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sphingomyelin/cereus
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Page 1 from 35 results
The binding and hydrolysis of sphingomyelin by phospholipase C (Bacillus cereus) as shown by 31P NMR.
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31P nuclear magnetic resonance studies showed that heavily inactivated phospholipase C (Bacillus cereus) initially caused line broadening in the 31P resonance from sphingomyelin thus indicating enzyme-lipid association. Using larger amounts of enzyme or longer preincubation caused a displacement of
Kinetic steps for the hydrolysis of sphingomyelin by Bacillus cereus sphingomyelinase in lipid monolayers.
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The sphingomyelinase (Sphmase) activity degrading sphingomyelin (Sphm) monolayers shows a slow-reaction latency period before exhibiting constant rate catalysis. These two kinetic regions are regulated independently by the lateral surface pressure and by lipids that are biomodulators of cell
Structural basis of the sphingomyelin phosphodiesterase activity in neutral sphingomyelinase from Bacillus cereus.
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Sphingomyelinase (SMase) from Bacillus cereus (Bc-SMase) hydrolyzes sphingomyelin to phosphocholine and ceramide in a divalent metal ion-dependent manner. Bc-SMase is a homologue of mammalian neutral SMase (nSMase) and mimics the actions of the endogenous mammalian nSMase in causing differentiation,
Processive interfacial catalytic turnover by Bacillus cereus sphingomyelinase on sphingomyelin vesicles.
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Sphingomyelinase (SMase), a water-soluble enzyme from Bacillus cereus, is shown to bind with high affinity to vesicles of sphingomyelin (SM) but not to vesicles of phosphatidylcholine (PC). The reaction progress by SMase bound to SM vesicles occurs in the scooting mode with virtually infinite
His151 and His296 are the acid-base catalytic residues of Bacillus cereus sphingomyelinase in sphingomyelin hydrolysis.
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Bacillus cereus sphingomyelinase belongs to the Mg(2+)-dependent neutral sphingomyelinase, which hydrolyses sphingomyelin to phosphocholine and ceramide, and acts as an extracellular hemolysin. The triplet residues, His151-Asp195-His296, of the enzyme are highly conserved among bacterial and
Structure-activity relationship of sphingomyelin analogs with sphingomyelinase from Bacillus cereus.
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The aim of this study was to examine how structural properties of different sphingomyelin (SM) analogs affected their substrate properties with sphingomyelinase (SMase) from Bacillus cereus. Using molecular docking and dynamics simulations (for SMase-SM complex), we then attempted to explain the
The hydrolysis of sphingomyelin by phospholipase C from Bacillus cereus.
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Action of phospholipase C (Bacillus cereus) on isolated myelin sheath preparations.
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The action of phospholipase C (Bacillus cereus) on the phospholipids of myelin sheath preparations has been investigated. With freshly isolated bovine brain myelin about 40% of the total phospholipid could be hydrolyzed by this enzyme. With bovine spinal cord myelin the phospholipid seemed more
Effect of Co2+-substitution on the substrate specificity of phospholipase C from Bacillus cereus during attack on two membrane systems.
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Phospholipid degradation by native phospholipase C from Bacillus cereus and enzyme forms where one or both of the Zn2+ prosthetic groups had been replaced with Co2+ was studied in human erythrocyte membranes (ghosts) and resuspended freeze-dried bovine brain myelin. The rate of total phospholipid
Studies on sphingomyelinase of Bacillus cereus. I. Purification and properties.
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A sphingomyelinase was purified 980-fold with recovery of 25.6% from the culture broth of Bacillus cereus, by (NH4)2SO4 precipitation and chromatography on CM-Sephadex, DEAE-cellulose and Sephadex G-75. The purified preparation was free of lipase, protease and other phospholipases. The enzyme
Effect of some divalent metal cations on phospholipase C from Bacillus cereus.
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Incubation of phospholipase C from Bacillus cereus with certain divalent metal cations caused enzyme inactivation with Cu(II) being particularly effective. The inactivation arose from the reversible exchange of Zn(II) in the enzyme with the metal cations. Both zinc atoms in the enzyme exchanged
Lysis of erythrocytes from stored human blood by phospholipase C (Bacillus cereus).
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The ability of phospholipase C (Bacillus cereus) to lyse erythrocytes from human blood that had been stored under Transfusion Service conditions for up to 16 weeks has been examined. When incubated at 20 degrees C with enzyme (0.03 mg/ml, 55 units/ml) for up to 1 h fresh erythrocytes were not lysed.
Increased arachidonic acid metabolites from cells in culture after treatment with the phosphatidylcholine-hydrolyzing phospholipase C from Bacillus cereus.
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Treatment of rat liver cells (the C-9 cell line), porcine aorta endothelial cells, bovine aorta smooth muscle cells, bovine aorta endothelial cells, mouse fibroblasts and rat keratinocytes with highly purified, crystallized Bacillus cereus phospholipase C, which hydrolyzes phosphatidylcholine,
Modulation of enzymatic activity and biological function of Listeria monocytogenes broad-range phospholipase C by amino acid substitutions and by replacement with the Bacillus cereus ortholog.
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The secreted broad-range phosphatidylcholine (PC)-preferring phospholipase C (PC-PLC) of Listeria monocytogenes plays a role in the bacterium's ability to escape from phagosomes and spread from cell to cell. Based on comparisons with two orthologs, Clostridium perfringens alpha-toxin and Bacillus
Nucleotide sequence and expression in Escherichia coli of the gene coding for sphingomyelinase of Bacillus cereus.
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Bacillus cereus secretes phospholipases C, which hydrolyze phosphatidylcholine, sphingomyelin and phosphatidylinositol. A 7.5-kb HindIII fragment of B. cereus DNA cloned into Escherichia coli, with pUC18 as a vector, directed the synthesis of the sphingomyelin-hydrolyzing phospholipase C,
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