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)

The cell envelope of Neisseria gonorrhoeae, colony type 4, was studied. Outer membrane was isolated by lysozyme and ethylenediaminetetraacetic acid treatment of plasmolyzed cells according to Wolf-Watz et al. (1973). The degree of purity of the membrane preparations was checked by electron microscopy. The membrane fraction obtained had a density of 1.25 g/cm(3), was rich in phospholipase A and lysophospholipase, and contained only 10% of the total membrane activity of succinate dehydrogenase and d-lactate dehydrogenase. The outer membrane protein profile after sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed at least six major proteins. The predominating protein showed a molecular weight of 35,000. The lipopolysaccharide component was characterized by gas chromatography. The carbohydrates found were galactose, glucose, and glucosamine. d-Glycero-l-manno-heptose was present in very low amounts. Lipid A contained lauric acid, stearic acid, and beta-hydroxy-myristic acid. About 20% of the fatty acids in the outer membrane was derived from lipid A. The phospholipids were characterized as phosphatidylethanolamine, phosphatidylglycerol, and diphosphatidylglycerol. There was no evidence for a lipoprotein anchored to the peptidoglycan. The peptidoglycan of N. gonorrhoeae was of the chemotype I. The cell envelope of N. gonorrhoeae was found to be highly permeable to gentian violet. Cell envelopes of one penicillin-resistant and two penicillin-sensitive strains were compared. Only moderate differences in fatty acid composition were found.
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PMID:Cell envelope of Neisseria gonorrhoeae: outer membrane and peptidoglycan composition of penicillin-sensitive and-resistant strains. 80 26

Lysophospholipase activity in brain subcellular fractions was measured by the release of myristic acid from 1-myristoylglycerophosphocholine or through the formation of [32P]glycerophosphocholine from [32P]lysophosphatidylcholine. Although the lysophospholipase activity was highest in microsomes, considerable enzyme activity was also found in other subcellular membrane fractions. The pH optimum for the microsomal enzyme was around 7, whereas the synaptosomes and non-synaptic plasma membranes exhibited a pH maximum around 8. Although the enzyme did not require divalent cations for activity, divalent cations (1 mM) such as Hg2+, Cu2+, and Zn2+ inhibited potently the enzyme activity. Enzyme activity was also partially inhibited by both saturated and polyunsaturated fatty acids (25-200 microM), and the inhibition seemed to be greater in the membrane than in the cytosolic fractions. Ionic detergents such as deoxycholate and taurocholate inhibited the lysophospholipase. On the other hand, the effect of Triton X-100 was biphasic, i.e., stimulation at concentrations below 100 micrograms/mg protein and inhibition at higher concentrations. Addition of cholesterol (50-250 micrograms/ml), but not cholesteryl esters, also potently inhibited enzyme activity. The presence of active lysophospholipase(s) in brain is probably an important mechanism for preventing unnecessary accumulation of lysophospholipids which may exert a deleterious effect on the membranes because of their detergent properties.
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PMID:Lysophospholipase activity in rat brain subcellular fractions. 358 3