@article{mbs:/content/journal/micro/10.1099/00221287-130-6-1391, author = "Michel, G. P. F. and Starka, J.", title = "Origin and Fate of the Lysophosphatidylethanolamine in a Chain-forming Mutant (envC) of Escherichia coli", journal= "Microbiology", year = "1984", volume = "130", number = "6", pages = "1391-1398", doi = "https://doi.org/10.1099/00221287-130-6-1391", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-130-6-1391", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "The role of phospholipid metabolism in the functioning of the bacterial envelope was investigated in the chain-forming Escherichia coli envC. Lysophosphatidylethanolamine (LPE) which accumulated in this strain during growth was indentified as the product of phosphatidylethanolamine (PE) hydrolysis by a phospholipase A1, 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 envC 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 envC 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 p HMB or p CMPS, and hydrolysed 1-acylLPE as well as 2-acylLPE. These results indicate the existence of a deacylation-reacylation cycle in E. coli and show that this cycle is perturbed in envC cells, especially at the lysophospholipase step.", }