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evolution
the enzyme belongs to a distinct zinc metallophospholipase C family present in bacteria and fungi
evolution
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the enzyme belongs to the plant non-specific phospholipase C gene family, phylogenetic tree, overview. The common ancestor of all seed plants already had at least one NPC1-, NPC2- and NPC6-like gene. Non-specific phospholipases C are a distinct type of plant phospholipid-cleaving enzyme homologous to bacterial phosphatidylcholine-specific phospholipases C
evolution
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the enzyme belongs to the plant non-specific phospholipase C gene family, phylogenetic tree, overview. The common ancestor of all seed plants already had at least one NPC1-, NPC2- and NPC6-like gene. Non-specific phospholipases C are a distinct type of plant phospholipid-cleaving enzyme homologous to bacterial phosphatidylcholine-specific phospholipases C
evolution
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the enzyme belongs to the plant non-specific phospholipase C gene family, phylogenetic tree, overview. The common ancestor of all seed plants already had at least one NPC1-, NPC2- and NPC6-like gene. Non-specific phospholipases C are a distinct type of plant phospholipid-cleaving enzyme homologous to bacterial phosphatidylcholine-specific phospholipases C
evolution
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the enzyme belongs to the plant non-specific phospholipase C gene family, phylogenetic tree, overview. The common ancestor of all seed plants already had at least one NPC1-, NPC2- and NPC6-like gene. Non-specific phospholipases C are a distinct type of plant phospholipid-cleaving enzyme homologous to bacterial phosphatidylcholine-specific phospholipases C
evolution
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the enzyme belongs to the plant non-specific phospholipase C gene family, phylogenetic tree, overview. The common ancestor of all seed plants already had at least one NPC1-, NPC2- and NPC6-like gene. Non-specific phospholipases C are a distinct type of plant phospholipid-cleaving enzyme homologous to bacterial phosphatidylcholine-specific phospholipases C
evolution
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the enzyme belongs to the plant non-specific phospholipase C gene family, phylogenetic tree, overview. The common ancestor of all seed plants already had at least one NPC1-, NPC2- and NPC6-like gene. Non-specific phospholipases C are a distinct type of plant phospholipid-cleaving enzyme homologous to bacterial phosphatidylcholine-specific phospholipases C
evolution
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the enzyme belongs to the plant non-specific phospholipase C gene family, phylogenetic tree, overview. The common ancestor of all seed plants already had at least one NPC1-, NPC2- and NPC6-like gene. Non-specific phospholipases C are a distinct type of plant phospholipid-cleaving enzyme homologous to bacterial phosphatidylcholine-specific phospholipases C
evolution
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the enzyme belongs to the plant non-specific phospholipase C gene family, phylogenetic tree, overview. The common ancestor of all seed plants already had at least one NPC1-, NPC2- and NPC6-like gene. Non-specific phospholipases C are a distinct type of plant phospholipid-cleaving enzyme homologous to bacterial phosphatidylcholine-specific phospholipases C
evolution
-
the enzyme belongs to the plant non-specific phospholipase C gene family, phylogenetic tree, overview. The common ancestor of all seed plants already had at least one NPC1-, NPC2- and NPC6-like gene. Non-specific phospholipases C are a distinct type of plant phospholipid-cleaving enzyme homologous to bacterial phosphatidylcholine-specific phospholipases C
evolution
-
the enzyme belongs to the plant non-specific phospholipase C gene family, phylogenetic tree, overview. The common ancestor of all seed plants already had at least one NPC1-, NPC2- and NPC6-like gene. Non-specific phospholipases C are a distinct type of plant phospholipid-cleaving enzyme homologous to bacterial phosphatidylcholine-specific phospholipases C
evolution
the enzyme belongs to the plant non-specific phospholipase C gene family, phylogenetic tree, overview. The common ancestor of all seed plants already had at least one NPC1-, NPC2- and NPC6-like gene. Non-specific phospholipases C are a distinct type of plant phospholipid-cleaving enzyme homologous to bacterial phosphatidylcholine-specific phospholipases C
evolution
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the enzyme is a the member of phospholipase C family
evolution
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the enzyme belongs to a distinct zinc metallophospholipase C family present in bacteria and fungi
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malfunction
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compared to wild-type, T-DNA insertional knockouts npc3 and npc4 show shorter primary roots and lower lateral root density at low brassinolide concentrations but increased lateral root densities in response to exogenous 0.05-1.0 mM brassinolide
malfunction
NPC4 knockout plants show increased sensitivity to salinity as compared with wild-type plants. Under salt stress npc4 plants have shorter roots, lower fresh weight, and reduced seed germination
malfunction
enzyme knock-out mutants of PlcC show abolished enzyme activity. Complementation of plcC knock-out mutants with wild-type plcC in trans restores the cell-associated enzyme activity defect
malfunction
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inhibition of the enzyme abrogates the Yersinia pseudotuberculosis-induced repression of caspase 3 activity
malfunction
npc4 knockout mutants are characterised by a reduced germination rate when sown on media containing 150 mM NaCl. Mutant npc4 plants also have reduced germination and overall viability under salt and drought stress conditions. Unlike wild-type plants, mutants overexpressing NPC4 are characterised by a higher germination level and maintain a greater root length and dry weight under both salt stress and hyperosmosis
malfunction
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the N-terminal domain of a-toxin retains PC-PLC activity when expressed in Escherichia coli, but lacks haemolytic and sphingomyelinase activities that are supposedly granted by a lipoxygenase-like C-terminal domain
malfunction
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enzyme knock-out mutants of PlcC show abolished enzyme activity. Complementation of plcC knock-out mutants with wild-type plcC in trans restores the cell-associated enzyme activity defect
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malfunction
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NPC4 knockout plants show increased sensitivity to salinity as compared with wild-type plants. Under salt stress npc4 plants have shorter roots, lower fresh weight, and reduced seed germination
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metabolism
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membrane lipid formation, turnover, and recycling in Sinorhizobium meliloti, overview
metabolism
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(S)-3-methyl-2-phenyl-N-(1-phenylpropyl)-4-quinolinecarboxamide activates TRP-like ion channels through an phosphatidylcholine-specific phospholipase C-dependent signaling pathway, mechanism, overview
metabolism
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model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
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model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
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model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
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model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
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model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
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model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
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model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
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model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
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model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
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model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
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protein kinase C and phosphatidylcholine-specific phospholipase C, but not tyrosine kinases or phosphatidylinositol-specific phospholipase C are key players in this dual polymorphonuclear leukocyte response to bacterial infection, e.g. by Yersinia pseudotuberculosis, Escherichia coli, or Staphylococcus aureus, and by pro-inflammatory cytokine production including interleukin-8 and tumor necrosis factor-alpha
metabolism
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the enzyme acts as a negative regulator in abscisic acid and brassinolide signaling pathways
physiological function
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alpha-toxin inhibits the expression of tumor necrosis factor-alpha and an inducible type of NO synthase protein and mRNA. It inhibits the phosphorylation of IkappaB-alpha and p65 NF-kappaB subunit, and the NF-kappaB luciferase reporter gene activity in lipopolysaccharide-stimulated RAW 264.7 cells. Pretreatment of alpha-toxin increases the level of intracellular ceramide. Treatment with alpha-toxin alone leads to the phosphorylation of mitogen-activated protein kinases
physiological function
PLC activity from eggs contributes to Chaetopterus egg activation and PLCgamma may play an important role during this biological process
physiological function
PLCbeta is probably not involved in egg activation
physiological function
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a phospholipase C activity, which appears to be specific for phosphatidic acid, is associated with the nicotinic acetylcholine receptor. The acetylcholine receptor may directly or indirectly influence lipid metabolism in a manner that enhances its own function
physiological function
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alpha-toxin, a major determinant of Clostridium perfringens toxicity, exhibits both phospholipase C and sphingomyelinase, EC 3.1.4.12, activities with distinct, but partially overlapping and interacting active sites
physiological function
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at least one PC-PLC is a plant signaling enzyme in brassinolide signal transduction and, as shown earlier, in elicitor signal transduction
physiological function
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PC-PLC is an important enzyme that plays a key role in a variety of cellular events and lipid homoeostases
physiological function
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phosphatidylcholine-specific phospholipase C is the major enzyme in the phosphatidylcholine cycle and is involved in many long-term cellular responses such as activation, proliferation, and differentiation events. Functional roles of PC-PLC and Cdc20 in the cell cycle, mitosis, and apoptosis in CBRH-7919 cancer cells. PC-PLC is involved in cell proliferation
physiological function
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PLC activation initiates the calcium signaling system. Phospholipase C activity is necessary for methylmercury-induced interleukin-6 release. Sustained interleukin-6 exposure can be detrimental to cerebellar granule neurons, one of the major cellular targets of methylmercury cytotoxicity
physiological function
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the enzyme can degrade endogenous preexisting membrane phospholipids as a source of phosphorus
physiological function
the enzyme reacts to environmental stresses such as phosphate deficiency and aluminium toxicity, and has a role in root development and brassinolide signalling, role for NPC4 in the response of Arabidopsis to salt stress, overview
physiological function
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the lipase activity serves the bacteriumto generate lipid signals in the host eukaryotic cell, and ultimately to degrade the host cellmembranes, and is the main virulence factor for gas gangrene in humans
physiological function
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brain phospholipase C is involved in (+/-)-epibatidine-induced activation of central adrenomedullary outflow in rats, overview. (+/-)-epibatidine activates spinally projecting neurons expressing monoacylglycerol lipase in the rat hypothalamic paraventricular nucleus, a control center of central sympatho-adrenomedullary outflow
physiological function
NPC3 might play a rolei in thermotolerance. The enzyme is responsible for lipid conversion during phosphate-limiting conditions. Two articles non-specific phospholipases C are involved in biotic and abiotic stress responses as well as phytohormone actions. The diacylglycerol produced via the enzymes is postulated to participate in membrane remodelling, general lipid metabolism and cross-talk with other phospholipid signalling systems in plants. Mode of action of the enzyme in lipid metabolism, signal transduction, and membrane remodelling, detailed overview, inducible expression and putative signalling role
physiological function
NPC4 participates in triggering plant salt stress responses likely via abscisic acid-dependent mechanisms. The enzyme is responsible for lipid conversion during phosphate-limiting conditions. Two articles non-specific phospholipases C are involved in biotic and abiotic stress responses as well as phytohormone actions. The diacylglycerol produced via the enzymes is postulated to participate in membrane remodelling, general lipid metabolism and cross-talk with other phospholipid signalling systems in plants. Mode of action of the enzyme in lipid metabolism, signal transduction, and membrane remodelling, detailed overview, inducible expression and putative signalling role
physiological function
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the enzyme inhibits the formation of cAMP by adenylate cyclase and is involved in the defence mechanism of bacteria to phagocytosis
physiological function
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the enzyme is involved in PC-PLC-medicated neuronal differentiation of bone marrow stromal cells, and heat shock protein 70 is the pivotal factor by blocking phospholipase C inhibitor D609-induced increase of transcription factor B-cell translocation gene 2 expression and cholinergic neuronal differentiation of bone marrow stromal cells, overview
physiological function
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the enzyme is involved in the regulation of Ca2+-permeable nonselective cation channels. (S)-3-methyl-2-phenyl-N-(1-phenylpropyl)-4-quinolinecarboxamide-induced current is mediated by the enzyme in neuronal nitric oxide synthase-expressing, GFP-responsive GABAergic neurons of the visual neocortex. (S)-3-methyl-2-phenyl-N-(1-phenylpropyl)-4-quinolinecarboxamide-induced current is mediated by G proteins and suppressed by D609, an inhibitor of phosphatidylcholine-specific phospholipase C, but not by inhibitors of phosphatidylinositol-specific phospholipase C, EC 3.1.4.11, adenylate cyclase or Src tyrosine kinases
physiological function
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the enzyme is responsible for lipid conversion during phosphate-limiting conditions. Non-specific phospholipases C are involved in biotic and abiotic stress responses as well as phytohormone actions. The diacylglycerol produced via the enzymes is postulated to participate in membrane remodelling, general lipid metabolism and cross-talk with other phospholipid signalling systems in plants. Mode of action of the enzyme in lipid metabolism, signal transduction, and membrane remodelling, detailed overview
physiological function
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the enzyme is responsible for lipid conversion during phosphate-limiting conditions. Non-specific phospholipases C are involved in biotic and abiotic stress responses as well as phytohormone actions. The diacylglycerol produced via the enzymes is postulated to participate in membrane remodelling, general lipid metabolism and cross-talk with other phospholipid signalling systems in plants. Mode of action of the enzyme in lipid metabolism, signal transduction, and membrane remodelling, detailed overview
physiological function
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the enzyme is responsible for lipid conversion during phosphate-limiting conditions. Non-specific phospholipases C are involved in biotic and abiotic stress responses as well as phytohormone actions. The diacylglycerol produced via the enzymes is postulated to participate in membrane remodelling, general lipid metabolism and cross-talk with other phospholipid signalling systems in plants. Mode of action of the enzyme in lipid metabolism, signal transduction, and membrane remodelling, detailed overview
physiological function
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the enzyme is responsible for lipid conversion during phosphate-limiting conditions. Non-specific phospholipases C are involved in biotic and abiotic stress responses as well as phytohormone actions. The diacylglycerol produced via the enzymes is postulated to participate in membrane remodelling, general lipid metabolism and cross-talk with other phospholipid signalling systems in plants. Mode of action of the enzyme in lipid metabolism, signal transduction, and membrane remodelling, detailed overview
physiological function
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the enzyme is responsible for lipid conversion during phosphate-limiting conditions. Non-specific phospholipases C are involved in biotic and abiotic stress responses as well as phytohormone actions. The diacylglycerol produced via the enzymes is postulated to participate in membrane remodelling, general lipid metabolism and cross-talk with other phospholipid signalling systems in plants. Mode of action of the enzyme in lipid metabolism, signal transduction, and membrane remodelling, detailed overview
physiological function
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the enzyme is responsible for lipid conversion during phosphate-limiting conditions. Non-specific phospholipases C are involved in biotic and abiotic stress responses as well as phytohormone actions. The diacylglycerol produced via the enzymes is postulated to participate in membrane remodelling, general lipid metabolism and cross-talk with other phospholipid signalling systems in plants. Mode of action of the enzyme in lipid metabolism, signal transduction, and membrane remodelling, detailed overview
physiological function
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the enzyme is responsible for lipid conversion during phosphate-limiting conditions. Non-specific phospholipases C are involved in biotic and abiotic stress responses as well as phytohormone actions. The diacylglycerol produced via the enzymes is postulated to participate in membrane remodelling, general lipid metabolism and cross-talk with other phospholipid signalling systems in plants. Mode of action of the enzyme in lipid metabolism, signal transduction, and membrane remodelling, detailed overview
physiological function
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the enzyme is responsible for lipid conversion during phosphate-limiting conditions. Non-specific phospholipases C are involved in biotic and abiotic stress responses as well as phytohormone actions. The diacylglycerol produced via the enzymes is postulated to participate in membrane remodelling, general lipid metabolism and cross-talk with other phospholipid signalling systems in plants. Mode of action of the enzyme in lipid metabolism, signal transduction, and membrane remodelling, detailed overview
physiological function
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the enzyme is responsible for lipid conversion during phosphate-limiting conditions. Non-specific phospholipases C are involved in biotic and abiotic stress responses as well as phytohormone actions. The diacylglycerol produced via the enzymes is postulated to participate in membrane remodelling, general lipid metabolism and cross-talk with other phospholipid signalling systems in plants. Mode of action of the enzyme in lipid metabolism, signal transduction, and membrane remodelling, detailed overview
physiological function
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the enzyme is responsible for lipid conversion during phosphate-limiting conditions. Two articles non-specific phospholipases C are involved in biotic and abiotic stress responses as well as phytohormone actions. The diacylglycerol produced via the enzymes is postulated to participate in membrane remodelling, general lipid metabolism and cross-talk with other phospholipid signalling systems in plants. Mode of action of the enzyme in lipid metabolism, signal transduction, and membrane remodelling, detailed overview
physiological function
the enzyme is responsible for lipid conversion during phosphate-limiting conditions. Two articles non-specific phospholipases C are involved in biotic and abiotic stress responses as well as phytohormone actions. The diacylglycerol produced via the enzymes is postulated to participate in membrane remodelling, general lipid metabolism and cross-talk with other phospholipid signalling systems in plants. Mode of action of the enzyme in lipid metabolism, signal transduction, and membrane remodelling, detailed overview
physiological function
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the enzyme plays an important role in sustained hypoxic pulmonary vasoconstriction possibly through the activation of protein kinase C-independent mechanism, which may be coupled with phosphocholine release. Phosphocholine induces sustained contraction in isolated intrapulmonary arteries and also transient pulmonary and systemic hypertension if administered intravenously
physiological function
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the enzyme signaling is required for polymorphonuclear leukocyte survival after bacterial infection and Toll-like receptor-mediated induction of interleukin-8 and TNFalpha gene expression. The enzyme activity is involved in bacteria-mediated suppression of caspase 3 activity
physiological function
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the enzyme's end-product 1,2-sn-diacylglycerol has an important effect on the bilayer architecture of the lipid membranes/lipid vesicles
physiological function
the enzyme, phosphatidylcholine-specific phospholipase C or effector PlcC/CegC1, together with Zn2+-dependent enzymes PlcA and PlcB, exhibiting phosphatidylglycerol hydrolysis activity, promote virulence, e.g. in Acanthamoeba castellanii amoebae and human U937 cells or in Galleria mellonella larvae, but are not essential. The enzyme is CpxR-co-regulated
physiological function
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the secreted enzyme plays a role in the aggregation of blood platelets and inhibits defensive superoxide generation in human polymorphonuclear leukocytes by interacting with membrane components of NADPH oxidase
physiological function
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isoforms PLC1 and PLC2 play a concerted role in hemolytic and cytolytic activities although isoform PLC1 plays a more critical role in the virulence of Acinetobacter baumannii
physiological function
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the enzyme, phosphatidylcholine-specific phospholipase C or effector PlcC/CegC1, together with Zn2+-dependent enzymes PlcA and PlcB, exhibiting phosphatidylglycerol hydrolysis activity, promote virulence, e.g. in Acanthamoeba castellanii amoebae and human U937 cells or in Galleria mellonella larvae, but are not essential. The enzyme is CpxR-co-regulated
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physiological function
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the enzyme reacts to environmental stresses such as phosphate deficiency and aluminium toxicity, and has a role in root development and brassinolide signalling, role for NPC4 in the response of Arabidopsis to salt stress, overview
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physiological function
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PLC activation initiates the calcium signaling system. Phospholipase C activity is necessary for methylmercury-induced interleukin-6 release. Sustained interleukin-6 exposure can be detrimental to cerebellar granule neurons, one of the major cellular targets of methylmercury cytotoxicity
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physiological function
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isoforms PLC1 and PLC2 play a concerted role in hemolytic and cytolytic activities although isoform PLC1 plays a more critical role in the virulence of Acinetobacter baumannii
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physiological function
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alpha-toxin, a major determinant of Clostridium perfringens toxicity, exhibits both phospholipase C and sphingomyelinase, EC 3.1.4.12, activities with distinct, but partially overlapping and interacting active sites
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physiological function
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the lipase activity serves the bacteriumto generate lipid signals in the host eukaryotic cell, and ultimately to degrade the host cellmembranes, and is the main virulence factor for gas gangrene in humans
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additional information
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establishing enzyme activity in lipid vesicles, method development, overview. Both lipase activities are sensitive to vesicle size, but in opposite ways: while phospholipase C is higher with larger vesicles, sphingomyelinase activity is lower
additional information
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PC-PLC maturation between bacterial plasma membrane and bacterial cell wall, translocation across the bacterial cell wall, and activity in the host cell, schematic overview. The N-terminus of the PC-PLC propeptide regulates the compartmentalization of PC-PLC. Enzyme enzymatic activity is regulated by a 24-amino-acid propeptide Cys28-Ser51. Individual amino acid residues within the N-terminus of the PC-PLC propeptide regulate Mpl-mediated maturation of PC-PLC. A single amino acid propeptide is sufficient to inhibit PC-PLC activity, whereas a six-residue propeptide is sufficient for Mpl to mediate the proteolytic maturation of PC-PLC
additional information
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enzyme binding to lipid vesicles is a slow, cooperative process, but after the initial cluster of bound enzyme molecules further binding and catalytic activity follows rapidly. At some late stage of enzyme activity, apparently three-dimensional structures or lipidic aggregates are formed which marks another burst of enzyme activity, and the lysis of the giant vesicle
additional information
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secondary and tertiary structure analysis of the enzyme at different pH values from pH 2.0-7.5, overview
additional information
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sequence comparisons and three-dimensional structure modeling, overview
additional information
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sequence comparisons and three-dimensional structure modeling, overview
additional information
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sequence comparisons and three-dimensional structure modeling, overview
additional information
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sequence comparisons and three-dimensional structure modeling, overview
additional information
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sequence comparisons and three-dimensional structure modeling, overview
additional information
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sequence comparisons and three-dimensional structure modeling, overview
additional information
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sequence comparisons and three-dimensional structure modeling, overview
additional information
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sequence comparisons and three-dimensional structure modeling, overview
additional information
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sequence comparisons and three-dimensional structure modeling, overview
additional information
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sequence comparisons and three-dimensional structure modeling, overview
additional information
sequence comparisons and three-dimensional structure modeling, overview
additional information
sequence comparisons and three-dimensional structure modeling, overview
additional information
sequence comparisons and three-dimensional structure modeling, overview
additional information
sequence comparisons and three-dimensional structure modeling, overview
additional information
sequence comparisons and three-dimensional structure modeling, overview
additional information
sequence comparisons and three-dimensional structure modeling, overview
additional information
the fifteen conserved amino acids Asp63, Tyr156, His166, Phe167, Phe244, His247, Asp251, Phe253, Arg265, His257, His284, Glu286, Asp314, Arg326, and Arg385 are essential for enzyme activity
additional information
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the fifteen conserved amino acids Asp63, Tyr156, His166, Phe167, Phe244, His247, Asp251, Phe253, Arg265, His257, His284, Glu286, Asp314, Arg326, and Arg385 are essential for enzyme activity
additional information
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the N-terminal domain contains the phospholipase C active site, which also incorporates zinc ions. The C-terminal C2-like PLAT (polycystin-1, lipoxygenase, alpha-toxin) domain was found to be similar to lipid binding domains in eukaryotes and appears to be responsible for binding membrane phospholipids in a calcium-dependent manner
additional information
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the fifteen conserved amino acids Asp63, Tyr156, His166, Phe167, Phe244, His247, Asp251, Phe253, Arg265, His257, His284, Glu286, Asp314, Arg326, and Arg385 are essential for enzyme activity
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additional information
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establishing enzyme activity in lipid vesicles, method development, overview. Both lipase activities are sensitive to vesicle size, but in opposite ways: while phospholipase C is higher with larger vesicles, sphingomyelinase activity is lower
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