Allicin, a naturally occurring antibiotic from garlic, specifically inhibits acetyl-CoA synthetase.
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.
Focke
M
M
Botanisches Institut der Universität Karlsruhe, FRG.
Feld
A
A
Lichtenthaler
K
K
D000106:Acetate-CoA Ligase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D000085:Acetates / Q000378:metabolism; D000818:Animals; D001419:Bacteria / Q000201:enzymology; D002417:Cattle; D002736:Chloroplasts / Q000201:enzymology; D003066:Coenzyme A Ligases / Q000037:antagonists & inhibitors*; D004220:Disulfides; D004305:Dose-Response Relationship, Drug; D005227:Fatty Acids / Q000096:biosynthesis; D009206:Myocardium / Q000201:enzymology; D013441:Sulfinic Acids / Q000378:metabolism / Q000494:pharmacology; D015003:Yeasts / Q000201:enzymology
D000085:Acetates; D004220:Disulfides; D005227:Fatty Acids; D013441:Sulfinic Acids; C006452:allicin; D003066:Coenzyme A Ligases; D000106:Acetate-CoA Ligase