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Experimental evidence and theoretical considerations are presented which show that the pure enzyme with oxidoreductase activity for alicyclic ketones which was isolated from pig liver is a fatty acid synthetase. The enzyme exhibits fatty acid synthetase activity with the natural substrates, acetyl- and malonyl­CoA, and when incubated with 14C-labeled acetyl-CoA, yields [14C]-palmitate and [14C]stearate. The oxidoreductase activity for alicyclic ketones and the fatty acid synthetase activity of the enzyme could not be separated by chromatography on two different column materials. Kinetic data obtained with the model substrate, S-acetoacetyl-N-acetyl-cysteamine, as well as stereospecificity considerations support the view that it is the 3-oxoacylacyl-carrier protein reductase component of the fatty acid synthetase complex which is responsible for the oxidoreductase activity toward alicyclic ketones. [ABSTRACT FROM AUTHOR]