Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
Zur Ablage hinzufügen
  Lokale TagsFreigabegeschichteDetailsÜbersicht

Freigegeben
Zeitschriftenartikel

Interaction of long-chain acyl-CoA analogs with pig kidney general acyl-CoA dehydrogenase

MPG-Autoren
/persons/resource/persons197838

Wieland,  Theodor
Max Planck Institute for Medical Research, Max Planck Society;

Externe Ressourcen

https://febs.onlinelibrary.wiley.com/doi/epdf/10.1111/j.1432-1033.1981.tb06397.x
(beliebiger Volltext)

https://doi.org/10.1111/j.1432-1033.1981.tb06397.x
(beliebiger Volltext)

Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Thorpe, C., Ciardelli, T. L., Stewart, C. J., & Wieland, T. (1981). Interaction of long-chain acyl-CoA analogs with pig kidney general acyl-CoA dehydrogenase. European Journal of Biochemistry, 118(2), 279-282. doi:10.1111/j.1432-1033.1981.tb06397.x.


Zitierlink: https://hdl.handle.net/21.11116/0000-0004-C776-7
Zusammenfassung
The interaction of two long-chain acyl-CoA analogs with pig kidney general acyl-CoA dehydrogenase (EC 1.3.99,3) was examined. The effect of S-heptadecyl-CoA and heptadecan-2-onyl-dethio-CoA on the flavo-protein was observed spectrophotometrically using the flavin as an active-site probe. The S-heptadecyl thioether analog bound strongly to the enzyme (Kd = 17 nM) and was a powerful competitive inhibitor (Ki less than 40 nM). In contrast to the thioether analog, the dethiocarba derivative, heptadecan-2-onyl-dethio-CoA, was a substrate inthe standard assay system being dehydrogenated at about 60% of the rate shown by palmitoyl-CoA. These results support the proposal that alpha-carbanion formation is an early event in the dehydrogenation of acyl-CoA substrates.