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FEBS Lett ; 261(1): 106-8, 1990 Feb 12.
Article in English | MEDLINE | ID: mdl-1968399

ABSTRACT

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.


Subject(s)
Acetate-CoA Ligase/antagonists & inhibitors , Coenzyme A Ligases/antagonists & inhibitors , Acetate-CoA Ligase/metabolism , Acetates/metabolism , Animals , Bacteria/enzymology , Cattle , Chloroplasts/enzymology , Disulfides , Dose-Response Relationship, Drug , Fatty Acids/biosynthesis , Myocardium/enzymology , Sulfinic Acids/metabolism , Sulfinic Acids/pharmacology , Yeasts/enzymology
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