Phosphorylation of phenylalanine ammonia-lyase: evidence for a novel protein kinase and identification of the phosphorylated residue.
Identifieur interne : 004902 ( Main/Corpus ); précédent : 004901; suivant : 004903Phosphorylation of phenylalanine ammonia-lyase: evidence for a novel protein kinase and identification of the phosphorylated residue.
Auteurs : E G Allwood ; D R Davies ; C. Gerrish ; B E Ellis ; G P BolwellSource :
- FEBS letters [ 0014-5793 ] ; 1999.
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
Links to Exploration step
pubmed:10486561Le 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></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><nlm:affiliation>Division of Biochemistry, Royal Holloway and Bedford New College, University of London, Egham, Surrey, UK.</nlm:affiliation></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. 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></analytic><series><title level="j">FEBS letters</title><idno type="ISSN">0014-5793</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Amino Acids (analysis)</term><term>Dose-Response Relationship, Drug (MeSH)</term><term>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Fabaceae (enzymology)</term><term>Kinetics (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Peptides (metabolism)</term><term>Phenylalanine Ammonia-Lyase (metabolism)</term><term>Phosphorylation (MeSH)</term><term>Plants, Medicinal (MeSH)</term><term>Recombinant Proteins (metabolism)</term><term>Threonine (metabolism)</term><term>Time Factors (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Amino Acids</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Fabaceae</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptides</term><term>Phenylalanine Ammonia-Lyase</term><term>Recombinant Proteins</term><term>Threonine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Dose-Response Relationship, Drug</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Kinetics</term><term>Molecular Sequence Data</term><term>Phosphorylation</term><term>Plants, Medicinal</term><term>Time Factors</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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.</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 Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS Lett</MedlineTA><NlmUniqueID>0155157</NlmUniqueID><ISSNLinking>0014-5793</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>2ZD004190S</RegistryNumber><NameOfSubstance UI="D013912">Threonine</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.3.1.24</RegistryNumber><NameOfSubstance UI="D010650">Phenylalanine Ammonia-Lyase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004305" MajorTopicYN="N">Dose-Response Relationship, Drug</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007887" MajorTopicYN="N">Fabaceae</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010650" MajorTopicYN="N">Phenylalanine Ammonia-Lyase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010946" MajorTopicYN="N">Plants, Medicinal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013912" MajorTopicYN="N">Threonine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013997" 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></record>Pour manipuler ce document sous Unix (Dilib)
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