Abstract
The allenic substrate analogue, 2,3-decadienoyl- N-acetylcys teamine, and free 2,3-decadienoic acid were previously shown to inhibit β-hydroxydecanoyl thioester dehydrase irreversibly. Racemic 2,3-decadienoic acid has now been resolved via its amphetamine salts. The dextrorotatory isomer is found to be twice as potent an inhibitor as the racemic acid, while the levorotatory allene affects enzyme activity only slightly. A series of inhibitors varying in the length of the acyl chain (C 8C 14) has been prepared. Enzyme inactivation occurs most rapidly with the C 10-congener of the acetylenic and allenic thioesters, while the C 12 homologue is the most potent of the free allenic acid inhibitors.
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