Publikation: Inactivation of General Acyl-CoA Dehydrogenase from Pig Kidney by a Metabolite of Hypoglycin A*
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1981
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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.
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570 Biowissenschaften, Biologie
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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. 9809-9812BibTex
@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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