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FEBS Lett ; 261(1): 106-8, 1990 Feb 12.
Artículo en Inglés | MEDLINE | ID: mdl-1968399

RESUMEN

Allicin is shown to be a specific inhibitor of the acetyl-CoA synthetases from plants, yeast and mammals. The bacterial acetyl-CoA-forming system, consisting of acetate kinase and phosphotransacetylase, was inhibited too. Non-specific interaction with sulfhydryl-groups could be excluded in experiments with dithioerythritol and p-hydroxymercuribenzoate. Binding of allicin to the enzyme is non-covalent and reversible. [14C]-Acetate incorporation into fatty acids of isolated plastids was inhibited by allicin with an I50-value lower than 10 microM. Other enzymes of the fatty acid synthesis sequence were not affected, as was shown using precursors other than acetate.


Asunto(s)
Acetato CoA Ligasa/antagonistas & inhibidores , Coenzima A Ligasas/antagonistas & inhibidores , Acetato CoA Ligasa/metabolismo , Acetatos/metabolismo , Animales , Bacterias/enzimología , Bovinos , Cloroplastos/enzimología , Disulfuros , Relación Dosis-Respuesta a Droga , Ácidos Grasos/biosíntesis , Miocardio/enzimología , Ácidos Sulfínicos/metabolismo , Ácidos Sulfínicos/farmacología , Levaduras/enzimología
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