Inactivation of General Acyl-CoA Dehydrogenase from Pig Kidney by a Metabolite of Hypoglycin A*

Wenz, Alexandra; Thorpe, Colin; Ghisla, Sandro

Inactivation of General Acyl-CoA Dehydrogenase from Pig Kidney by a Metabolite of Hypoglycin A*

Dateien

J_Biol_Chem_1981_WenzInactivation_of_general_acyl_CoA_dehydrogen.pdfGröße: 512.71 KBDownloads: 300

Datum

1981

Autor:innen

Wenz, Alexandra

Thorpe, Colin

Ghisla, Sandro

URI (zitierfähiger Link)

http://nbn-resolving.de/urn:nbn:de:bsz:352-opus-57301

Link zur Lizenz

Attribution-NonCommercial-NoDerivs 2.0 Generic

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Journal of Biological Chemistry. 1981, 256(19), pp. 9809-9812

Zusammenfassung

Pig kidney general acyl-CoA dehydrogenase is irreversibly inactivated by methylenecyclopropylacetyl-CoA, a metabolite of the hypoglycemic amino acid hypoglycin from Blighia sapida, to less that 2% of native activity. Octanoyl-CoA affords strong protection against this inhibition. During inactivation, about 80% of the enzyme FAD is covalently and irreversibly modified with the residual inhibition possibly resulting from modification of the protein. Denaturation of the inactivated enzyme yields several modified flavin derivatives in addition to about 20% unmodified FAD. From spectral comparison, the structure of one of these species is tentatively assigned to a derivative of 4a,5-dihydroflavin, while two further products resemble 6 -, and 8-substituted flavins. These results suggest that methylenecyclopropylacetyl-CoA (and consequently the methylenecyclopropylmethano moiety of hypoglycin) be considered "suicide" substrates.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

WENZ, Alexandra, Colin THORPE, Sandro GHISLA, 1981. Inactivation of General Acyl-CoA Dehydrogenase from Pig Kidney by a Metabolite of Hypoglycin A*. In: Journal of Biological Chemistry. 1981, 256(19), pp. 9809-9812

BibTex

@article{Wenz1981Inact-7964,
  year={1981},
  title={Inactivation of General Acyl-CoA Dehydrogenase from Pig Kidney by a Metabolite of Hypoglycin A*},
  number={19},
  volume={256},
  journal={Journal of Biological Chemistry},
  pages={9809--9812},
  author={Wenz, Alexandra and Thorpe, Colin and Ghisla, Sandro}
}

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    <dcterms:abstract xml:lang="eng">Pig kidney general acyl-CoA dehydrogenase is irreversibly inactivated by methylenecyclopropylacetyl-CoA, a metabolite of the hypoglycemic amino acid     hypoglycin from Blighia sapida, to less that 2% of native activity. Octanoyl-CoA affords strong protection against this inhibition. During inactivation, about 80% of the enzyme FAD is covalently and irreversibly modified with the residual inhibition possibly resulting from modification of the protein. Denaturation of the inactivated enzyme yields several modified flavin derivatives in addition to about 20% unmodified FAD. From spectral comparison, the structure of one of these species is tentatively assigned to a derivative of 4a,5-dihydroflavin, while two further products resemble 6 -, and 8-substituted flavins. These results suggest that methylenecyclopropylacetyl-CoA (and consequently the methylenecyclopropylmethano moiety of hypoglycin) be considered "suicide" substrates.</dcterms:abstract>
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Universitätsbibliographie

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