Molecular characterization of quinate and shikimate metabolism in Populus trichocarpa.
Identifieur interne : 002132 ( Main/Exploration ); précédent : 002131; suivant : 002133Molecular characterization of quinate and shikimate metabolism in Populus trichocarpa.
Auteurs : Jia Guo [Canada] ; Yuriko Carrington [Canada] ; Annette Alber [Canada] ; Jürgen Ehlting [Canada]Source :
- The Journal of biological chemistry [ 1083-351X ] ; 2014.
Descripteurs français
- KwdFr :
- Acide quinique (métabolisme), Acide shikimique (métabolisme), Alcohol oxidoreductases (composition chimique), Alcohol oxidoreductases (métabolisme), Amorces ADN (MeSH), Analyse de profil d'expression de gènes (MeSH), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Gènes de plante (MeSH), Populus (génétique), Populus (métabolisme), Réaction de polymérisation en chaîne (MeSH), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- composition chimique : Alcohol oxidoreductases.
- génétique : Populus.
- métabolisme : Acide quinique, Acide shikimique, Alcohol oxidoreductases, Populus.
- Amorces ADN, Analyse de profil d'expression de gènes, Clonage moléculaire, Données de séquences moléculaires, Gènes de plante, Réaction de polymérisation en chaîne, Similitude de séquences d'acides aminés, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Alcohol Oxidoreductases (chemistry), Alcohol Oxidoreductases (metabolism), Amino Acid Sequence (MeSH), Base Sequence (MeSH), Cloning, Molecular (MeSH), DNA Primers (MeSH), Gene Expression Profiling (MeSH), Genes, Plant (MeSH), Molecular Sequence Data (MeSH), Polymerase Chain Reaction (MeSH), Populus (genetics), Populus (metabolism), Quinic Acid (metabolism), Sequence Homology, Amino Acid (MeSH), Shikimic Acid (metabolism).
- MESH :
- chemical , chemistry : Alcohol Oxidoreductases.
- chemical , metabolism : Alcohol Oxidoreductases, Quinic Acid, Shikimic Acid.
- genetics : Populus.
- metabolism : Populus.
- Amino Acid Sequence, Base Sequence, Cloning, Molecular, DNA Primers, Gene Expression Profiling, Genes, Plant, Molecular Sequence Data, Polymerase Chain Reaction, Sequence Homology, Amino Acid.
Abstract
The shikimate pathway leads to the biosynthesis of aromatic amino acids essential for protein biosynthesis and the production of a wide array of plant secondary metabolites. Among them, quinate is an astringent feeding deterrent that can be formed in a single step reaction from 3-dehydroquinate catalyzed by quinate dehydrogenase (QDH). 3-Dehydroquinate is also the substrate for shikimate biosynthesis through the sequential actions of dehydroquinate dehydratase (DQD) and shikimate dehydrogenase (SDH) contained in a single protein in plants. The reaction mechanism of QDH resembles that of SDH. The poplar genome encodes five DQD/SDH-like genes (Poptr1 to Poptr5), which have diverged into two distinct groups based on sequence analysis and protein structure prediction. In vitro biochemical assays proved that Poptr1 and -5 are true DQD/SDHs, whereas Poptr2 and -3 instead have QDH activity with only residual DQD/SDH activity. Poplar DQD/SDHs have distinct expression profiles suggesting separate roles in protein and lignin biosynthesis. Also, the QDH genes are differentially expressed. In summary, quinate (secondary metabolism) and shikimate (primary metabolism) metabolic activities are encoded by distinct members of the same gene family, each having different physiological functions.
DOI: 10.1074/jbc.M114.558536
PubMed: 24942735
PubMed Central: PMC4156088
Affiliations:
Links toward previous steps (curation, corpus...)
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(MeSH)</term><term>Analyse de profil d'expression de gènes (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Gènes de plante (MeSH)</term><term>Populus (génétique)</term><term>Populus (métabolisme)</term><term>Réaction de polymérisation en chaîne (MeSH)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Alcohol Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Alcohol Oxidoreductases</term><term>Quinic Acid</term><term>Shikimic Acid</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Alcohol oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Populus</term></keywords><keywords 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d'acides aminés</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The shikimate pathway leads to the biosynthesis of aromatic amino acids essential for protein biosynthesis and the production of a wide array of plant secondary metabolites. Among them, quinate is an astringent feeding deterrent that can be formed in a single step reaction from 3-dehydroquinate catalyzed by quinate dehydrogenase (QDH). 3-Dehydroquinate is also the substrate for shikimate biosynthesis through the sequential actions of dehydroquinate dehydratase (DQD) and shikimate dehydrogenase (SDH) contained in a single protein in plants. The reaction mechanism of QDH resembles that of SDH. The poplar genome encodes five DQD/SDH-like genes (Poptr1 to Poptr5), which have diverged into two distinct groups based on sequence analysis and protein structure prediction. In vitro biochemical assays proved that Poptr1 and -5 are true DQD/SDHs, whereas Poptr2 and -3 instead have QDH activity with only residual DQD/SDH activity. Poplar DQD/SDHs have distinct expression profiles suggesting separate roles in protein and lignin biosynthesis. Also, the QDH genes are differentially expressed. In summary, quinate (secondary metabolism) and shikimate (primary metabolism) metabolic activities are encoded by distinct members of the same gene family, each having different physiological functions. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24942735</PMID><DateCompleted><Year>2014</Year><Month>12</Month><Day>15</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>289</Volume><Issue>34</Issue><PubDate><Year>2014</Year><Month>Aug</Month><Day>22</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Molecular characterization of quinate and shikimate metabolism in Populus trichocarpa.</ArticleTitle><Pagination><MedlinePgn>23846-58</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M114.558536</ELocationID><Abstract><AbstractText>The shikimate pathway leads to the biosynthesis of aromatic amino acids essential for protein biosynthesis and the production of a wide array of plant secondary metabolites. Among them, quinate is an astringent feeding deterrent that can be formed in a single step reaction from 3-dehydroquinate catalyzed by quinate dehydrogenase (QDH). 3-Dehydroquinate is also the substrate for shikimate biosynthesis through the sequential actions of dehydroquinate dehydratase (DQD) and shikimate dehydrogenase (SDH) contained in a single protein in plants. The reaction mechanism of QDH resembles that of SDH. The poplar genome encodes five DQD/SDH-like genes (Poptr1 to Poptr5), which have diverged into two distinct groups based on sequence analysis and protein structure prediction. In vitro biochemical assays proved that Poptr1 and -5 are true DQD/SDHs, whereas Poptr2 and -3 instead have QDH activity with only residual DQD/SDH activity. Poplar DQD/SDHs have distinct expression profiles suggesting separate roles in protein and lignin biosynthesis. Also, the QDH genes are differentially expressed. In summary, quinate (secondary metabolism) and shikimate (primary metabolism) metabolic activities are encoded by distinct members of the same gene family, each having different physiological functions. </AbstractText><CopyrightInformation>© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Guo</LastName><ForeName>Jia</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>From the Department of Biology and Centre for Forest Biology, University of Victoria, Victoria, British Columbia V8W 2Y2, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Carrington</LastName><ForeName>Yuriko</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>From the Department of Biology and Centre for Forest Biology, University of Victoria, Victoria, British Columbia V8W 2Y2, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Alber</LastName><ForeName>Annette</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>From the Department of Biology and Centre for Forest Biology, University of Victoria, Victoria, British Columbia V8W 2Y2, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ehlting</LastName><ForeName>Jürgen</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>From the Department of Biology and Centre for Forest Biology, University of Victoria, Victoria, British Columbia V8W 2Y2, Canada je@uvic.ca.</Affiliation></AffiliationInfo></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>2014</Year><Month>06</Month><Day>18</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017931">DNA Primers</NameOfSubstance></Chemical><Chemical><RegistryNumber>058C04BGYI</RegistryNumber><NameOfSubstance UI="D011801">Quinic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>29MS2WI2NU</RegistryNumber><NameOfSubstance UI="D012765">Shikimic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D000429">Alcohol Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.24</RegistryNumber><NameOfSubstance UI="C022511">quinate dehydrogenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.25</RegistryNumber><NameOfSubstance UI="C022641">Shikimate dehydrogenase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000429" MajorTopicYN="N">Alcohol Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017931" MajorTopicYN="N">DNA Primers</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020869" MajorTopicYN="N">Gene Expression Profiling</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017343" MajorTopicYN="N">Genes, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016133" MajorTopicYN="N">Polymerase Chain Reaction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011801" MajorTopicYN="N">Quinic Acid</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012765" MajorTopicYN="N">Shikimic Acid</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Enzyme Kinetics</Keyword><Keyword MajorTopicYN="N">Gene Expression</Keyword><Keyword MajorTopicYN="N">Plant Biochemistry</Keyword><Keyword MajorTopicYN="N">Plant Defense</Keyword><Keyword MajorTopicYN="N">Primary Metabolism</Keyword><Keyword MajorTopicYN="N">Quinate Biosynthesis</Keyword><Keyword MajorTopicYN="N">Secondary Metabolism</Keyword><Keyword MajorTopicYN="N">Shikimate Pathway</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>6</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>6</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>12</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24942735</ArticleId><ArticleId IdType="pii">M114.558536</ArticleId><ArticleId IdType="doi">10.1074/jbc.M114.558536</ArticleId><ArticleId 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