Publikation:

Studies on the reaction mechanism of general acyl-CoA dehydrogenase : determination of selective isotope effects in the dehydrogenation of butyryl-CoA

Lade...
Vorschaubild

Datum

1986

Autor:innen

Pohl, Brigitte
Raichle, Thomas

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

European Journal of Biochemistry. 1986, 160(1), pp. 109-115. ISSN 0014-2956. eISSN 1432-1033. Available under: doi: 10.1111/j.1432-1033.1986.tb09946.x

Zusammenfassung

The kinetic properties of general acyl-CoA dehydrogenase from pig kidney have been investigated using normal butyryl-CoA as well as a α-deutero, β-deutero-and perdeutero-butyryl-CoA. In turnover catalysis, isotope effects of 2, 3.6, and 9 were found respectively. In the reductive half reaction the isotope effects were 2.5, 14, and 28 for the same substrates, and 21 for (2R,3R)-(2,3-D2)butyryl-CoA. No intermediates are apparent during the reduction of oxidized enzyme to the presumed complex of reduced enzyme and crotonyl-CoA. The results are interpreted as indicating a high degree of concertedness during the rupture of the α and β C-H bonds. They are compatible with a mechanism in which simultaneously the α-hydrogen is abstracted as a proton, while the β-hydrogen is transferred to the oxidized flavin as a hydride.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
570 Biowissenschaften, Biologie

Schlagwörter

Konferenz

Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Zugehörige Datensätze in KOPS

Zitieren

ISO 690POHL, Brigitte, Thomas RAICHLE, Sandro GHISLA, 1986. Studies on the reaction mechanism of general acyl-CoA dehydrogenase : determination of selective isotope effects in the dehydrogenation of butyryl-CoA. In: European Journal of Biochemistry. 1986, 160(1), pp. 109-115. ISSN 0014-2956. eISSN 1432-1033. Available under: doi: 10.1111/j.1432-1033.1986.tb09946.x
BibTex
@article{Pohl1986Studi-7325,
  year={1986},
  doi={10.1111/j.1432-1033.1986.tb09946.x},
  title={Studies on the reaction mechanism of general acyl-CoA dehydrogenase : determination of selective isotope effects in the dehydrogenation of butyryl-CoA},
  number={1},
  volume={160},
  issn={0014-2956},
  journal={European Journal of Biochemistry},
  pages={109--115},
  author={Pohl, Brigitte and Raichle, Thomas 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/123456789/7325">
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:33:33Z</dcterms:available>
    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <dcterms:issued>1986</dcterms:issued>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/7325/1/Studies_on_the_reaction_mechanism_of_general_acyl_CoA_dehydrogenase.pdf"/>
    <dc:contributor>Pohl, Brigitte</dc:contributor>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/>
    <dc:format>application/pdf</dc:format>
    <dc:contributor>Ghisla, Sandro</dc:contributor>
    <dc:creator>Raichle, Thomas</dc:creator>
    <dc:creator>Pohl, Brigitte</dc:creator>
    <dc:language>eng</dc:language>
    <dcterms:abstract xml:lang="eng">The kinetic properties of general acyl-CoA dehydrogenase from pig kidney have been investigated using normal butyryl-CoA as well as a α-deutero, β-deutero-and perdeutero-butyryl-CoA. In turnover catalysis, isotope effects of 2, 3.6, and 9 were found respectively. In the reductive half reaction the isotope effects were 2.5, 14, and 28 for the same substrates, and 21 for (2R,3R)-(2,3-D2)butyryl-CoA. No intermediates are apparent during the reduction of oxidized enzyme to the presumed complex of reduced enzyme and crotonyl-CoA. The results are interpreted as indicating a high degree of concertedness during the rupture of the α and β C-H bonds. They are compatible with a mechanism in which simultaneously the α-hydrogen is abstracted as a proton, while the β-hydrogen is transferred to the oxidized flavin as a hydride.</dcterms:abstract>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/7325/1/Studies_on_the_reaction_mechanism_of_general_acyl_CoA_dehydrogenase.pdf"/>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:title>Studies on the reaction mechanism of general acyl-CoA dehydrogenase : determination of selective isotope effects in the dehydrogenation of butyryl-CoA</dcterms:title>
    <dc:creator>Ghisla, Sandro</dc:creator>
    <dc:contributor>Raichle, Thomas</dc:contributor>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/7325"/>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:33:33Z</dc:date>
    <dcterms:bibliographicCitation>First publ. in: European Journal of Biochemistry 160 (1986), 1, pp. 109-115</dcterms:bibliographicCitation>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
  </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