@article{Wenz1985Studi-7298,
  year={1985},
  title={Studies with general acyl-CoA dehydrogenase from pig kidney : inactivation by a novel type of "suicide" inhibitor, 3,4-pentadienoyl-CoA},
  number={3},
  volume={147},
  issn={0014-2956},
  journal={European Journal of Biochemistry},
  pages={553--560},
  author={Wenz, Alexandra and Ghisla, Sandro and Thorpe, Colin}
}

<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/123456789/7298">
    <dcterms:title>Studies with general acyl-CoA dehydrogenase from pig kidney : inactivation by a novel type of "suicide" inhibitor, 3,4-pentadienoyl-CoA</dcterms:title>
    <dc:contributor>Ghisla, Sandro</dc:contributor>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:33:20Z</dcterms:available>
    <dc:contributor>Thorpe, Colin</dc:contributor>
    <dcterms:abstract xml:lang="eng">3,4-Pentadienoyl-CoA, an allenic substrate analog, is a potent inhibitor of the flavoprotein pig-kidney general acyl-CoA dehydrogenase. The analog reacts very rapidly (k = 2.4 x 103 min -1) with the native oxidized enzyme to form a covalent flavin adduct probably involving the isoalloxazine position N-5. This species is inactive, but activity may be regained by two pathways. The allenic thioester can be displaced (k = 0.3 min - 1) by a large excess of octanoyl-CoA substrate upon reversal of covalent adduct formation. Alternatively, the enzyme inactivator adduct slowly decomposes (t 111 = 75 min) to form the strongly thermodynamically favoured 2,4-diene and catalytically active, oxidized enzyme. During this latter process 15-20% of the activity is irreversibly lost probably due to covalent modification of the protein. These data suggest that 3,4-pentadienoyl-CoA should be considered a suicide substrate of the acyl-CoA dehydrogenase. The mechanism of the reactions, and in particular the 3,4-&gt;2,4 tautomerization, are consistent with a catalytic sequence initiated by abstraction of an a-hydrogen as a proton.</dcterms:abstract>
    <dc:format>application/pdf</dc:format>
    <dc:contributor>Wenz, Alexandra</dc:contributor>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/7298/1/Studies_with_general_acyl_CoA_dehydrogenase_from_pig_kidney.pdf"/>
    <dc:creator>Ghisla, Sandro</dc:creator>
    <dcterms:issued>1985</dcterms:issued>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/7298/1/Studies_with_general_acyl_CoA_dehydrogenase_from_pig_kidney.pdf"/>
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:33:20Z</dc:date>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/7298"/>
    <dc:language>eng</dc:language>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <dc:creator>Wenz, Alexandra</dc:creator>
    <dcterms:bibliographicCitation>First publ. in: European Journal of Biochemistry 147 (1985), 3, pp. 553-560</dcterms:bibliographicCitation>
    <dc:creator>Thorpe, Colin</dc:creator>
  </rdf:Description>
</rdf:RDF>