Fatty Acid Degradation in <i>Escherichia coli</i>

Abstract

The properties of a transport system for the uptake of fatty acids into Escherichia coli cells are described. The system is induced under the same conditions as the enzymes involved in fatty acid degradation. In accordance with the chain‐length specificity of the acyl‐CoA synthetase, only fatty acids with more than eight carbon atoms are taken up. The reduced rate of uptake of fatty acids in mutants with various lesions in fatty acid degradation indicates that transport and metabolism are tightly coupled processes. The absence of an efflux reaction and the inability of a mutant lacking the acyl‐CoA synthetase to take up fatty acids support the hypothesis that this enzyme is involved in a vectorial acylation during the permeation process. Mutants lacking one or all of the enzymes enoyl‐CoA hydrase, β‐hydroxyacyl‐CoA dehydro‐genase and thiolase, when assayed with substrates having four carbon atoms, can partially degrade long‐chain length and medium‐chain length fatty acids. This suggests that there are at least two types of enzyme activity in the cell which differ in their specificities for acyl‐CoA substrates of various chain‐lengths. A new old locus situated between the genes proA and proB on the E. coli linkage group is described. Lesions in this gene make the cell unable to degrade fatty acids of any carbon number, and must therefore lack an element common to the degradation of all fatty acids. Fatty acids taken up by these mutants are exclusively incorporated into membrane phospholipids.