FROM:
FEBS Lett 1990; 261 (1) Feb 12: 106–108
Focke M, Feld A, Lichtenthaler K
Botanisches Institut der Universitat Karlsruhe, FRG
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 M. Other
enzymes of the fatty acid synthesis sequence were not affected,
as was shown using precursors other than acetate.