Aromatization of Cyclohexanecarboxylic Acid

From the ¹ From The James Bryant Conant Laboratory, Department of Chemistry, Harvard University, Cambridge, Massachusetts 02138

An enzyme which catalyzes the aromatization of cyclohexanecarboxyl coenzyme A has been isolated from whole liver as well as from liver mitochondria. Incubation of the soluble, partially purified enzyme with cyclohexanecarboxyl-CoA produces cyclohexene-1-carboxyl-CoA, benzoyl-CoA, and a polar compound which has not been further characterized.

All three isomers of cyclohexenecarboxyl-CoA are converted to benzoyl-CoA by the liver enzyme, but evidence is presented indicating that only cyclohexene-1-carboxyl-CoA lies on the path from cyclohexanecarboxyl-CoA to benzoyl-CoA.

Aromatization takes place either in air or anaerobically in the presence of artificial electron acceptors. The enzyme system is inactivated by low pH and activity is restored by the addition of flavin adenine dinucleotide.

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