Different Enzymatic Processing of γ-Phosphoramidate and γ-Phosphoester-Modified ATP Analogues

Lade...
Vorschaubild
Dateien
Ermert_0-406367.pdf
Ermert_0-406367.pdfGröße: 183.67 KBDownloads: 603
Datum
2017
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
Sammlungen
Core Facility der Universität Konstanz
Gesperrt bis
Titel in einer weiteren Sprache
Forschungsvorhaben
Organisationseinheiten
Zeitschriftenheft
Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published
Erschienen in
Zusammenfassung

Monitoring the activity of ATP-consuming enzymes provides the basis for elucidating their modes of action and regulation. Although a number of ATP analogues have been developed for this, their scope is restricted because of the limited acceptance by respective enzymes. In order to clarify which kind of phosphate-modified ATP analogues are accepted by the α-β-phosphoanhydride-cleaving ubiquitin-activating enzyme 1 (UBA1) and the β-γ-phosphoanhydride-cleaving focal adhesion kinase (FAK), we tested phosphoramidate- and phosphoester-modified ATP analogues. UBA1 and FAK were able to convert phosphoramidate-modified ATP analogues, even with a bulky modification like biotin. In contrast, a phosphoester-modified analogue was poorly accepted. These results demonstrate that minor variations in the design of ATP analogues for monitoring ATP utilization have a significant impact on enzymatic acceptance.

Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
Konferenz
Rezension
undefined / . - undefined, undefined
Zitieren
ISO 690ERMERT, Susanne, Stephan M. HACKER, Alexander BUNTRU, Martin SCHEFFNER, Christof R. HAUCK, Andreas MARX, 2017. Different Enzymatic Processing of γ-Phosphoramidate and γ-Phosphoester-Modified ATP Analogues. In: ChemBioChem. 2017, 18(4), pp. 378-381. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.201600590
BibTex
@article{Ermert2017-02-16Diffe-38686,
  year={2017},
  doi={10.1002/cbic.201600590},
  title={Different Enzymatic Processing of γ-Phosphoramidate and γ-Phosphoester-Modified ATP Analogues},
  number={4},
  volume={18},
  issn={1439-4227},
  journal={ChemBioChem},
  pages={378--381},
  author={Ermert, Susanne and Hacker, Stephan M. and Buntru, Alexander and Scheffner, Martin and Hauck, Christof R. and Marx, Andreas}
}
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/123456789/38686">
    <dc:contributor>Hacker, Stephan M.</dc:contributor>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dc:contributor>Scheffner, Martin</dc:contributor>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:contributor>Ermert, Susanne</dc:contributor>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/38686/1/Ermert_0-406367.pdf"/>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/38686/1/Ermert_0-406367.pdf"/>
    <dc:language>eng</dc:language>
    <dcterms:issued>2017-02-16</dcterms:issued>
    <dcterms:title>Different Enzymatic Processing of γ-Phosphoramidate and γ-Phosphoester-Modified ATP Analogues</dcterms:title>
    <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/38686"/>
    <dc:creator>Buntru, Alexander</dc:creator>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:contributor>Hauck, Christof R.</dc:contributor>
    <dc:creator>Hauck, Christof R.</dc:creator>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-05-02T09:55:03Z</dcterms:available>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:contributor>Marx, Andreas</dc:contributor>
    <dc:contributor>Buntru, Alexander</dc:contributor>
    <dc:creator>Ermert, Susanne</dc:creator>
    <dc:creator>Marx, Andreas</dc:creator>
    <dc:creator>Scheffner, Martin</dc:creator>
    <dcterms:abstract xml:lang="eng">Monitoring the activity of ATP-consuming enzymes provides the basis for elucidating their modes of action and regulation. Although a number of ATP analogues have been developed for this, their scope is restricted because of the limited acceptance by respective enzymes. In order to clarify which kind of phosphate-modified ATP analogues are accepted by the α-β-phosphoanhydride-cleaving ubiquitin-activating enzyme 1 (UBA1) and the β-γ-phosphoanhydride-cleaving focal adhesion kinase (FAK), we tested phosphoramidate- and phosphoester-modified ATP analogues. UBA1 and FAK were able to convert phosphoramidate-modified ATP analogues, even with a bulky modification like biotin. In contrast, a phosphoester-modified analogue was poorly accepted. These results demonstrate that minor variations in the design of ATP analogues for monitoring ATP utilization have a significant impact on enzymatic acceptance.</dcterms:abstract>
    <dc:creator>Hacker, Stephan M.</dc:creator>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-05-02T09:55:03Z</dc:date>
    <dc:rights>terms-of-use</dc:rights>
  </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
Ja
Begutachtet
Diese Publikation teilen