric Regulation, Biosynthetic Pathways, Phosphorylation, Populus, Substrate Specificity, Xylem.
- enzymology : Populus.
- metabolism : Xylem.
- Binding Sites, Blotting, Western, Computer Simulation, Kinetics, Plant Extracts, Propionates, Proteomics, Sequence Homology, Amino Acid.
Abstract
4-Coumaric acid:coenzyme A ligase (4CL) is involved in monolignol biosynthesis for lignification in plant cell walls. It ligates coenzyme A (CoA) with hydroxycinnamic acids, such as 4-coumaric and caffeic acids, into hydroxycinnamoyl-CoA thioesters. The ligation ensures the activated state of the acid for reduction into monolignols. In Populus spp., it has long been thought that one monolignol-specific 4CL is involved. Here, we present evidence of two monolignol 4CLs, Ptr4CL3 and Ptr4CL5, in Populus trichocarpa. Ptr4CL3 is the ortholog of the monolignol 4CL reported for many other species. Ptr4CL5 is novel. The two Ptr4CLs exhibited distinct Michaelis-Menten kinetic properties. Inhibition kinetics demonstrated that hydroxycinnamic acid substrates are also inhibitors of 4CL and suggested that Ptr4CL5 is an allosteric enzyme. Experimentally validated flux simulation, incorporating reaction/inhibition kinetics, suggested two CoA ligation paths in vivo: one through 4-coumaric acid and the other through caffeic acid. We previously showed that a membrane protein complex mediated the 3-hydroxylation of 4-coumaric acid to caffeic acid. The demonstration here of two ligation paths requiring these acids supports this 3-hydroxylation function. Ptr4CL3 regulates both CoA ligation paths with similar efficiencies, whereas Ptr4CL5 regulates primarily the caffeic acid path. Both paths can be inhibited by caffeic acid. The Ptr4CL5-catalyzed caffeic acid metabolism, therefore, may also act to mitigate the inhibition by caffeic acid to maintain a proper ligation flux. A high level of caffeic acid was detected in stem-differentiating xylem of P. trichocarpa. Our results suggest that Ptr4CL5 and caffeic acid coordinately modulate the CoA ligation flux for monolignol biosynthesis.
DOI: 10.1104/pp.112.210971
PubMed: 23344904
PubMed Central: PMC3585612
Links to Exploration step
pubmed:23344904Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Monolignol pathway 4-coumaric acid:coenzyme A ligases in Populus trichocarpa: novel specificity, metabolic regulation, and simulation of coenzyme A ligation fluxes.</title>
<author><name sortKey="Chen, Hsi Chuan" sort="Chen, Hsi Chuan" uniqKey="Chen H" first="Hsi-Chuan" last="Chen">Hsi-Chuan Chen</name>
<affiliation><nlm:affiliation>Forest Biotechnology Group, Department of Forestry and Environmental Resources , North Carolina State University, Raleigh, NC 27606, USA.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Song, Jina" sort="Song, Jina" uniqKey="Song J" first="Jina" last="Song">Jina Song</name>
</author>
<author><name sortKey="Williams, Cranos M" sort="Williams, Cranos M" uniqKey="Williams C" first="Cranos M" last="Williams">Cranos M. Williams</name>
</author>
<author><name sortKey="Shuford, Christopher M" sort="Shuford, Christopher M" uniqKey="Shuford C" first="Christopher M" last="Shuford">Christopher M. Shuford</name>
</author>
<author><name sortKey="Liu, Jie" sort="Liu, Jie" uniqKey="Liu J" first="Jie" last="Liu">Jie Liu</name>
</author>
<author><name sortKey="Wang, Jack P" sort="Wang, Jack P" uniqKey="Wang J" first="Jack P" last="Wang">Jack P. Wang</name>
</author>
<author><name sortKey="Li, Quanzi" sort="Li, Quanzi" uniqKey="Li Q" first="Quanzi" last="Li">Quanzi Li</name>
</author>
<author><name sortKey="Shi, Rui" sort="Shi, Rui" uniqKey="Shi R" first="Rui" last="Shi">Rui Shi</name>
</author>
<author><name sortKey="Gokce, Emine" sort="Gokce, Emine" uniqKey="Gokce E" first="Emine" last="Gokce">Emine Gokce</name>
</author>
<author><name sortKey="Ducoste, Joel" sort="Ducoste, Joel" uniqKey="Ducoste J" first="Joel" last="Ducoste">Joel Ducoste</name>
</author>
<author><name sortKey="Muddiman, David C" sort="Muddiman, David C" uniqKey="Muddiman D" first="David C" last="Muddiman">David C. Muddiman</name>
</author>
<author><name sortKey="Sederoff, Ronald R" sort="Sederoff, Ronald R" uniqKey="Sederoff R" first="Ronald R" last="Sederoff">Ronald R. Sederoff</name>
</author>
<author><name sortKey="Chiang, Vincent L" sort="Chiang, Vincent L" uniqKey="Chiang V" first="Vincent L" last="Chiang">Vincent L. Chiang</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2013">2013</date>
<idno type="RBID">pubmed:23344904</idno>
<idno type="pmid">23344904</idno>
<idno type="doi">10.1104/pp.112.210971</idno>
<idno type="pmc">PMC3585612</idno>
<idno type="wicri:Area/Main/Corpus">002721</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002721</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Monolignol pathway 4-coumaric acid:coenzyme A ligases in Populus trichocarpa: novel specificity, metabolic regulation, and simulation of coenzyme A ligation fluxes.</title>
<author><name sortKey="Chen, Hsi Chuan" sort="Chen, Hsi Chuan" uniqKey="Chen H" first="Hsi-Chuan" last="Chen">Hsi-Chuan Chen</name>
<affiliation><nlm:affiliation>Forest Biotechnology Group, Department of Forestry and Environmental Resources , North Carolina State University, Raleigh, NC 27606, USA.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Song, Jina" sort="Song, Jina" uniqKey="Song J" first="Jina" last="Song">Jina Song</name>
</author>
<author><name sortKey="Williams, Cranos M" sort="Williams, Cranos M" uniqKey="Williams C" first="Cranos M" last="Williams">Cranos M. Williams</name>
</author>
<author><name sortKey="Shuford, Christopher M" sort="Shuford, Christopher M" uniqKey="Shuford C" first="Christopher M" last="Shuford">Christopher M. Shuford</name>
</author>
<author><name sortKey="Liu, Jie" sort="Liu, Jie" uniqKey="Liu J" first="Jie" last="Liu">Jie Liu</name>
</author>
<author><name sortKey="Wang, Jack P" sort="Wang, Jack P" uniqKey="Wang J" first="Jack P" last="Wang">Jack P. Wang</name>
</author>
<author><name sortKey="Li, Quanzi" sort="Li, Quanzi" uniqKey="Li Q" first="Quanzi" last="Li">Quanzi Li</name>
</author>
<author><name sortKey="Shi, Rui" sort="Shi, Rui" uniqKey="Shi R" first="Rui" last="Shi">Rui Shi</name>
</author>
<author><name sortKey="Gokce, Emine" sort="Gokce, Emine" uniqKey="Gokce E" first="Emine" last="Gokce">Emine Gokce</name>
</author>
<author><name sortKey="Ducoste, Joel" sort="Ducoste, Joel" uniqKey="Ducoste J" first="Joel" last="Ducoste">Joel Ducoste</name>
</author>
<author><name sortKey="Muddiman, David C" sort="Muddiman, David C" uniqKey="Muddiman D" first="David C" last="Muddiman">David C. Muddiman</name>
</author>
<author><name sortKey="Sederoff, Ronald R" sort="Sederoff, Ronald R" uniqKey="Sederoff R" first="Ronald R" last="Sederoff">Ronald R. Sederoff</name>
</author>
<author><name sortKey="Chiang, Vincent L" sort="Chiang, Vincent L" uniqKey="Chiang V" first="Vincent L" last="Chiang">Vincent L. Chiang</name>
</author>
</analytic>
<series><title level="j">Plant physiology</title>
<idno type="eISSN">1532-2548</idno>
<imprint><date when="2013" type="published">2013</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Allosteric Regulation (drug effects)</term>
<term>Binding Sites (MeSH)</term>
<term>Biosynthetic Pathways (drug effects)</term>
<term>Blotting, Western (MeSH)</term>
<term>Caffeic Acids (pharmacology)</term>
<term>Coenzyme A (metabolism)</term>
<term>Coenzyme A Ligases (antagonists & inhibitors)</term>
<term>Coenzyme A Ligases (metabolism)</term>
<term>Computer Simulation (MeSH)</term>
<term>Coumaric Acids (chemistry)</term>
<term>Coumaric Acids (metabolism)</term>
<term>Coumaric Acids (pharmacology)</term>
<term>Kinetics (MeSH)</term>
<term>Lignin (biosynthesis)</term>
<term>Lignin (chemistry)</term>
<term>Phenylpropionates (metabolism)</term>
<term>Phosphoproteins (metabolism)</term>
<term>Phosphorylation (drug effects)</term>
<term>Plant Extracts (MeSH)</term>
<term>Populus (drug effects)</term>
<term>Populus (enzymology)</term>
<term>Propionates (MeSH)</term>
<term>Proteomics (MeSH)</term>
<term>Recombinant Fusion Proteins (metabolism)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>Substrate Specificity (drug effects)</term>
<term>Xylem (drug effects)</term>
<term>Xylem (metabolism)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Coenzyme A Ligases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Lignin</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Coumaric Acids</term>
<term>Lignin</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Coenzyme A</term>
<term>Coenzyme A Ligases</term>
<term>Coumaric Acids</term>
<term>Phenylpropionates</term>
<term>Phosphoproteins</term>
<term>Recombinant Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Caffeic Acids</term>
<term>Coumaric Acids</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Allosteric Regulation</term>
<term>Biosynthetic Pathways</term>
<term>Phosphorylation</term>
<term>Populus</term>
<term>Substrate Specificity</term>
<term>Xylem</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Xylem</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term>
<term>Blotting, Western</term>
<term>Computer Simulation</term>
<term>Kinetics</term>
<term>Plant Extracts</term>
<term>Propionates</term>
<term>Proteomics</term>
<term>Sequence Homology, Amino Acid</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">4-Coumaric acid:coenzyme A ligase (4CL) is involved in monolignol biosynthesis for lignification in plant cell walls. It ligates coenzyme A (CoA) with hydroxycinnamic acids, such as 4-coumaric and caffeic acids, into hydroxycinnamoyl-CoA thioesters. The ligation ensures the activated state of the acid for reduction into monolignols. In Populus spp., it has long been thought that one monolignol-specific 4CL is involved. Here, we present evidence of two monolignol 4CLs, Ptr4CL3 and Ptr4CL5, in Populus trichocarpa. Ptr4CL3 is the ortholog of the monolignol 4CL reported for many other species. Ptr4CL5 is novel. The two Ptr4CLs exhibited distinct Michaelis-Menten kinetic properties. Inhibition kinetics demonstrated that hydroxycinnamic acid substrates are also inhibitors of 4CL and suggested that Ptr4CL5 is an allosteric enzyme. Experimentally validated flux simulation, incorporating reaction/inhibition kinetics, suggested two CoA ligation paths in vivo: one through 4-coumaric acid and the other through caffeic acid. We previously showed that a membrane protein complex mediated the 3-hydroxylation of 4-coumaric acid to caffeic acid. The demonstration here of two ligation paths requiring these acids supports this 3-hydroxylation function. Ptr4CL3 regulates both CoA ligation paths with similar efficiencies, whereas Ptr4CL5 regulates primarily the caffeic acid path. Both paths can be inhibited by caffeic acid. The Ptr4CL5-catalyzed caffeic acid metabolism, therefore, may also act to mitigate the inhibition by caffeic acid to maintain a proper ligation flux. A high level of caffeic acid was detected in stem-differentiating xylem of P. trichocarpa. Our results suggest that Ptr4CL5 and caffeic acid coordinately modulate the CoA ligation flux for monolignol biosynthesis.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23344904</PMID>
<DateCompleted><Year>2013</Year>
<Month>08</Month>
<Day>15</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1532-2548</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>161</Volume>
<Issue>3</Issue>
<PubDate><Year>2013</Year>
<Month>Mar</Month>
</PubDate>
</JournalIssue>
<Title>Plant physiology</Title>
<ISOAbbreviation>Plant Physiol</ISOAbbreviation>
</Journal>
<ArticleTitle>Monolignol pathway 4-coumaric acid:coenzyme A ligases in Populus trichocarpa: novel specificity, metabolic regulation, and simulation of coenzyme A ligation fluxes.</ArticleTitle>
<Pagination><MedlinePgn>1501-16</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1104/pp.112.210971</ELocationID>
<Abstract><AbstractText>4-Coumaric acid:coenzyme A ligase (4CL) is involved in monolignol biosynthesis for lignification in plant cell walls. It ligates coenzyme A (CoA) with hydroxycinnamic acids, such as 4-coumaric and caffeic acids, into hydroxycinnamoyl-CoA thioesters. The ligation ensures the activated state of the acid for reduction into monolignols. In Populus spp., it has long been thought that one monolignol-specific 4CL is involved. Here, we present evidence of two monolignol 4CLs, Ptr4CL3 and Ptr4CL5, in Populus trichocarpa. Ptr4CL3 is the ortholog of the monolignol 4CL reported for many other species. Ptr4CL5 is novel. The two Ptr4CLs exhibited distinct Michaelis-Menten kinetic properties. Inhibition kinetics demonstrated that hydroxycinnamic acid substrates are also inhibitors of 4CL and suggested that Ptr4CL5 is an allosteric enzyme. Experimentally validated flux simulation, incorporating reaction/inhibition kinetics, suggested two CoA ligation paths in vivo: one through 4-coumaric acid and the other through caffeic acid. We previously showed that a membrane protein complex mediated the 3-hydroxylation of 4-coumaric acid to caffeic acid. The demonstration here of two ligation paths requiring these acids supports this 3-hydroxylation function. Ptr4CL3 regulates both CoA ligation paths with similar efficiencies, whereas Ptr4CL5 regulates primarily the caffeic acid path. Both paths can be inhibited by caffeic acid. The Ptr4CL5-catalyzed caffeic acid metabolism, therefore, may also act to mitigate the inhibition by caffeic acid to maintain a proper ligation flux. A high level of caffeic acid was detected in stem-differentiating xylem of P. trichocarpa. Our results suggest that Ptr4CL5 and caffeic acid coordinately modulate the CoA ligation flux for monolignol biosynthesis.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Hsi-Chuan</ForeName>
<Initials>HC</Initials>
<AffiliationInfo><Affiliation>Forest Biotechnology Group, Department of Forestry and Environmental Resources , North Carolina State University, Raleigh, NC 27606, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Song</LastName>
<ForeName>Jina</ForeName>
<Initials>J</Initials>
</Author>
<Author ValidYN="Y"><LastName>Williams</LastName>
<ForeName>Cranos M</ForeName>
<Initials>CM</Initials>
</Author>
<Author ValidYN="Y"><LastName>Shuford</LastName>
<ForeName>Christopher M</ForeName>
<Initials>CM</Initials>
</Author>
<Author ValidYN="Y"><LastName>Liu</LastName>
<ForeName>Jie</ForeName>
<Initials>J</Initials>
</Author>
<Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Jack P</ForeName>
<Initials>JP</Initials>
</Author>
<Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Quanzi</ForeName>
<Initials>Q</Initials>
</Author>
<Author ValidYN="Y"><LastName>Shi</LastName>
<ForeName>Rui</ForeName>
<Initials>R</Initials>
</Author>
<Author ValidYN="Y"><LastName>Gokce</LastName>
<ForeName>Emine</ForeName>
<Initials>E</Initials>
</Author>
<Author ValidYN="Y"><LastName>Ducoste</LastName>
<ForeName>Joel</ForeName>
<Initials>J</Initials>
</Author>
<Author ValidYN="Y"><LastName>Muddiman</LastName>
<ForeName>David C</ForeName>
<Initials>DC</Initials>
</Author>
<Author ValidYN="Y"><LastName>Sederoff</LastName>
<ForeName>Ronald R</ForeName>
<Initials>RR</Initials>
</Author>
<Author ValidYN="Y"><LastName>Chiang</LastName>
<ForeName>Vincent L</ForeName>
<Initials>VL</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>
<ArticleDate DateType="Electronic"><Year>2013</Year>
<Month>01</Month>
<Day>23</Day>
</ArticleDate>
</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="D002109">Caffeic Acids</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D003373">Coumaric Acids</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010666">Phenylpropionates</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010750">Phosphoproteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010936">Plant Extracts</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011422">Propionates</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>5Q445IN5CU</RegistryNumber>
<NameOfSubstance UI="C035253">3-phenylpropionic acid</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>9005-53-2</RegistryNumber>
<NameOfSubstance UI="D008031">Lignin</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>AVM951ZWST</RegistryNumber>
<NameOfSubstance UI="C004999">ferulic acid</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 6.2.1.-</RegistryNumber>
<NameOfSubstance UI="D003066">Coenzyme A Ligases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>IBS9D1EU3J</RegistryNumber>
<NameOfSubstance UI="C495469">trans-3-(4'-hydroxyphenyl)-2-propenoic acid</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>SAA04E81UX</RegistryNumber>
<NameOfSubstance UI="D003065">Coenzyme A</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>U2S3A33KVM</RegistryNumber>
<NameOfSubstance UI="C040048">caffeic acid</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000494" MajorTopicYN="N">Allosteric Regulation</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D053898" MajorTopicYN="Y">Biosynthetic Pathways</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015153" MajorTopicYN="N">Blotting, Western</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002109" MajorTopicYN="N">Caffeic Acids</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003065" MajorTopicYN="N">Coenzyme A</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003066" MajorTopicYN="N">Coenzyme A Ligases</DescriptorName>
<QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003198" MajorTopicYN="Y">Computer Simulation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003373" MajorTopicYN="N">Coumaric Acids</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName>
<QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010666" MajorTopicYN="N">Phenylpropionates</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010750" MajorTopicYN="N">Phosphoproteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010936" MajorTopicYN="N">Plant Extracts</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011422" MajorTopicYN="N">Propionates</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D040901" MajorTopicYN="N">Proteomics</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName>
<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>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D052584" MajorTopicYN="N">Xylem</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2013</Year>
<Month>1</Month>
<Day>25</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2013</Year>
<Month>1</Month>
<Day>25</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2013</Year>
<Month>8</Month>
<Day>16</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">23344904</ArticleId>
<ArticleId IdType="pii">pp.112.210971</ArticleId>
<ArticleId IdType="doi">10.1104/pp.112.210971</ArticleId>
<ArticleId IdType="pmc">PMC3585612</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>J Biol Chem. 1977 Sep 25;252(18):6438-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">893418</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant J. 2012 Jun;70(5):818-30</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22313236</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Physiol. 2000 Jan;122(1):107-16</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10631254</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Cell Physiol. 2010 Jan;51(1):144-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19996151</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Planta. 2012 Sep;236(3):795-808</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22628084</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Planta. 2009 Aug;230(3):589-97</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19526248</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Phytochemistry. 2008 Oct;69(13):2449-56</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18722632</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8955-60</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10430877</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Cell. 1997 Nov;9(11):1985-98</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9401123</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant J. 1999 Jul;19(1):9-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10417722</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Proteomics. 2012 Sep;11(9):814-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22595788</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Physiol. 2011 Oct;157(2):574-86</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21807887</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2003 Jul 8;100(14):8601-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12819348</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2002 Nov 14;420(6912):206-10</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12432404</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Can J Biochem Physiol. 1963 Mar;41:613-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">13954437</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1961 Aug 4;134(3475):305-13</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17819301</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>PLoS Comput Biol. 2011 May;7(5):e1002047</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21625579</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1998 Apr 28;95(9):5407-12</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9560289</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Physiol. 2010 Apr;152(4):1763-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20118273</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Biotechnol. 2002 Jun;20(6):557-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12042854</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Can J Biochem Physiol. 1963 Mar;41:621-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">13954436</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2011 Dec 27;108(52):21253-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22160716</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Am J Physiol Renal Physiol. 2005 Aug;289(2):F247-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16006590</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Proteome Res. 2012 Jun 1;11(6):3390-404</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22524869</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Planta. 1986 Mar;169(1):97-107</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24232434</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Cell. 2007 Nov;19(11):3327-38</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18055607</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1976 Feb 20;191(4228):773-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17754175</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Proteome Res. 2011 Sep 2;10(9):4041-53</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21736374</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Biotechnol. 2007 Jul;25(7):759-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17572667</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1955 Apr 16;175(4459):688-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14370198</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Eur J Biochem. 1975 Mar 17;52(2):311-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">240682</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2000 Mar 3;275(9):6537-45</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10692459</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Cell Physiol. 1996 Oct;37(7):957-65</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8979396</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Can J Biochem Physiol. 1956 Jul;34(4):769-78</Citation>
<ArticleIdList><ArticleId IdType="pubmed">13343038</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Physiol. 2002 Feb;128(2):428-38</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11842147</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>New Phytol. 2008;179(4):987-1003</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18627494</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Syst Biol. 2011 Apr 12;7:482</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21487401</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Cell. 2001 Jul;13(7):1567-86</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11449052</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Biotechnol. 1999 Aug;17(8):808-12</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10429249</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Physiol. 2003 Nov;133(3):1051-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14612585</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Physiol. 2010 Oct;154(2):874-86</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20729393</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>BMC Plant Biol. 2011;11:158</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22074553</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Proteome Res. 2012 Dec 7;11(12):5827-35</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23039028</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2003 Apr 15;100(8):4939-44</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12668766</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Cell. 2012 Sep;24(9):3506-29</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23012438</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Cell. 2010 Sep;22(9):3093-104</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20841425</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Planta. 2012 Sep;236(3):879-85</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22729823</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PoplarV1/Data/Main/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002721 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd -nk 002721 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Bois |area= PoplarV1 |flux= Main |étape= Corpus |type= RBID |clé= pubmed:23344904 |texte= Monolignol pathway 4-coumaric acid:coenzyme A ligases in Populus trichocarpa: novel specificity, metabolic regulation, and simulation of coenzyme A ligation fluxes. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Corpus/RBID.i -Sk "pubmed:23344904" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Corpus/biblio.hfd \ | NlmPubMed2Wicri -a PoplarV1
![]() | This area was generated with Dilib version V0.6.37. | ![]() |