Publikation:

Medium-chain acyl CoA dehydrogenase : evidence for phosphorylation

Lade...
Vorschaubild

Dateien

Medium_chain_acyl_CoA_dehydrogenase.pdf
Medium_chain_acyl_CoA_dehydrogenase.pdfGröße: 217.72 KBDownloads: 300

Datum

1997

Autor:innen

Macheroux, Peter
Sanner, Christoph
Büttner, Hermann
Kieweg, Volker
Rüterjans, Heinz

Herausgeber:innen

Kontakt

ISSN der Zeitschrift

Electronic ISSN

ISBN

Bibliografische Daten

Verlag

Schriftenreihe

Auflagebezeichnung

ArXiv-ID

Internationale Patentnummer

Angaben zur Forschungsförderung

Projekt

Open Access-Veröffentlichung
Open Access Green
Core Facility der Universität Konstanz

Gesperrt bis

Titel in einer weiteren Sprache

Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published

Erschienen in

Biological Chemistry. 1997, 378(11), pp. 1381-1385. ISSN 1431-6730. eISSN 1437-4315. Available under: doi: 10.1515/bchm.1997.378.11.1381

Zusammenfassung

Mature medium chain acyl-CoA dehydrogenase isolated from pig kidney (pkMCADH) and originating from mitochondria carries a phosphate group as demonstrated by 31P-NMR-spectroscopy and chemical analysis. Two broad resonances at - 6.3 and - 8 ppm are observed and are assigned to the pyrophosphate group of the cofactor FAD. A third, narrow resonance at 4.65 ppm indicates the presence of a phosphomonoester residue. Chemical analysis of intact pkMCADH shows the presence of 3 ± 0.3 phosphates, those of FAD and of an additional covalently attached phosphate. With recombinant, human wild type MCADH expressed in and purified from E. coli only the two FAD phosphates (2 ± 0.35) are found. Similarly, pkMCADH which has been converted to the apoenzyme and reconstituted to holoenzyme also contains 2 ± 0.4 phosphates. The covalently bound phosphate can be hydrolyzed by phosphatase and subsequently removed by dialysis. The phosphate group has no detectable effect on the catalytic activity of the MCADH measured with artificial and natural electron acceptors such as pig electron transferring flavoprotein. However, phosphorylation has a marked effect on protein solubility which is +5-fold lower for the dephosphorylated protein.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
570 Biowissenschaften, Biologie

Schlagwörter

Flavin, beta-oxidation, 31P-NMR

Konferenz

Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Zugehörige Datensätze in KOPS

Zitieren

ISO 690MACHEROUX, Peter, Christoph SANNER, Hermann BÜTTNER, Volker KIEWEG, Heinz RÜTERJANS, Sandro GHISLA, 1997. Medium-chain acyl CoA dehydrogenase : evidence for phosphorylation. In: Biological Chemistry. 1997, 378(11), pp. 1381-1385. ISSN 1431-6730. eISSN 1437-4315. Available under: doi: 10.1515/bchm.1997.378.11.1381
BibTex
@article{Macheroux1997Mediu-7645,
  year={1997},
  doi={10.1515/bchm.1997.378.11.1381},
  title={Medium-chain acyl CoA dehydrogenase : evidence for phosphorylation},
  number={11},
  volume={378},
  issn={1431-6730},
  journal={Biological Chemistry},
  pages={1381--1385},
  author={Macheroux, Peter and Sanner, Christoph and Büttner, Hermann and Kieweg, Volker and Rüterjans, Heinz and Ghisla, Sandro}
}
RDF
<rdf:RDF
    xmlns:dcterms="http://purl.org/dc/terms/"
    xmlns:dc="http://purl.org/dc/elements/1.1/"
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:bibo="http://purl.org/ontology/bibo/"
    xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
    xmlns:foaf="http://xmlns.com/foaf/0.1/"
    xmlns:void="http://rdfs.org/ns/void#"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > 
  <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/7645">
    <dc:creator>Macheroux, Peter</dc:creator>
    <dc:format>application/pdf</dc:format>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:36:01Z</dc:date>
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/7645/1/Medium_chain_acyl_CoA_dehydrogenase.pdf"/>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:36:01Z</dcterms:available>
    <dc:creator>Büttner, Hermann</dc:creator>
    <dc:contributor>Sanner, Christoph</dc:contributor>
    <dcterms:bibliographicCitation>First publ. in: Biological Chemistry 378 (1997), pp. 1381-1385</dcterms:bibliographicCitation>
    <dc:contributor>Rüterjans, Heinz</dc:contributor>
    <dc:contributor>Macheroux, Peter</dc:contributor>
    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/7645"/>
    <dc:creator>Sanner, Christoph</dc:creator>
    <dc:contributor>Ghisla, Sandro</dc:contributor>
    <dc:contributor>Kieweg, Volker</dc:contributor>
    <dc:contributor>Büttner, Hermann</dc:contributor>
    <dc:creator>Kieweg, Volker</dc:creator>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/7645/1/Medium_chain_acyl_CoA_dehydrogenase.pdf"/>
    <dc:creator>Rüterjans, Heinz</dc:creator>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dcterms:title>Medium-chain acyl CoA dehydrogenase : evidence for phosphorylation</dcterms:title>
    <dc:creator>Ghisla, Sandro</dc:creator>
    <dcterms:issued>1997</dcterms:issued>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:language>eng</dc:language>
    <dcterms:abstract xml:lang="deu">Mature medium chain acyl-CoA dehydrogenase isolated from pig kidney (pkMCADH) and originating from mitochondria carries a phosphate group as demonstrated by 31P-NMR-spectroscopy and chemical analysis. Two broad resonances at - 6.3 and - 8 ppm are observed and are assigned to the pyrophosphate group of the cofactor FAD. A third, narrow resonance at 4.65 ppm indicates the presence of a phosphomonoester residue. Chemical analysis of intact pkMCADH shows the presence of 3 ± 0.3 phosphates, those of FAD and of an additional covalently attached phosphate. With recombinant, human wild type MCADH expressed in and purified from E. coli only the two FAD phosphates (2 ± 0.35) are found. Similarly, pkMCADH which has been converted to the apoenzyme and reconstituted to holoenzyme also contains 2 ± 0.4 phosphates. The covalently bound phosphate can be hydrolyzed by phosphatase and subsequently removed by dialysis. The phosphate group has no detectable effect on the catalytic activity of the MCADH measured with artificial and natural electron acceptors such as pig electron transferring flavoprotein. However, phosphorylation has a marked effect on protein solubility which is +5-fold lower for the dephosphorylated protein.</dcterms:abstract>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
  </rdf:Description>
</rdf:RDF>

Interner Vermerk

xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter

Kontakt
URL der Originalveröffentl.

Prüfdatum der URL

Prüfungsdatum der Dissertation

Finanzierungsart

Kommentar zur Publikation

Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Nein
Begutachtet
Diese Publikation teilen