The role of phospholipid metabolism in the functioning of the bacterial envelope was investigated in the chain-forming Lysophosphatidylethanolamine (LPE) which accumulated in this strain during growth was indentified as the product of phosphatidylethanolamine (PE) hydrolysis by a phospholipase A, i.e. 2-acylLPE. Isotopically labelled LPE transferred into intact mutant and parent cells by liposome/bacteria interaction was rapidly reacylated to PE. However, in the final PE/LPE ratio was lower than that in the parent, thus showing that the fate of LPE is modified. Crude cell extracts degraded LPE to a lesser extent in than in the parent but were unable to promote reacylation activity under our experimental conditions. In both strains, the lysophospholipase activity was neither calcium-dependent nor inhibited by the SH-group inhibitors HMB or CMPS, and hydrolysed 1-acylLPE as well as 2-acylLPE. These results indicate the existence of a deacylation-reacylation cycle in and show that this cycle is perturbed in cells, especially at the lysophospholipase step.


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