A standard reaction condition and a single HPLC separation system are sufficient for estimation of monolignol biosynthetic pathway enzyme activities.
Identifieur interne : 002C20 ( Main/Exploration ); précédent : 002C19; suivant : 002C21A standard reaction condition and a single HPLC separation system are sufficient for estimation of monolignol biosynthetic pathway enzyme activities.
Auteurs : Jie Liu [États-Unis] ; Rui Shi ; Quanzi Li ; Ronald R. Sederoff ; Vincent L. ChiangSource :
- Planta [ 1432-2048 ] ; 2012.
Descripteurs français
- KwdFr :
- Chromatographie en phase liquide à haute performance (MeSH), Dosages enzymatiques (MeSH), Lignine (biosynthèse), Methyltransferases (métabolisme), Mixed function oxygenases (métabolisme), Oxidoreductases (métabolisme), Pinus taeda (enzymologie), Populus (enzymologie), Protéines végétales (analyse), Spécificité du substrat (MeSH), Tiges de plante (enzymologie), Voies de biosynthèse (MeSH), Xylème (enzymologie).
- MESH :
- analyse : Protéines végétales.
- biosynthèse : Lignine.
- enzymologie : Pinus taeda, Populus, Tiges de plante, Xylème.
- métabolisme : Methyltransferases, Mixed function oxygenases, Oxidoreductases.
- Chromatographie en phase liquide à haute performance, Dosages enzymatiques, Spécificité du substrat, Voies de biosynthèse.
English descriptors
- KwdEn :
- Biosynthetic Pathways (MeSH), Chromatography, High Pressure Liquid (MeSH), Enzyme Assays (MeSH), Lignin (biosynthesis), Methyltransferases (metabolism), Mixed Function Oxygenases (metabolism), Oxidoreductases (metabolism), Pinus taeda (enzymology), Plant Proteins (analysis), Plant Stems (enzymology), Populus (enzymology), Substrate Specificity (MeSH), Xylem (enzymology).
- MESH :
- chemical , analysis : Plant Proteins.
- chemical , biosynthesis : Lignin.
- chemical , metabolism : Methyltransferases, Mixed Function Oxygenases, Oxidoreductases.
- enzymology : Pinus taeda, Plant Stems, Populus, Xylem.
- Biosynthetic Pathways, Chromatography, High Pressure Liquid, Enzyme Assays, Substrate Specificity.
Abstract
Lignin content and composition are largely determined by the composition and quantity of the monolignol precursors. Individual enzymes of the monolignol biosynthetic pathway determine the composition and quantity of monolignols. Monolignol biosynthesis in angiosperms is mediated by ten enzyme families. We developed a method using a total protein extract (soluble and microsomal) for the comprehensive and simultaneous analysis of these ten enzyme activities in a single target tissue, stem differentiating xylem (SDX) of Populus trichocarpa. As little as 300 mg fresh weight of SDX is sufficient for triplicate assays of all ten enzyme activities. To expand the effectiveness of the analysis, we quantified the reaction products directly by HPLC and developed a universal method that can separate the substrates and products of all enzymes. The specific activities measured with this simple approach are similar to those obtained with the optimum conditions previously established for each individual enzyme. This approach is applicable to the enzyme activity analysis for both P. trichocarpa (angiosperm) and Pinus taeda (gymnosperm) and is particularly useful when a large number of samples need to be analyzed for all monolignol biosynthetic enzymes.
DOI: 10.1007/s00425-012-1688-9
PubMed: 22729823
Affiliations:
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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="2012">2012</date><idno type="RBID">pubmed:22729823</idno><idno type="pmid">22729823</idno><idno type="doi">10.1007/s00425-012-1688-9</idno><idno type="wicri:Area/Main/Corpus">002984</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002984</idno><idno type="wicri:Area/Main/Curation">002984</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">002984</idno><idno type="wicri:Area/Main/Exploration">002984</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">A standard reaction condition and a single HPLC separation system are sufficient for estimation of monolignol biosynthetic pathway enzyme activities.</title><author><name sortKey="Liu, Jie" sort="Liu, Jie" uniqKey="Liu J" first="Jie" last="Liu">Jie Liu</name><affiliation wicri:level="2"><nlm:affiliation>Forest Biotechnology Group, Department of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC 27695, USA. jliu13@ncsu.edu</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Forest Biotechnology Group, Department of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC 27695</wicri:regionArea><placeName><region type="state">Caroline du Nord</region></placeName></affiliation></author><author><name sortKey="Shi, Rui" sort="Shi, Rui" uniqKey="Shi R" first="Rui" last="Shi">Rui Shi</name></author><author><name sortKey="Li, Quanzi" sort="Li, Quanzi" uniqKey="Li Q" first="Quanzi" last="Li">Quanzi Li</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">Planta</title><idno type="eISSN">1432-2048</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biosynthetic Pathways (MeSH)</term><term>Chromatography, High Pressure Liquid (MeSH)</term><term>Enzyme Assays (MeSH)</term><term>Lignin (biosynthesis)</term><term>Methyltransferases (metabolism)</term><term>Mixed Function Oxygenases (metabolism)</term><term>Oxidoreductases (metabolism)</term><term>Pinus taeda (enzymology)</term><term>Plant Proteins (analysis)</term><term>Plant Stems (enzymology)</term><term>Populus (enzymology)</term><term>Substrate Specificity (MeSH)</term><term>Xylem (enzymology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Chromatographie en phase liquide à haute performance (MeSH)</term><term>Dosages enzymatiques (MeSH)</term><term>Lignine (biosynthèse)</term><term>Methyltransferases (métabolisme)</term><term>Mixed function oxygenases (métabolisme)</term><term>Oxidoreductases (métabolisme)</term><term>Pinus taeda (enzymologie)</term><term>Populus (enzymologie)</term><term>Protéines végétales (analyse)</term><term>Spécificité du substrat (MeSH)</term><term>Tiges de plante (enzymologie)</term><term>Voies de biosynthèse (MeSH)</term><term>Xylème (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Lignin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Methyltransferases</term><term>Mixed Function Oxygenases</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Lignine</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Pinus taeda</term><term>Populus</term><term>Tiges de plante</term><term>Xylème</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Pinus taeda</term><term>Plant Stems</term><term>Populus</term><term>Xylem</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Methyltransferases</term><term>Mixed function oxygenases</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biosynthetic Pathways</term><term>Chromatography, High Pressure Liquid</term><term>Enzyme Assays</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie en phase liquide à haute performance</term><term>Dosages enzymatiques</term><term>Spécificité du substrat</term><term>Voies de biosynthèse</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lignin content and composition are largely determined by the composition and quantity of the monolignol precursors. Individual enzymes of the monolignol biosynthetic pathway determine the composition and quantity of monolignols. Monolignol biosynthesis in angiosperms is mediated by ten enzyme families. We developed a method using a total protein extract (soluble and microsomal) for the comprehensive and simultaneous analysis of these ten enzyme activities in a single target tissue, stem differentiating xylem (SDX) of Populus trichocarpa. As little as 300 mg fresh weight of SDX is sufficient for triplicate assays of all ten enzyme activities. To expand the effectiveness of the analysis, we quantified the reaction products directly by HPLC and developed a universal method that can separate the substrates and products of all enzymes. The specific activities measured with this simple approach are similar to those obtained with the optimum conditions previously established for each individual enzyme. This approach is applicable to the enzyme activity analysis for both P. trichocarpa (angiosperm) and Pinus taeda (gymnosperm) and is particularly useful when a large number of samples need to be analyzed for all monolignol biosynthetic enzymes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22729823</PMID><DateCompleted><Year>2013</Year><Month>03</Month><Day>26</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-2048</ISSN><JournalIssue CitedMedium="Internet"><Volume>236</Volume><Issue>3</Issue><PubDate><Year>2012</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Planta</Title><ISOAbbreviation>Planta</ISOAbbreviation></Journal><ArticleTitle>A standard reaction condition and a single HPLC separation system are sufficient for estimation of monolignol biosynthetic pathway enzyme activities.</ArticleTitle><Pagination><MedlinePgn>879-85</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00425-012-1688-9</ELocationID><Abstract><AbstractText>Lignin content and composition are largely determined by the composition and quantity of the monolignol precursors. Individual enzymes of the monolignol biosynthetic pathway determine the composition and quantity of monolignols. Monolignol biosynthesis in angiosperms is mediated by ten enzyme families. We developed a method using a total protein extract (soluble and microsomal) for the comprehensive and simultaneous analysis of these ten enzyme activities in a single target tissue, stem differentiating xylem (SDX) of Populus trichocarpa. As little as 300 mg fresh weight of SDX is sufficient for triplicate assays of all ten enzyme activities. To expand the effectiveness of the analysis, we quantified the reaction products directly by HPLC and developed a universal method that can separate the substrates and products of all enzymes. The specific activities measured with this simple approach are similar to those obtained with the optimum conditions previously established for each individual enzyme. This approach is applicable to the enzyme activity analysis for both P. trichocarpa (angiosperm) and Pinus taeda (gymnosperm) and is particularly useful when a large number of samples need to be analyzed for all monolignol biosynthetic enzymes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Jie</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Forest Biotechnology Group, Department of Forestry and Environmental Resources, North Carolina State University, Raleigh, NC 27695, USA. jliu13@ncsu.edu</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shi</LastName><ForeName>Rui</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Quanzi</ForeName><Initials>Q</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>2012</Year><Month>06</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Planta</MedlineTA><NlmUniqueID>1250576</NlmUniqueID><ISSNLinking>0032-0935</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D006899">Mixed Function Oxygenases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber><NameOfSubstance UI="D008780">Methyltransferases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D053898" MajorTopicYN="N">Biosynthetic Pathways</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057075" MajorTopicYN="N">Enzyme Assays</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008780" MajorTopicYN="N">Methyltransferases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006899" MajorTopicYN="N">Mixed Function Oxygenases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D041603" MajorTopicYN="N">Pinus taeda</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018547" MajorTopicYN="N">Plant Stems</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000201" 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Chiang</name><name sortKey="Li, Quanzi" sort="Li, Quanzi" uniqKey="Li Q" first="Quanzi" last="Li">Quanzi Li</name><name sortKey="Sederoff, Ronald R" sort="Sederoff, Ronald R" uniqKey="Sederoff R" first="Ronald R" last="Sederoff">Ronald R. Sederoff</name><name sortKey="Shi, Rui" sort="Shi, Rui" uniqKey="Shi R" first="Rui" last="Shi">Rui Shi</name></noCountry><country name="États-Unis"><region name="Caroline du Nord"><name sortKey="Liu, Jie" sort="Liu, Jie" uniqKey="Liu J" first="Jie" last="Liu">Jie Liu</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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