Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous
Identifieur interne : 001109 ( Istex/Corpus ); précédent : 001108; suivant : 001110Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous
Auteurs : F. Rob JacksonSource :
- Journal of Molecular Evolution [ 0022-2844 ] ; 1990-10-01.
English descriptors
- KwdEn :
- Acad, Acid decarboxylase, Bhdc, Cgad, Database, Decarboxylase, Decarboxylase family, Dopa, Dopa decarboxylase, Drosophila, Eukaryotic, Eukaryotic decarboxylases, Famd, Fddc, Fgad, Histidine, Histidine decarboxylase, Multiple sequence alignment, Natl, Nucleotide sequence, Other decarboxylases, Proc, Proc natl acad, Ptdc, Rddc, Rhdc.
- Teeft :
- Acad, Acid decarboxylase, Bhdc, Cgad, Database, Decarboxylase, Decarboxylase family, Dopa, Dopa decarboxylase, Drosophila, Eukaryotic, Eukaryotic decarboxylases, Famd, Fddc, Fgad, Histidine, Histidine decarboxylase, Multiple sequence alignment, Natl, Nucleotide sequence, Other decarboxylases, Proc, Proc natl acad, Ptdc, Rddc, Rhdc.
Abstract
Summary: A database search has revealed significant and extensive sequence similarities among prokaryotic and eukaryotic pyridoxal phosphate (PLP)-dependent decarboxylases, includingDrosophila glutamic acid decarboxylase (GAD) and bacterial histidine decarboxylase (HDC). Based on these findings, the sequences of seven PLP-dependent decarboxylases from five different organisms have been aligned to derive a consensus sequence for this family of enzymes. In addition, quantitative methods have been employed to calculate the relative evolutionary distances between pairs of the decarboxylases comprising this family. The multiple sequence analysis together with the quantitative results strongly suggest an ancient and common origin for all PLP-dependent decarboxylases. This analysis also indicates that prokaryotic and eukaryotic HDC activities evolved independently. Finally, a sensitive search algorithm (PROFILE) was unable to detect additional members of this decarboxylase family in protein sequence databases.
Url:
DOI: 10.1007/BF02101126
Links to Exploration step
ISTEX:9EADD954CD6EE983DE0BC564B31DDD9B3B571E14Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous</title><author><name sortKey="Jackson, F Rob" sort="Jackson, F Rob" uniqKey="Jackson F" first="F. Rob" last="Jackson">F. Rob Jackson</name><affiliation><mods:affiliation>Neurobiology Division, The Worcester Foundation For Experimental Biology, 222 Maple Avenue, 01545, Shrewsbury, Massachusetts, USA</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:9EADD954CD6EE983DE0BC564B31DDD9B3B571E14</idno><date when="1990" year="1990">1990</date><idno type="doi">10.1007/BF02101126</idno><idno type="url">https://api.istex.fr/document/9EADD954CD6EE983DE0BC564B31DDD9B3B571E14/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">001109</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001109</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous</title><author><name sortKey="Jackson, F Rob" sort="Jackson, F Rob" uniqKey="Jackson F" first="F. Rob" last="Jackson">F. Rob Jackson</name><affiliation><mods:affiliation>Neurobiology Division, The Worcester Foundation For Experimental Biology, 222 Maple Avenue, 01545, Shrewsbury, Massachusetts, USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Molecular Evolution</title><title level="j" type="abbrev">J Mol Evol</title><idno type="ISSN">0022-2844</idno><idno type="eISSN">1432-1432</idno><imprint><publisher>Springer-Verlag</publisher><pubPlace>New York</pubPlace><date type="published" when="1990-10-01">1990-10-01</date><biblScope unit="volume">31</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="325">325</biblScope><biblScope unit="page" to="329">329</biblScope></imprint><idno type="ISSN">0022-2844</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0022-2844</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acad</term><term>Acid decarboxylase</term><term>Bhdc</term><term>Cgad</term><term>Database</term><term>Decarboxylase</term><term>Decarboxylase family</term><term>Dopa</term><term>Dopa decarboxylase</term><term>Drosophila</term><term>Eukaryotic</term><term>Eukaryotic decarboxylases</term><term>Famd</term><term>Fddc</term><term>Fgad</term><term>Histidine</term><term>Histidine decarboxylase</term><term>Multiple sequence alignment</term><term>Natl</term><term>Nucleotide sequence</term><term>Other decarboxylases</term><term>Proc</term><term>Proc natl acad</term><term>Ptdc</term><term>Rddc</term><term>Rhdc</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Acad</term><term>Acid decarboxylase</term><term>Bhdc</term><term>Cgad</term><term>Database</term><term>Decarboxylase</term><term>Decarboxylase family</term><term>Dopa</term><term>Dopa decarboxylase</term><term>Drosophila</term><term>Eukaryotic</term><term>Eukaryotic decarboxylases</term><term>Famd</term><term>Fddc</term><term>Fgad</term><term>Histidine</term><term>Histidine decarboxylase</term><term>Multiple sequence alignment</term><term>Natl</term><term>Nucleotide sequence</term><term>Other decarboxylases</term><term>Proc</term><term>Proc natl acad</term><term>Ptdc</term><term>Rddc</term><term>Rhdc</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Summary: A database search has revealed significant and extensive sequence similarities among prokaryotic and eukaryotic pyridoxal phosphate (PLP)-dependent decarboxylases, includingDrosophila glutamic acid decarboxylase (GAD) and bacterial histidine decarboxylase (HDC). Based on these findings, the sequences of seven PLP-dependent decarboxylases from five different organisms have been aligned to derive a consensus sequence for this family of enzymes. In addition, quantitative methods have been employed to calculate the relative evolutionary distances between pairs of the decarboxylases comprising this family. The multiple sequence analysis together with the quantitative results strongly suggest an ancient and common origin for all PLP-dependent decarboxylases. This analysis also indicates that prokaryotic and eukaryotic HDC activities evolved independently. Finally, a sensitive search algorithm (PROFILE) was unable to detect additional members of this decarboxylase family in protein sequence databases.</div></front></TEI><istex><corpusName>springer</corpusName><keywords><teeft><json:string>decarboxylase</json:string><json:string>bhdc</json:string><json:string>fgad</json:string><json:string>rddc</json:string><json:string>ptdc</json:string><json:string>rhdc</json:string><json:string>database</json:string><json:string>fddc</json:string><json:string>drosophila</json:string><json:string>famd</json:string><json:string>cgad</json:string><json:string>eukaryotic</json:string><json:string>histidine</json:string><json:string>dopa</json:string><json:string>proc</json:string><json:string>natl</json:string><json:string>acad</json:string><json:string>proc natl acad</json:string><json:string>multiple sequence alignment</json:string><json:string>decarboxylase family</json:string><json:string>eukaryotic decarboxylases</json:string><json:string>nucleotide sequence</json:string><json:string>other decarboxylases</json:string><json:string>dopa decarboxylase</json:string><json:string>histidine decarboxylase</json:string><json:string>acid decarboxylase</json:string></teeft></keywords><author><json:item><name>F. Rob Jackson</name><affiliations><json:string>Neurobiology Division, The Worcester Foundation For Experimental Biology, 222 Maple Avenue, 01545, Shrewsbury, Massachusetts, USA</json:string></affiliations></json:item></author><articleId><json:string>BF02101126</json:string><json:string>Art8</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>Letter</json:string></originalGenre><abstract>Summary: A database search has revealed significant and extensive sequence similarities among prokaryotic and eukaryotic pyridoxal phosphate (PLP)-dependent decarboxylases, includingDrosophila glutamic acid decarboxylase (GAD) and bacterial histidine decarboxylase (HDC). Based on these findings, the sequences of seven PLP-dependent decarboxylases from five different organisms have been aligned to derive a consensus sequence for this family of enzymes. In addition, quantitative methods have been employed to calculate the relative evolutionary distances between pairs of the decarboxylases comprising this family. The multiple sequence analysis together with the quantitative results strongly suggest an ancient and common origin for all PLP-dependent decarboxylases. This analysis also indicates that prokaryotic and eukaryotic HDC activities evolved independently. Finally, a sensitive search algorithm (PROFILE) was unable to detect additional members of this decarboxylase family in protein sequence databases.</abstract><qualityIndicators><score>5.101</score><pdfWordCount>3553</pdfWordCount><pdfCharCount>21884</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>5</pdfPageCount><pdfPageSize>540 x 734.28 pts</pdfPageSize><refBibsNative>false</refBibsNative><abstractWordCount>129</abstractWordCount><abstractCharCount>1018</abstractCharCount><keywordCount>0</keywordCount></qualityIndicators><title>Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous</title><genre><json:string>review-article</json:string></genre><host><title>Journal of Molecular Evolution</title><language><json:string>unknown</json:string></language><publicationDate>1990</publicationDate><copyrightDate>1990</copyrightDate><issn><json:string>0022-2844</json:string></issn><eissn><json:string>1432-1432</json:string></eissn><journalId><json:string>239</json:string></journalId><volume>31</volume><issue>4</issue><pages><first>325</first><last>329</last></pages><genre><json:string>journal</json:string></genre><subject><json:item><value>Plant Sciences</value></json:item><json:item><value>Cell Biology</value></json:item><json:item><value>Microbiology</value></json:item></subject></host><categories><wos><json:string>science</json:string><json:string>genetics & heredity</json:string><json:string>evolutionary biology</json:string><json:string>biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>natural sciences</json:string><json:string>biology</json:string><json:string>evolutionary biology</json:string></scienceMetrix><inist><json:string>sciences appliquees, technologies et medecines</json:string><json:string>sciences biologiques et medicales</json:string><json:string>sciences biologiques fondamentales et appliquees. psychologie</json:string><json:string>sylviculture</json:string></inist></categories><publicationDate>1990</publicationDate><copyrightDate>1990</copyrightDate><doi><json:string>10.1007/BF02101126</json:string></doi><id>9EADD954CD6EE983DE0BC564B31DDD9B3B571E14</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/9EADD954CD6EE983DE0BC564B31DDD9B3B571E14/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/9EADD954CD6EE983DE0BC564B31DDD9B3B571E14/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/9EADD954CD6EE983DE0BC564B31DDD9B3B571E14/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous</title><respStmt><resp>Références bibliographiques récupérées via GROBID</resp><name resp="ISTEX-API">ISTEX-API (INIST-CNRS)</name></respStmt></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://publisher-list.data.istex.fr">Springer-Verlag</publisher><pubPlace>New York</pubPlace><availability><licence><p>Springer-Verlag New York Inc., 1990</p></licence><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</p></availability><date>1990-01-15</date></publicationStmt><notesStmt><note type="review-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-L5L7X3NF-P">review-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note><note>Letter to the Editor</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous</title><author xml:id="author-0000" corresp="yes"><persName><forename type="first">F.</forename><surname>Jackson</surname></persName><affiliation>Neurobiology Division, The Worcester Foundation For Experimental Biology, 222 Maple Avenue, 01545, Shrewsbury, Massachusetts, USA</affiliation></author><idno type="istex">9EADD954CD6EE983DE0BC564B31DDD9B3B571E14</idno><idno type="ark">ark:/67375/1BB-SFCN0803-T</idno><idno type="DOI">10.1007/BF02101126</idno><idno type="article-id">BF02101126</idno><idno type="article-id">Art8</idno></analytic><monogr><title level="j">Journal of Molecular Evolution</title><title level="j" type="abbrev">J Mol Evol</title><idno type="pISSN">0022-2844</idno><idno type="eISSN">1432-1432</idno><idno type="journal-ID">true</idno><idno type="issue-article-count">11</idno><idno type="volume-issue-count">6</idno><imprint><publisher>Springer-Verlag</publisher><pubPlace>New York</pubPlace><date type="published" when="1990-10-01"></date><biblScope unit="volume">31</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="325">325</biblScope><biblScope unit="page" to="329">329</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1990-01-15</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Summary: A database search has revealed significant and extensive sequence similarities among prokaryotic and eukaryotic pyridoxal phosphate (PLP)-dependent decarboxylases, includingDrosophila glutamic acid decarboxylase (GAD) and bacterial histidine decarboxylase (HDC). Based on these findings, the sequences of seven PLP-dependent decarboxylases from five different organisms have been aligned to derive a consensus sequence for this family of enzymes. In addition, quantitative methods have been employed to calculate the relative evolutionary distances between pairs of the decarboxylases comprising this family. The multiple sequence analysis together with the quantitative results strongly suggest an ancient and common origin for all PLP-dependent decarboxylases. This analysis also indicates that prokaryotic and eukaryotic HDC activities evolved independently. Finally, a sensitive search algorithm (PROFILE) was unable to detect additional members of this decarboxylase family in protein sequence databases.</p></abstract><textClass><keywords scheme="Journal Subject"><list><head>Life Sciences</head><item><term>Plant Sciences</term></item><item><term>Cell Biology</term></item><item><term>Microbiology</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1990-01-15">Created</change><change when="1990-10-01">Published</change><change xml:id="refBibs-istex" who="#ISTEX-API" when="2017-10-2">References added</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/9EADD954CD6EE983DE0BC564B31DDD9B3B571E14/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Springer, Publisher found" wicri:toSee="no header"><istex:xmlDeclaration>version="1.0" encoding="UTF-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//Springer-Verlag//DTD A++ V2.4//EN" URI="http://devel.springer.de/A++/V2.4/DTD/A++V2.4.dtd" name="istex:docType"></istex:docType><istex:document><Publisher><PublisherInfo><PublisherName>Springer-Verlag</PublisherName><PublisherLocation>New York</PublisherLocation></PublisherInfo><Journal><JournalInfo JournalProductType="ArchiveJournal" NumberingStyle="Unnumbered"><JournalID>239</JournalID><JournalPrintISSN>0022-2844</JournalPrintISSN><JournalElectronicISSN>1432-1432</JournalElectronicISSN><JournalTitle>Journal of Molecular Evolution</JournalTitle><JournalAbbreviatedTitle>J Mol Evol</JournalAbbreviatedTitle><JournalSubjectGroup><JournalSubject Type="Primary">Life Sciences</JournalSubject><JournalSubject Type="Secondary">Plant Sciences</JournalSubject><JournalSubject Type="Secondary">Cell Biology</JournalSubject><JournalSubject Type="Secondary">Microbiology</JournalSubject></JournalSubjectGroup></JournalInfo><Volume><VolumeInfo VolumeType="Regular" TocLevels="0"><VolumeIDStart>31</VolumeIDStart><VolumeIDEnd>31</VolumeIDEnd><VolumeIssueCount>6</VolumeIssueCount></VolumeInfo><Issue IssueType="Regular"><IssueInfo TocLevels="0"><IssueIDStart>4</IssueIDStart><IssueIDEnd>4</IssueIDEnd><IssueArticleCount>11</IssueArticleCount><IssueHistory><CoverDate><Year>1990</Year><Month>10</Month></CoverDate></IssueHistory><IssueCopyright><CopyrightHolderName>Springer-Verlag New York Inc.</CopyrightHolderName><CopyrightYear>1990</CopyrightYear></IssueCopyright></IssueInfo><Article ID="Art8"><ArticleInfo Language="En" ArticleType="Letter" NumberingStyle="Unnumbered" TocLevels="0" ContainsESM="No"><ArticleID>BF02101126</ArticleID><ArticleDOI>10.1007/BF02101126</ArticleDOI><ArticleSequenceNumber>8</ArticleSequenceNumber><ArticleTitle Language="En">Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous</ArticleTitle><ArticleCategory>Letter to the Editor</ArticleCategory><ArticleFirstPage>325</ArticleFirstPage><ArticleLastPage>329</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2005</Year><Month>8</Month><Day>2</Day></RegistrationDate><Received><Year>1990</Year><Month>1</Month><Day>15</Day></Received><Revised><Year>1990</Year><Month>4</Month><Day>25</Day></Revised><Accepted><Year>1990</Year><Month>5</Month><Day>10</Day></Accepted></ArticleHistory><ArticleCopyright><CopyrightHolderName>Springer-Verlag New York Inc.</CopyrightHolderName><CopyrightYear>1990</CopyrightYear></ArticleCopyright><ArticleGrants Type="Regular"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants><ArticleContext><JournalID>239</JournalID><VolumeIDStart>31</VolumeIDStart><VolumeIDEnd>31</VolumeIDEnd><IssueIDStart>4</IssueIDStart><IssueIDEnd>4</IssueIDEnd></ArticleContext></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1" CorrespondingAffiliationID="Aff1"><AuthorName DisplayOrder="Western"><GivenName>F.</GivenName><GivenName>Rob</GivenName><FamilyName>Jackson</FamilyName></AuthorName></Author><Affiliation ID="Aff1"><OrgDivision>Neurobiology Division</OrgDivision><OrgName>The Worcester Foundation For Experimental Biology</OrgName><OrgAddress><Street>222 Maple Avenue</Street><Postcode>01545</Postcode><City>Shrewsbury</City><State>Massachusetts</State><Country>USA</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Summary</Heading><Para>A database search has revealed significant and extensive sequence similarities among prokaryotic and eukaryotic pyridoxal phosphate (PLP)-dependent decarboxylases, including<Emphasis Type="Italic">Drosophila</Emphasis> glutamic acid decarboxylase (GAD) and bacterial histidine decarboxylase (HDC). Based on these findings, the sequences of seven PLP-dependent decarboxylases from five different organisms have been aligned to derive a consensus sequence for this family of enzymes. In addition, quantitative methods have been employed to calculate the relative evolutionary distances between pairs of the decarboxylases comprising this family. The multiple sequence analysis together with the quantitative results strongly suggest an ancient and common origin for all PLP-dependent decarboxylases. This analysis also indicates that prokaryotic and eukaryotic HDC activities evolved independently. Finally, a sensitive search algorithm (PROFILE) was unable to detect additional members of this decarboxylase family in protein sequence databases.</Para></Abstract><KeywordGroup Language="En"><Heading>Key words</Heading><Keyword>PLP-dependent decarboxylase</Keyword><Keyword>Evolution</Keyword><Keyword>Profile analysis</Keyword></KeywordGroup></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous</title></titleInfo><name type="personal" displayLabel="corresp"><namePart type="given">F.</namePart><namePart type="given">Rob</namePart><namePart type="family">Jackson</namePart><affiliation>Neurobiology Division, The Worcester Foundation For Experimental Biology, 222 Maple Avenue, 01545, Shrewsbury, Massachusetts, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="review-article" displayLabel="Letter" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-L5L7X3NF-P">review-article</genre><originInfo><publisher>Springer-Verlag</publisher><place><placeTerm type="text">New York</placeTerm></place><dateCreated encoding="w3cdtf">1990-01-15</dateCreated><dateIssued encoding="w3cdtf">1990-10-01</dateIssued><dateIssued encoding="w3cdtf">1990</dateIssued><copyrightDate encoding="w3cdtf">1990</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Summary: A database search has revealed significant and extensive sequence similarities among prokaryotic and eukaryotic pyridoxal phosphate (PLP)-dependent decarboxylases, includingDrosophila glutamic acid decarboxylase (GAD) and bacterial histidine decarboxylase (HDC). Based on these findings, the sequences of seven PLP-dependent decarboxylases from five different organisms have been aligned to derive a consensus sequence for this family of enzymes. In addition, quantitative methods have been employed to calculate the relative evolutionary distances between pairs of the decarboxylases comprising this family. The multiple sequence analysis together with the quantitative results strongly suggest an ancient and common origin for all PLP-dependent decarboxylases. This analysis also indicates that prokaryotic and eukaryotic HDC activities evolved independently. Finally, a sensitive search algorithm (PROFILE) was unable to detect additional members of this decarboxylase family in protein sequence databases.</abstract><note>Letter to the Editor</note><relatedItem type="host"><titleInfo><title>Journal of Molecular Evolution</title></titleInfo><titleInfo type="abbreviated"><title>J Mol Evol</title></titleInfo><genre type="journal" displayLabel="Archive Journal" authority="ISTEX" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>Springer</publisher><dateIssued encoding="w3cdtf">1990-10-01</dateIssued><copyrightDate encoding="w3cdtf">1990</copyrightDate></originInfo><subject><genre>Life Sciences</genre><topic>Plant Sciences</topic><topic>Cell Biology</topic><topic>Microbiology</topic></subject><identifier type="ISSN">0022-2844</identifier><identifier type="eISSN">1432-1432</identifier><identifier type="JournalID">239</identifier><identifier type="IssueArticleCount">11</identifier><identifier type="VolumeIssueCount">6</identifier><part><date>1990</date><detail type="volume"><number>31</number><caption>vol.</caption></detail><detail type="issue"><number>4</number><caption>no.</caption></detail><extent unit="pages"><start>325</start><end>329</end></extent></part><recordInfo><recordOrigin>Springer-Verlag New York Inc., 1990</recordOrigin></recordInfo></relatedItem><identifier type="istex">9EADD954CD6EE983DE0BC564B31DDD9B3B571E14</identifier><identifier type="ark">ark:/67375/1BB-SFCN0803-T</identifier><identifier type="DOI">10.1007/BF02101126</identifier><identifier type="ArticleID">BF02101126</identifier><identifier type="ArticleID">Art8</identifier><accessCondition type="use and reproduction" contentType="copyright">Springer-Verlag New York Inc., 1990</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</recordContentSource><recordOrigin>Springer-Verlag New York Inc., 1990</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/document/9EADD954CD6EE983DE0BC564B31DDD9B3B571E14/metadata/json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Lorraine/explor/LrgpV1/Data/Istex/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001109 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Istex/Corpus/biblio.hfd -nk 001109 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Lorraine
|area= LrgpV1
|flux= Istex
|étape= Corpus
|type= RBID
|clé= ISTEX:9EADD954CD6EE983DE0BC564B31DDD9B3B571E14
|texte= Prokaryotic and eukaryotic pyridoxal-dependent decarboxylases are homologous
}}
| This area was generated with Dilib version V0.6.32. |  |