Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.1.5 (neuropathy target esterase)
 1,070 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Phospholipase activities releasing fatty acyl moieties from phosphatidylcholine and phosphatidylethanolamine and lysophospholipase activity releasing fatty acid from lyso-phosphatidylcholine were detected in both Mycobacterium microti and Mycobacterium avium. Fatty acyl groups were released from both the 1- and 2-positions of phosphatidylcholine. Generally, phospholipase activities of M. avium were cryptic while phospholipase activities of M. microti were located on the bacterial surface. However, intact M. microti did not release fatty acids from phospholipids faster than M. avium. Neither Mycobacterium secreted acyl-hydrolysing phospholipase activity. All phospholipase activities were stimulated by including phospholipids in growth media: generally, cell extracts contained 6- to 15-fold higher specific activities than extracts from mycobacteria grown in media without added phospholipid. However, not all phospholipase activities were stimulated to the same degree in any given set of conditions, suggesting the existence of more than one phospholipase gene in each Mycobacterium.
J Gen Microbiol 1992 Apr
PMID:Control and location of acyl-hydrolysing phospholipase activity in pathogenic mycobacteria. 158 12

Lecithin-dependent haemolysin (LDH) of Vibrio parahaemolyticus was purified from Escherichia coli C600 transformed with a plasmid (pHL591) ligated with a 1.5 kb DNA fragment of V. parahaemolyticus. The final preparation comprised two LDH proteins with different molecular masses which were immunologically cross-reactive and had the same enzymic activity. The LDH was a phospholipase hydrolysing both fatty acid esters of phospholipid, i.e. it hydrolysed phosphatidylcholine (PC) to lysophosphatidylcholine (LPC) and then LPC to glycerophosphorylcholine (GPC). From this point of view, LDH should be classified as a phospholipase B. Phospholipase B, however, does not usually show haemolytic activity, because the intermediate (LPC), which is the actual haemolytic agent, is immediately hydrolysed to the final product (GPC). On the other hand, LPC formed by LDH action was comparatively stable, because the rates of the two reactions catalysed by LDH, PC to LPC and LPC to GPC, are almost the same. This is the reason that LDH shows haemolytic activity. Therefore, LDH of V. parahaemolyticus is an atypical phospholipase to be designated as phospholipase A2/lysophospholipase.
J Gen Microbiol 1991 Dec
PMID:Purification and characterization of a lecithin-dependent haemolysin from Escherichia coli transformed by a Vibrio parahaemolyticus gene. 179 26

Phospholipase A and lysophospholipase activities were measured in the culture fluid and in the blastospores of Candida albicans. When phospholipase activity was measured in six yeasts (four strains of C. albicans and a single strain each of Candida parapsilosis and Saccharomyces cerevisiae) a correlation was found between this activity and two potential parameters of pathogenicity. The C. albicans isolates which adhered most strongly to buccal epithelial cells and were most pathogenic in mice had the highest phospholipase activities. Non-pathogenic yeasts, including C. albicans isolates which did not adhere and did not kill mice, had lower phospholipase activities.
J Gen Microbiol 1985 May
PMID:A comparison of phospholipase activity, cellular adherence and pathogenicity of yeasts. 389 72

E. coli bearing hybrid plasmid pKOl (Oeda et al. (1981) Mol. Gen. Genet. 184, 191-199) expressed a large amount of lysophospholipase L2 activity. When a mutant which was defective in lysophospholipase L2 activity was transformed with plasmid pKOl, it overproduced lysophospholipase L2 activity. The gene responsible for the lysophospholipase L2 activity was designated as pld B. On the same hybrid plasmid another gene (pld A) coding for detergent-resistant phospholipase A (DR-phospholipase A) was also identified. These facts together with the results of a Pl transduction experiment revealed that the pld B gene must be between the pld A and met E genes on the E. coli chromosome.
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PMID:Identification and cloning of the gene coding for lysophospholipase L2 of E. coli K-12. 636 30

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 identified 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 pHMB or pCMPS, 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.
J Gen Microbiol 1984 Jun
PMID:Origin and fate of the lysophosphatidylethanolamine in a chain-forming mutant (envC) of Escherichia coli. 638 25