The Effect of Palmityl Coenzyme A on Pigeon Liver Fatty Acid Synthetase

Activation of yeast pyruvate carboxylase: interactions between acyl coenzyme A compounds, aspartate, and substrates of the reaction

“…acyl-CoAs (for example, palmitoyl-CoA). Palmitoyl-CoA is widely accepted as an inactivator of many enzymes (Taketa & Pogell, 1966;Dorsey & Porter, 1968), and in at least one other case [microsomal glucose-6-phosphatase (Nordlie et al, 1967)] palmitoyl-CoA has been shown to be an activator of its phosphotransferase activity. In most of these instances it is strongly suspected that the mechanism of action is nonspecific and due to the detergent-like action of the acyl moiety.…”

Participation of covalently linked fatty acryl coenzyme A products in the action of yeast fatty acid synthetase

“…The inhibition is considerably diminished by serum albumin, indicating a nonspecific binding phenomenon (Lust and Lynen, 1968). Dorsey and Porter (1968) report inhibition of the fatty acid synthetase complex of pigeon liver by palmityl-CoA due to its detergentlike action. They were, however, unable to detect any covalent binding of palmityl residue to the enzyme.…”

Specificity of long-chain acyl coenzyme A synthetase from rat liver microsomes. Influence of the position of double bonds in octadecadienoic acids

“…The critical micellar concentrations (cmc) of fatty acid salts and acyl-CoA have been studied by different authors (Corrin et al, 1946;Sakharova and Shutova, 1964;Lhomar and Tookey, 1959;Zahler et al, 1968). Although there are some differences in the value reported because of differences in assay systems, the cmc of most long-chain fatty acids range from 100 µ to 10 mM and that of palmityl-CoA is about 2 to 5 µ (Zahler et al, 1968;Dorsey and Porter, 1968). Therefore most of the studies on acyl-CoA synthetase, which were based on the methods cited above, have been done with substrate concentrations above their cmc.…”