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Inhibition of fatty acid synthetase in Halobacterium cutirubrum and Escherichia coli by high salt concentrations.

A cell-free enzyme preparation from Halobacterium cutirubrum was shown to catalyze the biosynthesis of fatty acids from malonyl-CoA at zero sodium chloride concentration, with a specific activity about that of a similarly prepared fatty acid synthetase from E. coli. Both the H. cutirubrum synthetase and that from E. coli were strongly inhibited by high sodium chloride or potassium chloride concentrations (0.5–4 M). The malonyl-CoA: ACP transacylase, which catalyzes the first step in the fatty acid biosynthetic pathway, was shown to be strongly inhibited by salt in H. cutirubrum, but not in E. coli. It is concluded that H. cutirubrum contains a fatty acid synthetase system which normally operates at a very low level of activity as a result of inhibition by the high intracellular salt concentration present in this organism.