HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 3.1.4.3 - phospholipase C
for references in articles please use BRENDA:EC3.1.4.3
Word Map on EC 3.1.4.3
- 3.1.4.3
- inositol
- phosphatidylinositol
- phospholipid
- diacylglycerol
- phosphoinositide
- pertussis
- camp
-
influx
-
phorbol
- platelet
-
arachidonic
-
g-proteins
- 1,4,5-trisphosphate
- 4,5-bisphosphate
-
receptor-mediated
- adenylate
-
adenylyl
-
protein-coupled
-
muscarinic
- vibrio
-
phosphatidic
- trisphosphate
-
evoked
- thapsigargin
-
blocker
- carbachol
- pip2
-
3-kinase
- cereus
-
13-acetate
-
metabotropic
-
toxin-sensitive
-
ca2+-free
-
fura-2
-
gtp-binding
-
thromboxane
- bradykinin
-
desensitization
- neomycin
-
phosphatidylinositol-specific
-
12-myristate
- nifedipine
- staurosporine
- perfringens
-
ryanodine
-
enterotoxin
-
store-operated
-
agonist-induced
-
prelabeled
- chelerythrine
- drug development
- analysis
- medicine
- pharmacology
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
3.1.4.3
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
phospholipase C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine
-
-
-
-
a phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine
mode of action of the plant enzyme family of non-specific phospholipases C, overview; mode of action of the plant enzyme family of non-specific phospholipases C, overview; mode of action of the plant enzyme family of non-specific phospholipases C, overview; mode of action of the plant enzyme family of non-specific phospholipases C, overview; mode of action of the plant enzyme family of non-specific phospholipases C, overview; mode of action of the plant enzyme family of non-specific phospholipases C, overview
a phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine
mode of action of the plant enzyme family of non-specific phospholipases C, overview
-
a phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine
mode of action of the plant enzyme family of non-specific phospholipases C, overview
-
a phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine
mode of action of the plant enzyme family of non-specific phospholipases C, overview
-
a phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine
mode of action of the plant enzyme family of non-specific phospholipases C, overview
-
a phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine
mode of action of the plant enzyme family of non-specific phospholipases C, overview
-
a phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine
mode of action of the plant enzyme family of non-specific phospholipases C, overview
-
a phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine
mode of action of the plant enzyme family of non-specific phospholipases C, overview
-
a phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine
mode of action of the plant enzyme family of non-specific phospholipases C, overview
-
a phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine
mode of action of the plant enzyme family of non-specific phospholipases C, overview
-
a phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine
mode of action of the plant enzyme family of non-specific phospholipases C, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
phosphatidylcholine cholinephosphohydrolase
The bacterial enzyme, which is a zinc protein, also acts on sphingomyelin and phosphatidylinositol; that from seminal plasma does not act on phosphatidylinositol.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9001-86-9
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
133931, 135281, 135300, 135302, 135308, 135309, 135311, 135312, 135313, 649316, 677752, 714455, 716013, 729610, 730853
-
-
isoforms phosphatidylcholine-specific phospholipase C, i.e. PC-PLC, and phosphatidylinositol-specific phospholipase C, i.e. PI-PLC
-
-
glutamate decarboxylase 67-green fluorescent protein, GAD67-GFP, knock-in mice
-
-
-
-
-
phospholipase C production by urinary tract isolates is significantly greater than that by lung, blood, or other isolates
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the enzyme belongs to a distinct zinc metallophospholipase C family present in bacteria and fungi
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; 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; 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; 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; 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; 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
-
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
-
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 a distinct zinc metallophospholipase C family present in bacteria and fungi
-
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
-
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
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
-
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
-
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
-
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
-
metabolism
-
membrane lipid formation, turnover, and recycling in Sinorhizobium meliloti, overview
metabolism
-
(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
-
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
model of metabolism regulation carried out by plant cell phospholipases, overview; model of metabolism regulation carried out by plant cell phospholipases, overview; model of metabolism regulation carried out by plant cell phospholipases, overview; model of metabolism regulation carried out by plant cell phospholipases, overview; model of metabolism regulation carried out by plant cell phospholipases, overview; model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
-
model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
-
model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
-
model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
-
model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
-
model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
-
model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
-
model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
-
model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
-
model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
-
model of metabolism regulation carried out by plant cell phospholipases, overview
physiological function
-
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; PLCbeta is probably not involved in egg activation
physiological function
-
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; 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
-
PC-PLC is an important enzyme that plays a key role in a variety of cellular events and lipid homoeostases
physiological function
-
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
-
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
-
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
-
at least one PC-PLC is a plant signaling enzyme in brassinolide signal transduction and, as shown earlier, in elicitor signal transduction
physiological function
-
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
-
the enzyme can degrade endogenous preexisting membrane phospholipids as a source of phosphorus
physiological function
-
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
-
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
-
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
-
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
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
-
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
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; 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; 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; 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; 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; 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 inhibits the formation of cAMP by adenylate cyclase and is involved in the defence mechanism of bacteria to phagocytosis
physiological function
-
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
-
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
-
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. 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. 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. 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. 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. 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. 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. 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. 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 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
-
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
-
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; 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
-
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
-
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
-
additional information
-
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
-
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
-
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
-
secondary and tertiary structure analysis of the enzyme at different pH values from pH 2.0-7.5, 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
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
sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview
additional information
sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview
additional information
sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview
additional information
sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview
additional information
sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview; sequence comparisons and three-dimensional structure modeling, overview
additional information
-
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
-
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
-
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
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-diacyl-sn-glycero-3-phosphatide + H2O
1,2-diacylglycerol + phosphorylalcohol
-
-
-
?
1,2-dicaproylphosphatidylcholine + H2O
1,2-dicaproylglycerol + phosphorylcholine
-
-
-
?
1,2-dihexanoyl-sn-glycero-3-phospho-L-serine + H2O
1,2-dihexanoyl-sn-glycerol + phosphorylserine
-
-
?
1,2-dihexanoyl-sn-glycero-3-phosphocholine + H2O
1,2-dihexanoyl-sn-glycerol + phosphorylcholine
-
-
?
1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + H2O
1,2-dihexanoyl-sn-glycerol + phosphoethanolamine
-
-
?
1,2-dilauroylphosphatidylcholine + H2O
1,2-dilaureoylglycerol + phosphorylcholine
-
-
-
?
1,2-dimyristoylphosphatidylcholine + H2O
1,2-dimyristoylglycerol + phosphorylcholine
-
-
-
?
1,2-dioleoylphosphatidylcholine + H2O
1,2-dioleoylglycerol + phosphorylcholine
-
-
-
?
1,2-dipalmitoylphosphatidylethanolamine + H2O
1,2-dipalmitoylglycerol + phosphorylethanolamine
-
-
-
?
1-arachidonoyl-2-lysophosphatidylcholine + H2O
1-arachidonoyl-sn-glycerol + phosphorylcholine
best substrate
-
-
?
1-arachidoyl-2-lysophosphatidylcholine + H2O
1-arachidoyl-sn-glycerol + phosphorylcholine
poor substrate
-
-
?
1-lauroyl-lysophosphatidylcholine + H2O
1-lauroyl-sn-glycerol + phosphorylcholine
potent substrate
-
-
?
1-linoleoyl-lysophosphatidylcholine + H2O
1-linoleoyl-sn-glycerol + phosphorylcholine
second best substrate
-
-
?
1-myristoyl-lysophosphatidylcholine + H2O
1-myristoyl-sn-glycerol + phosphorylcholine
potent substrate
-
-
?
1-O-(6-(p-methyl red)-amino-hexanoyl)-2-O-(12-(p-methyl red)-amino-dodecanoyl)-sn-glyceryl-N-(3-(5-BODIPY-pentanoyl)-amino-propyl)-N,Ndimethyl-phosphatidylethanolamine + H2O
?
-
fluorogenic analogue of phosphatidylcholine, direct substrate for real-time measurement of enzyme activity
-
-
?
1-oleoyl-lysophosphatidylcholine + H2O
1-oleoyl-sn-glycerol + phosphorylcholine
-
-
-
?
1-palmitoyl-lysophosphatidylcholine + H2O
1-palmitoyl-sn-glycerol + phosphorylcholine
-
-
-
?
1-palmitoyl-lysophosphatidylcholine + H2O
monopalmitoylglycerol + phosphorylcholine
-
-
-
?
1-stearoyl-lysophosphatidylcholine + H2O
1-stearoyl-sn-glycerol + phosphorylcholine
poor substrate
-
-
?
ceramide aminoethylphosphonate
N-acylsphingosine + aminoethylphosphonate
-
-
-
?
ceramide phosphorylethanolamine
N-acylsphingosine + phosphorylethanolamine
-
-
-
?
diheptanoylphosphatidylcholine + H2O
diheptanoylglycerol + phosphorylcholine
-
-
-
?
dihexanoylphosphatidylcholine + H2O
dihexanoylglycerol + phosphorylcholine
-
-
-
?
dimyristoylphosphatidylcholine + H2O
dimyristoylglycerol + phosphorylcholine
-
substrate in mixed micelles with sodium deoxycholate
-
-
?
egg lysophosphatidylcholine + H2O
monoacylglycerol + phosphorylcholine
NPP6 is a choline-specific glycerophosphodiester phosphodiesterase. In marked difference to NPP2 (lysoPLD/autotaxin), which equally hydrolyzes lysophosphatidylcholine, 1-oleoyl lysophosphatidylethanolamine, 1-oleoyl lysophosphatidylserine, and porcine liver lysophosphatidylinositol to form lysophosphatidic acid, NPP6 hydrolyzes only lysophosphatidylcholine
-
-
?
glycerophosphorylcholine + H2O
glycerol + phosphorylcholine
enzyme hydrolyzes GPC efficiently, measurement of GDE activity
-
-
?
lysoPAF + H2O
?
lyso platelet activating factor, partially hydrolyzed
-
-
?
membrane form variant surface glycoproteins + H2O
soluble variant surface glycoprotein + sn-1,2-dimyristoylglycerol
p-nitrophenyl phenylphosphate + H2O
?
pNPPP, classical NPP substrate
-
-
?
p-nitrophenyl phenylphosphate + H2O
p-nitrophenol + phenylphosphate
pNPPP, classical NPP substrate
-
-
?
p-nitrophenyl phosphorylcholine + H2O
?
recombinant NPP6 efficiently hydrolyzes the classical substrate for phospholipase C
-
-
?
p-nitrophenyl phosphorylcholine + H2O
? + p-nitrophenol
pNPPC, classical NPP substrate
-
-
?
p-nitrophenyl phosphorylcholine + H2O
p-nitrophenol + phosphorylcholine
pNPPC, classical NPP substrate, recombinant NPP6 efficiently hydrolyzes the classical substrate for phospholipase C
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
specific for
-
-
?
phosphatidic acid + H2O
1,2-sn-diacylglycerol + phosphate
-
-
-
?
phosphatidylethanolamine + H2O
1,2-sn-diacylglycerol + phosphoethanolamine
-
-
-
?
phosphatidylinositol + H2O
inositol + phosphatidate
-
Ca2+-dependent activity
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
sphingosylphosphorylcholine + H2O
?
SPC, measurement of lysoPLC activity of NPP6 toward choline-containing phospholipids
-
-
?
1,2-dioleoylphosphatidylethanolamine + H2O
1,2-dioleoylglycerol + phosphorylethanolamine
-
-
-
?
1,2-dioleoylphosphatidylethanolamine + H2O
1,2-dioleoylglycerol + phosphorylethanolamine
-
-
-
?
1,2-dipalmitoylphosphatidylcholine + H2O
1,2-dipalmitoylglycerol + phosphorylcholine
-
-
-
?
1,2-dipalmitoylphosphatidylcholine + H2O
1,2-dipalmitoylglycerol + phosphorylcholine
-
-
-
?
1,2-dipalmitoylphosphatidylcholine + H2O
1,2-dipalmitoylglycerol + phosphorylcholine
-
-
-
-
?
1,2-dipalmitoylphosphatidylcholine + H2O
1,2-dipalmitoylglycerol + phosphorylcholine
-
-
-
?
1,2-dipalmitoylphosphatidylcholine + H2O
1,2-dipalmitoylglycerol + phosphorylcholine
-
-
-
?
1,2-dipalmitoylphosphatidylcholine + H2O
1,2-dipalmitoylglycerol + phosphorylcholine
-
-
-
-
?
cardiolipin + H2O
phosphatidylglycerophosphate + 1,2-diacylglycerol
-
-
-
?
cardiolipin + H2O
phosphatidylglycerophosphate + 1,2-diacylglycerol
-
-
-
?
lysophosphatidylcholine + H2O
monoacylglycerol + phosphorylcholine
-
-
-
?
lysophosphatidylcholine + H2O
monoacylglycerol + phosphorylcholine
-
-
-
?
lysophosphatidylcholine + H2O
monoacylglycerol + phosphorylcholine
-
-
-
?
lysophosphatidylcholine + H2O
monoacylglycerol + phosphorylcholine
-
-
-
?
lysophosphatidylcholine + H2O
monoacylglycerol + phosphorylcholine
-
-
-
?
lysophosphatidylcholine + H2O
monoacylglycerol + phosphorylcholine
-
-
-
?
lysophosphatidylcholine + H2O
monoacylglycerol + phosphorylcholine
-
-
-
?
lysophosphatidylcholine + H2O
monoacylglycerol + phosphorylcholine
-
-
-
?
lysophosphatidylcholine + H2O
monoacylglycerol + phosphorylcholine
-
-
-
?
membrane form variant surface glycoproteins + H2O
soluble variant surface glycoprotein + sn-1,2-dimyristoylglycerol
-
-
-
?
membrane form variant surface glycoproteins + H2O
soluble variant surface glycoprotein + sn-1,2-dimyristoylglycerol
-
-
-
?
p-nitrophenylphosphoryl-choline + H2O
p-nitrophenol + phosphorylcholine
-
-
-
-
-
p-nitrophenylphosphoryl-choline + H2O
p-nitrophenol + phosphorylcholine
-
-
-
-
?
p-nitrophenylphosphorylcholine + H2O
p-nitrophenol + phosphorylcholine
-
-
-
-
?
p-nitrophenylphosphorylcholine + H2O
p-nitrophenol + phosphorylcholine
-
-
-
-
?
p-nitrophenylphosphorylcholine + H2O
p-nitrophenol + phosphorylcholine
-
-
-
-
?
p-nitrophenylphosphorylcholine + H2O
p-nitrophenol + phosphorylcholine
-
-
-
?
p-nitrophenylphosphorylcholine + H2O
p-nitrophenol + phosphorylcholine
-
-
-
-
?
p-nitrophenylphosphorylcholine + H2O
p-nitrophenol + phosphorylcholine
-
-
-
-
?
p-nitrophenylphosphorylcholine + H2O
p-nitrophenylglycerol + phosphorylcholine
-
-
-
?
p-nitrophenylphosphorylcholine + H2O
p-nitrophenylglycerol + phosphorylcholine
-
-
-
?
phosphatidic acid + H2O
?
-
9.04% of the activity with phosphatidylcholine
-
-
?
phosphatidic acid + H2O
?
-
9.04% of the activity with phosphatidylcholine
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
Clostridium welchii
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
substrate from egg yolk
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
hemolytic PLC
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
nonhemolytic PLC
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
phosphatidylcholine and sphingomyelin are cleaved at equal rate
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
substrate from egg yolk
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
the enzyme shows cell-associated phosphatidylcholine-specific phospholipase C activity in vivo
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
the enzyme shows cell-associated phosphatidylcholine-specific phospholipase C activity in vivo
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylethanolamine + H2O
1,2-diacyl-sn-glycerol + ethanolamine phosphate
-
-
-
-
?
phosphatidylethanolamine + H2O
1,2-diacyl-sn-glycerol + ethanolamine phosphate
-
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + 1,2-diacylglycerol
-
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + 1,2-diacylglycerol
-
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + 1,2-diacylglycerol
-
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
-
-
?
phosphatidylglycerol + H2O
1,2-sn-diacylglycerol + phosphatidate
-
-
-
?
phosphatidylglycerol + H2O
1,2-sn-diacylglycerol + phosphatidate
-
-
-
?
phosphatidylinositol + H2O
1,2-sn-diacylglycerol + phosphoinositol
-
-
-
?
phosphatidylinositol + H2O
1,2-sn-diacylglycerol + phosphoinositol
-
-
-
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
-
-
-
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
-
-
-
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
-
-
-
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
-
-
-
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
-
-
-
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
-
-
-
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
-
-
-
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
-
-
-
?
phosphatidylinositol 4,5-bisphosphate + H2O
inositol 4,5-bisphosphate + phosphatidate
-
Ca2+-independent activity
-
?
phosphatidylinositol 4,5-bisphosphate + H2O
inositol 4,5-bisphosphate + phosphatidate
-
-
-
?
phosphatidylinositol 4,5-bisphosphate + H2O
inositol 4,5-bisphosphate + phosphatidate
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylserine + H2O
phosphorylserine + diacylglycerol
-
-
-
?
phosphatidylserine + H2O
phosphorylserine + diacylglycerol
-
-
-
?
phosphatidylserine + H2O
phosphorylserine + diacylglycerol
-
-
-
?
phosphatidylserine + H2O
phosphorylserine + diacylglycerol
-
nonhemolytic PLC
-
-
?
phosphatidylserine + H2O
phosphorylserine + diacylglycerol
-
-
-
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
when substrate is presented in a biological membrane, for example in the human red cell membrane or myelin sheath
-
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
hemolytic PLC
-
-
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
phosphatidylcholine and sphingomyelin are cleaved at equal rate
-
-
?
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
-
-
-
-
?
additional information
?
-
-
PLCBC also catalyzes the hydrolysis of phosphatidylethanolamine and phosphatidylserine but with lower efficiency
-
-
-
additional information
?
-
-
modeling of active site and reaction mechanism, development of two different reaction mechanism models, overview
-
-
-
additional information
?
-
-
phospholipase C can catalyze the membrane fusion between cell membranes and phospholipid vehicles (liposomes) at pH 4.0-7.5, highest activity at pH 5.0, 37°C. The liposomes are composed of 1,2-dioleoyl-sn-glycero-3-phosphocholine, 1,2-dipalmitoyl-sn-glycero-3-phosphocholine, and cholesterol in a 1:1:1 molar ratio, membrane fusion is dependent of the lipid composition, overview. The enzyme takes a molten-globule state, with a large fluctuation at acidic pH, mechanism of enzyme-induced membrane fusion
-
-
-
additional information
?
-
enzyme is not haemolytic for human erythrocytes and not involved in multinucleated giant cell formation or induction of apoptotic cell death
-
-
-
additional information
?
-
-
the release of Ca2+ from the intracellular calcium stores after application of ATP or carbachol is mediated by phospholipase C
-
-
-
additional information
?
-
-
the enzyme is the major virulence factor in the pathogenesis of gas gangrene. Reduction in gangliosides renders cells more susceptible to the membrane f´damage caused by Cp-PLC
-
-
-
additional information
?
-
-
substrate specificity analysis by molecular docking reveals that the enzyme is also active with phosphatidylethanolamine and phosphatidylinositol, and to a lower level with phosphatidylglycerol, overview
-
-
-
additional information
?
-
-
substrate specificity analysis by molecular docking reveals that the enzyme is also active with phosphatidylethanolamine and phosphatidylinositol, and to a lower level with phosphatidylglycerol, overview
-
-
-
additional information
?
-
-
the signaling pathway of human imidazoline receptor antisera-selected protein IRAS in response to I1-imidazoline receptor agonists is coupled with the activation of isoform PC-PLC and its downstream signal transduction molecule ERK
-
-
-
additional information
?
-
-
isoform PC-PLC and reactive oxygen species are involved in chicken blastodisc differentiation to vascular endothelial cells
-
-
-
additional information
?
-
-
isoform PC-PLC plays an important role in regulating CD16 receptor membrane expression, the CD16-mediated cytolytic mechanism and CD16-triggered signal transduction
-
-
-
additional information
?
-
-
isoforms phosphatidylcholine-specific phospholipase C, i.e. PC-PLC, and phosphatidylinositol-specific phospholipase C, i.e. PI-PLC, control apoptosis by jointly regulating Akt phosphorylation, p53 expression, and affecting cell cycle in vascular endothelial cells
-
-
-
additional information
?
-
release of nucleoside 5'-monophosphate from a variety of nucleotides and nucleotide derivatives
-
-
-
additional information
?
-
recombinant NPP6 does not hydrolyze the classical nucleotide phosphodiesterase substrate, p-nitrophenyl thymidine 5'-monophosphate (pNP-TMP) and bis(p-nitrophenyl) phosphate. NPP6 does not act on sphingomyelin (SM)
-
-
-
additional information
?
-
-
the recombinant enzyme hydrolyzes a broad phospholipid spectrum, including phosphatidylcholine, phosphatidylglycerol, and phosphatidylinositol, broad substrate preference
-
-
-
additional information
?
-
the recombinant enzyme hydrolyzes a broad phospholipid spectrum, including phosphatidylcholine, phosphatidylglycerol, and phosphatidylinositol, broad substrate preference
-
-
-
additional information
?
-
the recombinant enzyme hydrolyzes a broad phospholipid spectrum, including phosphatidylcholine, phosphatidylglycerol, and phosphatidylinositol, broad substrate preference
-
-
-
additional information
?
-
-
the enzyme induces membrane fusion
-
-
-
additional information
?
-
release nucleoside 5'-monophosphate from a variety of nucleotides and nucleotide derivatives
-
-
-
additional information
?
-
-
the enzyme plays a key role in the pathogenesis of bacterial infection
-
-
-
additional information
?
-
-
the enzyme plays a key role in the pathogenesis of bacterial infection
-
-
-
additional information
?
-
-
the enzyme plays a key role in the pathogenesis of bacterial infection
-
-
-
additional information
?
-
-
the enzyme plays a key role in the pathogenesis of bacterial infection
-
-
-
additional information
?
-
-
phospholipase C hydrolyzes phosphatidylethanolamine and phosphatidylcholine but not other glycerophospholipids
-
-
-
additional information
?
-
-
phospholipase C hydrolyzes phosphatidylethanolamine and phosphatidylcholine but not other glycerophospholipids
-
-
-
additional information
?
-
-
enzyme activity is necessary for PLC-induced inflammation
-
-
-
additional information
?
-
-
hemolytic fractions from strain ATCC 19660 cause paralysis, death, dermonecrosis, footpad swelling, and vascular permeability in mice. The toxicity is directly associated with enzymatic activity
-
-
-
additional information
?
-
-
homoserine lactone-mediated quorum sensing regulates the expression of PA0026, which encodes PlcB. PlcB is required for directed twitching motility up a gradient of certain kinds of phospholipids
-
-
-
additional information
?
-
-
phospholipase C causes platelet aggregation in a concentration-dependent manner
-
-
-
additional information
?
-
-
phospholipase C plays a role in pathogenesis of infections by Pseudomonas aeruginosa
-
-
-
additional information
?
-
-
the enzyme, when injected intradermally into the skin of sheep, elicits histopathological lesions virtually identical to that seen in naturally occuring fleecerot
-
-
-
additional information
?
-
-
the catalytic activity of enyme induces substrate vesicle fusion without relase of vesicular content. The presence of phosphatidylserine in the vesicle composition does not modify significantly enzyme. Induced liposome aggregation, but completely abolishes fusion. Enzyme is inactive on phospholipids that lack choline head groups
-
-
-
additional information
?
-
-
The sphingomyelinase, but not the phospholipase C activity, is essential for induction of hot-cold hemolysis in human erythrocytes, that contain both phosphatidylcholine and sphingomyelin but also in goat erythrocytes, which lack phosphatidylcholine, however, in horse erythrocytes, with a large proportion of phosphatidylcholine and almost no sphingomyelin, hot-cold hemolysis induced by PlcHR2 is not observed, overview
-
-
-
additional information
?
-
-
PlcHR2 toxin from Pseudomonas aeruginosa is an enzyme with both phospholipase C and sphingomyelinase activities, PlcHR2 hydrolyzes phosphatidylcholine and sphingomyelin at similar rates, but other phospholipids are cleaved at much lower rates, if at all
-
-
-
additional information
?
-
-
activity measurement with substrate on giant unilamellar lipid vesicles. Enzyme binding to the vesicles appears to be a cooperative process and is irreversible, binding analysis using wild-type enzyme and catalytically inactive enzyme mutant T178A. After the initial cluster of bound enzyme is detected, further binding and catalytic activity follow rapidly. The enzyme preferentially binds the more disordered domains, and, in most cases, the catalytic activity causes the disordering of the other domains, at a further stage of lipid hydrolysis, lipid aggregates are formed and vesicles disintegrate, overview
-
-
-
additional information
?
-
-
PlcHR2 is a secreted toxin that exhibits phospholipase C and sphingomyelinase activities. It shows hydrolytic activity of PlcHR2 on bilayers of varying lipid compositions, e.g. on giant unilamellar vesicles composed of sphingomyelin, phosphatidylcholine, phosphatidylethanolamine, and cholesterol
-
-
-
additional information
?
-
-
phosphatidylethanolamine, sphingomyelin, phosphatidylinositol and phosphatidylserine are hydrolyzed at less than 1% of the activity with phosphatidylcholine
-
-
-
additional information
?
-
-
phosphatidylethanolamine, sphingomyelin, phosphatidylinositol and phosphatidylserine are hydrolyzed at less than 1% of the activity with phosphatidylcholine
-
-
-
additional information
?
-
-
enzyme induces cell cycle progression, overexpression of enzyme induces overexpression of cyclin D3
-
?
additional information
?
-
-
enzyme is regulated through redox- and calcium-dependent manners in alveolar macrophage
-
-
-
additional information
?
-
-
low isoform PC-PLC activity is required for mesenchymal stem cell neuronal differentiation, and basic fibroblast growth factor is necessary for maintaining the neuronal differentiation state
-
-
-
additional information
?
-
-
interaction between PC-PLC and cell division cycle 20 homologue, Cdc20, initiating the degradation of PC-PLC by Cdc20-mediated ubiquitin proteasome pathway
-
-
-
additional information
?
-
-
cPC-PLC may contribute to the parasite evasion against the host immune response
-
-
-
additional information
?
-
-
mPC-PLC may play a role in the intercellular multiplication of Uronema marinum
-
-
-
additional information
?
-
-
no activity with phosphatidylinositol and phosphatidylethanolamine
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-diacyl-sn-glycero-3-phosphatide + H2O
1,2-diacylglycerol + phosphorylalcohol
-
-
-
?
membrane form variant surface glycoproteins + H2O
soluble variant surface glycoprotein + sn-1,2-dimyristoylglycerol
phosphatidylethanolamine + H2O
1,2-sn-diacylglycerol + phosphoethanolamine
O81020, Q8H965, Q8L7Y9, Q9S816, Q9SRQ6
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
membrane form variant surface glycoproteins + H2O
soluble variant surface glycoprotein + sn-1,2-dimyristoylglycerol
-
-
-
?
membrane form variant surface glycoproteins + H2O
soluble variant surface glycoprotein + sn-1,2-dimyristoylglycerol
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
Q9SRQ7
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
Q9SRQ7
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
Clostridium welchii
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
O81020, Q8H965, Q8L7Y9, Q9S816, Q9SRQ6
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
Q5ZZJ8
the enzyme shows cell-associated phosphatidylcholine-specific phospholipase C activity in vivo
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
Q5ZZJ8
the enzyme shows cell-associated phosphatidylcholine-specific phospholipase C activity in vivo
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
-
-
?
additional information
?
-
-
PLCBC also catalyzes the hydrolysis of phosphatidylethanolamine and phosphatidylserine but with lower efficiency
-
-
-
additional information
?
-
Q9RGS8
enzyme is not haemolytic for human erythrocytes and not involved in multinucleated giant cell formation or induction of apoptotic cell death
-
-
-
additional information
?
-
-
the release of Ca2+ from the intracellular calcium stores after application of ATP or carbachol is mediated by phospholipase C
-
-
-
additional information
?
-
-
the enzyme is the major virulence factor in the pathogenesis of gas gangrene. Reduction in gangliosides renders cells more susceptible to the membrane f´damage caused by Cp-PLC
-
-
-
additional information
?
-
-
the signaling pathway of human imidazoline receptor antisera-selected protein IRAS in response to I1-imidazoline receptor agonists is coupled with the activation of isoform PC-PLC and its downstream signal transduction molecule ERK
-
-
-
additional information
?
-
-
isoform PC-PLC and reactive oxygen species are involved in chicken blastodisc differentiation to vascular endothelial cells
-
-
-
additional information
?
-
-
isoform PC-PLC plays an important role in regulating CD16 receptor membrane expression, the CD16-mediated cytolytic mechanism and CD16-triggered signal transduction
-
-
-
additional information
?
-
-
isoforms phosphatidylcholine-specific phospholipase C, i.e. PC-PLC, and phosphatidylinositol-specific phospholipase C, i.e. PI-PLC, control apoptosis by jointly regulating Akt phosphorylation, p53 expression, and affecting cell cycle in vascular endothelial cells
-
-
-
additional information
?
-
Q6UWR7
release of nucleoside 5'-monophosphate from a variety of nucleotides and nucleotide derivatives
-
-
-
additional information
?
-
-
the enzyme induces membrane fusion
-
-
-
additional information
?
-
Q8BGN3
release nucleoside 5'-monophosphate from a variety of nucleotides and nucleotide derivatives
-
-
-
additional information
?
-
-
the enzyme plays a key role in the pathogenesis of bacterial infection
-
-
-
additional information
?
-
-
the enzyme plays a key role in the pathogenesis of bacterial infection
-
-
-
additional information
?
-
-
the enzyme plays a key role in the pathogenesis of bacterial infection
-
-
-
additional information
?
-
-
the enzyme plays a key role in the pathogenesis of bacterial infection
-
-
-
additional information
?
-
-
enzyme activity is necessary for PLC-induced inflammation
-
-
-
additional information
?
-
-
hemolytic fractions from strain ATCC 19660 cause paralysis, death, dermonecrosis, footpad swelling, and vascular permeability in mice. The toxicity is directly associated with enzymatic activity
-
-
-
additional information
?
-
-
homoserine lactone-mediated quorum sensing regulates the expression of PA0026, which encodes PlcB. PlcB is required for directed twitching motility up a gradient of certain kinds of phospholipids
-
-
-
additional information
?
-
-
phospholipase C causes platelet aggregation in a concentration-dependent manner
-
-
-
additional information
?
-
-
phospholipase C plays a role in pathogenesis of infections by Pseudomonas aeruginosa
-
-
-
additional information
?
-
-
the enzyme, when injected intradermally into the skin of sheep, elicits histopathological lesions virtually identical to that seen in naturally occuring fleecerot
-
-
-
additional information
?
-
-
The sphingomyelinase, but not the phospholipase C activity, is essential for induction of hot-cold hemolysis in human erythrocytes, that contain both phosphatidylcholine and sphingomyelin but also in goat erythrocytes, which lack phosphatidylcholine, however, in horse erythrocytes, with a large proportion of phosphatidylcholine and almost no sphingomyelin, hot-cold hemolysis induced by PlcHR2 is not observed, overview
-
-
-
additional information
?
-
-
PlcHR2 is a secreted toxin that exhibits phospholipase C and sphingomyelinase activities. It shows hydrolytic activity of PlcHR2 on bilayers of varying lipid compositions, e.g. on giant unilamellar vesicles composed of sphingomyelin, phosphatidylcholine, phosphatidylethanolamine, and cholesterol
-
-
-
additional information
?
-
-
enzyme induces cell cycle progression, overexpression of enzyme induces overexpression of cyclin D3
-
?
additional information
?
-
-
enzyme is regulated through redox- and calcium-dependent manners in alveolar macrophage
-
-
-
additional information
?
-
-
low isoform PC-PLC activity is required for mesenchymal stem cell neuronal differentiation, and basic fibroblast growth factor is necessary for maintaining the neuronal differentiation state
-
-
-
additional information
?
-
-
interaction between PC-PLC and cell division cycle 20 homologue, Cdc20, initiating the degradation of PC-PLC by Cdc20-mediated ubiquitin proteasome pathway
-
-
-
additional information
?
-
-
cPC-PLC may contribute to the parasite evasion against the host immune response
-
-
-
additional information
?
-
-
mPC-PLC may play a role in the intercellular multiplication of Uronema marinum
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
Zn2+
additional information
Ca2+
-
recombinant PLC d3: maximum activity with 0.001 mM, recombinant PLC d1: maximum activity with 0.01 mM
Ca2+
-
PLC-beta 1a and -beta 1b: maximum activity with 3 mM with phosphatidylinositol for substrate, PLC translocation to membranes by free Ca2+ concentration of 100 nM
Ca2+
-
0.4 mM required for maximal activition, mPC-PLC; 1.6 mM required for maximal activition, cPC-PLC
Co2+
-
restores activity after EDTA treatment; restores activity after o-phenanthroline-treatment
Mg2+
-
restores ability of Ca2+-inhibited PLC to hydrolyse sphingomyelin
Mg2+
-
2.5 mM required for maximal activation, mPC-PLC; 2.5 mM required for maximal activity, cPC-PLC
Mn2+
-
restores activity after EDTA treatment; restores activity after o-phenanthroline-treatment
Zn2+
-
2 mol Zn2+ per mol enzyme; metalloenzyme; renaturation of guanidinium chloride treated PLC
Zn2+
-
3 Zn2+ ions in active site; in the active site of the enzyme; metalloenzyme
Zn2+
-
phospholipase C is a trinuclear zinc enzyme, structure analysis, using also the crystal structure from PDB entry 1AH7, overview
Zn2+
-
zinc-dependent enzyme. His216 is required for coordinate binding of zinc
Zn2+
-
metalloenzyme; restores activity after EDTA treatment; restores activity after o-phenanthroline-treatment
additional information
none of the divalent cations tested (Ca2+, Mg2+, Zn2+, Ni2+, Co2+, Fe2+, and Cu2+) rescued the lost activity after treatment with EDTA, EGTA
additional information
-
enzyme belongs to the group of metallophospholipases C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-[6-[[(17beta)-3-methoxyestra-1,3,5(10)-trien-17-yl]amino]hexyl]-1H-pyrrole-2,5-dione
-
i.e. U-73122, a phospholipase C inhibitor
1-[hydroxy[2-(trimethylammonio)ethyl]amino]-1-oxododecan-2-aminium
-
uncompetitive inhibition
1-[hydroxy[3-(trimethylammonio)propyl]amino]-1-oxododecan-2-aminium
-
mixed type inhibition
2-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]dodecanoyl]amino]-N,N,N-trimethylethanaminium
-
-
2-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]hexadecanoyl]amino]-N,N,N-trimethylethanaminium
-
-
2-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]icosanoyl]amino]-N,N,N-trimethylethanaminium
-
-
2-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]octanoyl]amino]-N,N,N-trimethylethanaminium
-
-
3(S),4-dihexanoylbutyl-1-phosphonycholine
-
non-hydrolyzable, competitive inhibitor of bacterial PLC, analog of the natural phospholipid substrate, binds with its phosphonyl group to the three Zn-ions in the active site of the enzyme
3-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]dodecanoyl]amino]-N,N,N-trimethylpropan-1-aminium
-
mixed type inhibition
3-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]octanoyl]amino]-N,N,N-trimethylpropan-1-aminium
-
-
48/80
-
compound 48/80, oligomeric mixture of condensation products of N-methyl-p-methoxyphenethylamine and formaldehyde. Specific inhibition of phosphatidylinositol-specific phospholipase C, i.e. PI-PLC. Suppression of PI-PLC promotes apoptosis of vascular endothelial cells by inhibiting Akt phosphorylation, elevating p53 expression, and affecting cell cycle distribution
AlCl3
-
at 1 mM, about 60% inhibition of soluble isoform, 50% inhibition of membrane-associated isoform, inhibition of root growth
EGTA
enzyme activity against 1-myristoyl-lysophosphatidylcholine, glycerophosphorylcholine, and p-nitrophenyl phosphorylcholine are readily inhibited by EGTA. Indicates that a divalent cation is essential for catalytic activity
tert-butyl (1-[(benzyloxy)[3-(dimethylamino)propyl]amino]-1-oxododecan-2-yl)carbamate
-
noncompetitive inhibition
tert-butyl (1-[(benzyloxy)[3-(dimethylamino)propyl]amino]-1-oxooctan-2-yl)carbamate
-
-
tricyclodecan-9-yl-potassium xanthate
-
The recovery of both variables to their original levels in serum-restimulated (or lysophosphatidic acid-restimulated) EOC cells is strongly delayed, for at least 24 h, in the presence of the PC-PLC inhibitor tricyclodecan-9-yl-potassium xanthate (D609). The S-phase of serum-restimulated EONT cells is not sensitive to D609
Ca2+
-
inhibits phosphatidylethanolamine hydrolysis
Ca2+
-
activity rapidly decreases at concentrations of 0.015-0.030 mM and above
Cu2+
-
study of in vivo inhibitory capacity, time course, recovery after 7 days
D609
-
i.e. tricyclodecan-9-yl potassium xanthate, inhibition of isoform PC-PLC. After application on blastodisc at 24 h, cell differentiation cannot progress and intracellular level of reactive oxygen species is elevated
D609
-
specific inhibition of phosphatidylcholine-specific phospholipase C, i.e. PC-PLC. Suppression of PC-PLC promotes the phosphorylation of Akt protein
D609
-
inhibitor of isoform PC-PLC, preincubation with D609 results in a dramatic decrease both in CD16 receptor and PC-PLC expression on the plasma membrane and reduction of CD16-mediated cytotoxicity
D609
-
suppression of isoform PC-PLC by D609 inhibits apoptosis in young cells, but not in senescent cells, and depresses reactive oxygen species levels in both young and senescent cells
D609
-
inhibition of isoform PC-PLC blocks the silica-stimulated induction of TNF-alpha and interleukin-1beta
D609
-
inhibition of isoform PC-PLC activity coupled with induction of neuronal differentiation. Simultaneously, the level of reactive oxygen species, and the activity of NADPH oxidase increase significantly, without alteration of the levels of Mn-superoxide dismutase and Cu/ZN superoxide dismutase
EDTA
enzyme activity against 1-myristoyl-lysophosphatidylcholine, glycerophosphorylcholine, and p-nitrophenyl phosphorylcholine are readily inhibited by EDTA. Indicates that a divalent cation is essential for catalytic activity
Hg2+
-
study of in vivo inhibitory capacity, time course, recovery after 7 days
Mg2+
-
inhibits phosphatidylethanolamine hydrolysis
Mn2+
-
inhibits phosphatidylethanolamine hydrolysis
o-phenanthroline
-
inhibits the phospholipase C hydrolytic activity of the enzyme, but not its membrane fusion activity