Phosphorylation of phenylalanine ammonia-lyase: evidence for a novel protein kinase and identification of the phosphorylated residue.
Identifieur interne : 004868 ( Main/Exploration ); précédent : 004867; suivant : 004869Phosphorylation of phenylalanine ammonia-lyase: evidence for a novel protein kinase and identification of the phosphorylated residue.
Auteurs : E G Allwood [Royaume-Uni] ; D R Davies ; C. Gerrish ; B E Ellis ; G P BolwellSource :
- FEBS letters [ 0014-5793 ] ; 1999.
Descripteurs français
- KwdFr :
- Acides aminés (analyse), Cinétique (MeSH), Données de séquences moléculaires (MeSH), Fabaceae (enzymologie), Facteurs temps (MeSH), Peptides (métabolisme), Phenylalanine ammonia-lyase (métabolisme), Phosphorylation (MeSH), Plantes médicinales (MeSH), Protéines recombinantes (métabolisme), Relation dose-effet des médicaments (MeSH), Séquence d'acides aminés (MeSH), Thréonine (métabolisme), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- analyse : Acides aminés.
- enzymologie : Fabaceae.
- métabolisme : Peptides, Phenylalanine ammonia-lyase, Protéines recombinantes, Thréonine.
- Cinétique, Données de séquences moléculaires, Facteurs temps, Phosphorylation, Plantes médicinales, Relation dose-effet des médicaments, Séquence d'acides aminés, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Amino Acids (analysis), Dose-Response Relationship, Drug (MeSH), Electrophoresis, Polyacrylamide Gel (MeSH), Fabaceae (enzymology), Kinetics (MeSH), Molecular Sequence Data (MeSH), Peptides (metabolism), Phenylalanine Ammonia-Lyase (metabolism), Phosphorylation (MeSH), Plants, Medicinal (MeSH), Recombinant Proteins (metabolism), Threonine (metabolism), Time Factors (MeSH).
- MESH :
- chemical , analysis : Amino Acids.
- enzymology : Fabaceae.
- chemical , metabolism : Peptides, Phenylalanine Ammonia-Lyase, Recombinant Proteins, Threonine.
- Amino Acid Sequence, Dose-Response Relationship, Drug, Electrophoresis, Polyacrylamide Gel, Kinetics, Molecular Sequence Data, Phosphorylation, Plants, Medicinal, Time Factors.
Abstract
The site of phosphorylation of phenylalanine ammonia-lyase (PAL) has been identified as a threonine residue. A Ca(2+)-stimulated protein kinase of approximately 55 kDa has been partially purified from elicited cells. The kinase can phosphorylate a synthetic peptide derived from PAL and a recombinant poplar PAL. PAL phosphorylation was associated with a decrease in Vmax in agreement with the suggestion that protein phosphorylation is involved in marking PAL subunits for turnover. The phosphorylation site in French bean PAL is most likely Thr545 in the sequence VAKRTLTT (539-546). Conservation of the phosphorylation site in PAL from diverse species suggests that phosphorylation of PAL may be a ubiquitous regulatory mechanism in higher plants.
DOI: 10.1016/s0014-5793(99)00998-9
PubMed: 10486561
Affiliations:
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Le document en format XML
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Gerrish</name></author><author><name sortKey="Ellis, B E" sort="Ellis, B E" uniqKey="Ellis B" first="B E" last="Ellis">B E Ellis</name></author><author><name sortKey="Bolwell, G P" sort="Bolwell, G P" uniqKey="Bolwell G" first="G P" last="Bolwell">G P Bolwell</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1999">1999</date><idno type="RBID">pubmed:10486561</idno><idno type="pmid">10486561</idno><idno type="doi">10.1016/s0014-5793(99)00998-9</idno><idno type="wicri:Area/Main/Corpus">004902</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">004902</idno><idno type="wicri:Area/Main/Curation">004902</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">004902</idno><idno type="wicri:Area/Main/Exploration">004902</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Phosphorylation of phenylalanine ammonia-lyase: evidence for a novel protein kinase and identification of the phosphorylated residue.</title><author><name sortKey="Allwood, E G" sort="Allwood, E G" uniqKey="Allwood E" first="E G" last="Allwood">E G Allwood</name><affiliation wicri:level="4"><nlm:affiliation>Division of Biochemistry, Royal Holloway and Bedford New College, University of London, Egham, Surrey, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Division of Biochemistry, Royal Holloway and Bedford New College, University of London, Egham, Surrey</wicri:regionArea><orgName type="university">Université de Londres</orgName><placeName><settlement type="city">Londres</settlement><region type="country">Angleterre</region><region type="région" nuts="1">Grand Londres</region></placeName></affiliation></author><author><name sortKey="Davies, D R" sort="Davies, D R" uniqKey="Davies D" first="D R" last="Davies">D R Davies</name></author><author><name sortKey="Gerrish, C" sort="Gerrish, C" uniqKey="Gerrish C" first="C" last="Gerrish">C. 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A Ca(2+)-stimulated protein kinase of approximately 55 kDa has been partially purified from elicited cells. The kinase can phosphorylate a synthetic peptide derived from PAL and a recombinant poplar PAL. PAL phosphorylation was associated with a decrease in Vmax in agreement with the suggestion that protein phosphorylation is involved in marking PAL subunits for turnover. The phosphorylation site in French bean PAL is most likely Thr545 in the sequence VAKRTLTT (539-546). Conservation of the phosphorylation site in PAL from diverse species suggests that phosphorylation of PAL may be a ubiquitous regulatory mechanism in higher plants.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10486561</PMID><DateCompleted><Year>1999</Year><Month>10</Month><Day>08</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>457</Volume><Issue>1</Issue><PubDate><Year>1999</Year><Month>Aug</Month><Day>20</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Phosphorylation of phenylalanine ammonia-lyase: evidence for a novel protein kinase and identification of the phosphorylated residue.</ArticleTitle><Pagination><MedlinePgn>47-52</MedlinePgn></Pagination><Abstract><AbstractText>The site of phosphorylation of phenylalanine ammonia-lyase (PAL) has been identified as a threonine residue. A Ca(2+)-stimulated protein kinase of approximately 55 kDa has been partially purified from elicited cells. The kinase can phosphorylate a synthetic peptide derived from PAL and a recombinant poplar PAL. PAL phosphorylation was associated with a decrease in Vmax in agreement with the suggestion that protein phosphorylation is involved in marking PAL subunits for turnover. The phosphorylation site in French bean PAL is most likely Thr545 in the sequence VAKRTLTT (539-546). Conservation of the phosphorylation site in PAL from diverse species suggests that phosphorylation of PAL may be a ubiquitous regulatory mechanism in higher plants.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Allwood</LastName><ForeName>E G</ForeName><Initials>EG</Initials><AffiliationInfo><Affiliation>Division of Biochemistry, Royal Holloway and Bedford New College, University of London, Egham, Surrey, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Davies</LastName><ForeName>D R</ForeName><Initials>DR</Initials></Author><Author ValidYN="Y"><LastName>Gerrish</LastName><ForeName>C</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Ellis</LastName><ForeName>B E</ForeName><Initials>BE</Initials></Author><Author ValidYN="Y"><LastName>Bolwell</LastName><ForeName>G P</ForeName><Initials>GP</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal 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MajorTopicYN="N">Time Factors</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1999</Year><Month>9</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1999</Year><Month>9</Month><Day>16</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1999</Year><Month>9</Month><Day>16</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10486561</ArticleId><ArticleId IdType="pii">S0014-5793(99)00998-9</ArticleId><ArticleId IdType="doi">10.1016/s0014-5793(99)00998-9</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Grand Londres</li></region><settlement><li>Londres</li></settlement><orgName><li>Université de Londres</li></orgName></list><tree><noCountry><name sortKey="Bolwell, G P" sort="Bolwell, G P" uniqKey="Bolwell G" first="G P" last="Bolwell">G P Bolwell</name><name sortKey="Davies, D R" sort="Davies, D R" uniqKey="Davies D" first="D R" last="Davies">D R Davies</name><name sortKey="Ellis, B E" sort="Ellis, B E" uniqKey="Ellis B" first="B E" last="Ellis">B E Ellis</name><name sortKey="Gerrish, C" sort="Gerrish, C" uniqKey="Gerrish C" first="C" last="Gerrish">C. Gerrish</name></noCountry><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Allwood, E G" sort="Allwood, E G" uniqKey="Allwood E" first="E G" last="Allwood">E G Allwood</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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