Suicide Substrates as Irreversible Inhibitors of Flavoenzymes

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1980
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Wenz, Alexandra
Thorpe, Colin
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Erschienen in
Enzyme Inhibitors : proceedings of a meeting held in Basel, on 20 and 21 March 1980 / Brodbeck, Urs (Hrsg.). - Weinheim : Verl. Chemie, 1980. - S. 43-60
Zusammenfassung
An increasing number of flavin dependent enzymes have recently been found to be inhibited by substrate analogs which fulfill the requirements set forth for suicide inhibitors. In most cases inactivation results from covalent modification of the flavin coenzyme; in other cases protein alkylation at the enzyme active center is involved. Examples of the first are the inactivation of general acylCoA dehydrogenase from pig kidney, and butyryl-CoA dehydrogenase from Megasphera elsdenii by a metabolite of the hypoglycaemic agent hypoglycin, and by 3,4-pentadienoyl-CoA; these are described in some detail. A survey of the suicide inhibitors investigated so far indicates that either an acetylenic, an allenic or the methylenecyclopropane moieties flanking the function to be oxidized, are required for suicide inactivation of flavin enzymes.
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570 Biowissenschaften, Biologie
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Zitieren
ISO 690GHISLA, Sandro, Alexandra WENZ, Colin THORPE, 1980. Suicide Substrates as Irreversible Inhibitors of Flavoenzymes. In: BRODBECK, Urs, ed.. Enzyme Inhibitors : proceedings of a meeting held in Basel, on 20 and 21 March 1980. Weinheim:Verl. Chemie, pp. 43-60
BibTex
@inproceedings{Ghisla1980Suici-7034,
  year={1980},
  title={Suicide Substrates as Irreversible Inhibitors of Flavoenzymes},
  publisher={Verl. Chemie},
  address={Weinheim},
  booktitle={Enzyme Inhibitors : proceedings of a meeting held in Basel, on 20 and 21 March 1980},
  pages={43--60},
  editor={Brodbeck, Urs},
  author={Ghisla, Sandro and Wenz, Alexandra and Thorpe, Colin}
}
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