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Information on EC 3.1.4.3 - phospholipase C
for references in articles please use BRENDA:EC3.1.4.3
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.4 Phosphoric-diester hydrolases
3.1.4.3 phospholipase C
IUBMB Comments
The bacterial enzyme, which is a zinc protein, also acts on sphingomyelin and phosphatidylinositol; that from seminal plasma does not act on phosphatidylinositol.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 3.1.4.3
- inositol
- agonist
- phosphatidylinositol
- pkc
- phospholipid
- diacylglycerol
- phosphoinositide
- cyclase
- pertussis
- camp
-
phorbol
- g-proteins
- platelet
-
arachidonic
- 1,4,5-trisphosphate
- 4,5-bisphosphate
-
receptor-mediated
- vibrio
- thapsigargin
- trisphosphate
- adenylate
-
protein-coupled
-
blocker
-
adenylyl
- phospholipases
-
muscarinic
-
phosphatidic
- cereus
- carbachol
- perfringens
- pip2
-
fura-2
- neomycin
-
ca2+-free
-
phosphatidylinositol-specific
-
metabotropic
-
13-acetate
-
thromboxane
- nifedipine
- parahaemolyticus
- staurosporine
- bradykinin
- enterotoxin
-
desensitization
-
ryanodine
-
prelabeled
-
toxin-sensitive
-
store-operated
- chelerythrine
-
agonist-induced
- analysis
- drug development
- medicine
- food industry
- pharmacology
showSynonyms
phospholipase c, plc, hemolysin, pc-plc, lecithinase, phosphatidylcholine-specific phospholipase c, plcbeta, plcg2, beta toxin, plcg1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-toxin
Beta toxin
-
-
-
-
Beta-hemolysin
-
-
-
-
Beta-toxin
-
-
-
-
broad-range phospholipase C
Cbp
-
-
-
-
cholinespecific glycerophosphodiester phosphodiesterase
Clostridium oedematiens beta- and gamma-toxins
-
-
-
-
Clostridium welchii alpha-toxin
-
-
-
-
Dot/Icm-injected effector
Gamma-toxin
-
-
-
-
Heat labile-hemolysin
-
-
-
-
heat-labile hemolysin
-
-
-
-
Hemolysin
-
-
-
-
Lecithinase
lecithinase C
-
-
-
-
lipophosphodiesterase C
-
-
-
-
lipophosphodiesterase I
-
-
-
-
LmPC-PLC
MTP40 antigen
-
-
-
-
non-specific phospholipase C
nonspecific phospholipase C
NPC
NPC1
NPC2
NPC3
NPC4
NPC5
NPC6
NPP6
nucleotide pyrophosphatase/phosphodiesterase
PC-PLC
phosphatidase C
-
-
-
-
Phosphatidylcholine cholinephosphohydrolase
-
-
-
-
phosphatidylcholine phospholipase C
phosphatidylcholine-hydrolysing phospholipase C
phosphatidylcholine-hydrolyzing phospholipase C
phosphatidylcholine-specific phospholipase C
phospholipase C
phospholipase C/sphingomyelinase
PLC
PLC1
PLC2
PlcB
PLCbeta
plcC
PlcC/CegC1
PLCgamma
PlcH
PLCLM
Rv3487c
SMase
-
-
-
-
sphingomyelinase
-
-
-
-
additional information
alpha-toxin
-
-
-
-
Lecithinase
-
-
-
-
PC-PLC
-
-
-
-
phosphatidylcholine-specific phospholipase C
-
-
PLC
-
-
-
-
additional information
the enzyme is a member of the plant phospholipase family
additional information
the enzyme is a member of the plant phospholipase family
-
additional information
-
cf. EC 3.1.4.12, the enzyme is the prototype of another phosphatase superfamily
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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
-
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
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
2-arachidonoylglycerol biosynthesis, phospholipases, plasmalogen biosynthesis I (aerobic), plasmalogen degradation
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9001-86-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-diacyl-sn-glycero-3-phosphatide + H2O
1,2-diacylglycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
1,2-dibutyryl-sn-glycero-3-phosphocholine + H2O
1,2-dibutyryl-sn-glycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
1,2-dicaproylphosphatidylcholine + H2O
1,2-dicaproylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
1,2-diheptanoyl-sn-glycero-3-phosphocholine + H2O
1,2-diheptanoyl-sn-glycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
1,2-dihexanoyl-sn-glycero-3-phospho-L-serine + H2O
1,2-dihexanoyl-sn-glycerol + phosphorylserine
Substrates: -
Products: -
Products: -
?
1,2-dihexanoyl-sn-glycero-3-phosphocholine + H2O
1,2-dihexanoyl-sn-glycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
1,2-dihexanoyl-sn-glycero-3-phosphocholine + H2O
1,2-dihexanoyl-sn-glycerol + phosphorylcholine
Substrates: -
Products: -
Products: -
?
1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + H2O
1,2-dihexanoyl-sn-glycerol + phosphoethanolamine
1,2-dilauroylphosphatidylcholine + H2O
1,2-dilaureoylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
1,2-dimyristoylphosphatidylcholine + H2O
1,2-dimyristoylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
1,2-dioleoyl-sn-glycero-3-phospho-(1'-rac-glycerol) + H2O
1,2-dioleoyl-sn-glycerol + glycerol 1-phosphate
-
Substrates: about 25% activity compared to 1,2-dioleoyl-sn-glycero-3-phosphocholine
Products: -
Products: -
?
1,2-dioleoyl-sn-glycero-3-phospho-L-serine + H2O
1,2-dioleoyl-sn-glycerol + phospho-L-serine
-
Substrates: 60% activity compared to 1,2-dioleoyl-sn-glycero-3-phosphocholine
Products: -
Products: -
?
1,2-dioleoyl-sn-glycero-3-phospho-L-serine-N-(7-nitro-2-1,3-benzoxadiazol-4-yl) + H2O
?
-
Substrates: -
Products: -
Products: -
?
1,2-dioleoyl-sn-glycero-3-phosphocholine + H2O
1,2-dioleoyl-sn-glycerol + phosphocholine
-
Substrates: 100% activity
Products: -
Products: -
?
1,2-dioleoyl-sn-glycero-3-phosphocholine-N-(cyanine 5) + H2O
?
-
Substrates: -
Products: -
Products: -
?
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine + H2O
1,2-dioleoyl-sn-glycerol + phosphoethanolamine
-
Substrates: about 70% activity compared to 1,2-dioleoyl-sn-glycero-3-phosphocholine
Products: -
Products: -
?
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-(7-nitro-2-1,3-benzoxadiazol-4-yl) + H2O
?
-
Substrates: -
Products: -
Products: -
?
1,2-dioleoylphosphatidylcholine + H2O
1,2-dioleoylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
1,2-dipalmitoylphosphatidylethanolamine + H2O
1,2-dipalmitoylglycerol + phosphorylethanolamine
-
Substrates: -
Products: -
Products: -
?
1-arachidonoyl-2-lysophosphatidylcholine + H2O
1-arachidonoyl-sn-glycerol + phosphorylcholine
Substrates: best substrate
Products: -
Products: -
?
1-arachidoyl-2-lysophosphatidylcholine + H2O
1-arachidoyl-sn-glycerol + phosphorylcholine
Substrates: poor substrate
Products: -
Products: -
?
1-lauroyl-lysophosphatidylcholine + H2O
1-lauroyl-sn-glycerol + phosphorylcholine
Substrates: potent substrate
Products: -
Products: -
?
1-linoleoyl-lysophosphatidylcholine + H2O
1-linoleoyl-sn-glycerol + phosphorylcholine
Substrates: second best substrate
Products: -
Products: -
?
1-myristoyl-lysophosphatidylcholine + H2O
1-myristoyl-sn-glycerol + phosphorylcholine
Substrates: potent substrate
Products: -
Products: -
?
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
?
-
Substrates: fluorogenic analogue of phosphatidylcholine, direct substrate for real-time measurement of enzyme activity
Products: -
Products: -
?
1-oleoyl-lysophosphatidylcholine + H2O
1-oleoyl-sn-glycerol + phosphorylcholine
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphate + choline
Substrates: the enzyme hydrolyzes 98.4% of mixed micelle 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine in 1 h
Products: -
Products: -
?
1-palmitoyl-lysophosphatidylcholine + H2O
monopalmitoylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
1-stearoyl-lysophosphatidylcholine + H2O
1-stearoyl-sn-glycerol + phosphorylcholine
Substrates: poor substrate
Products: -
Products: -
?
2-oleoyl-1-palmitoyl-sn-glycero-3-phosphocholine + H2O
1-palmitoyl-2-oleoyl-sn-glycerol + phosphocholine
Substrates: -
Products: -
Products: -
?
BODIPY-phosphatidylcholine + H2O
BODIPY-1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
ceramide aminoethylphosphonate
N-acylsphingosine + aminoethylphosphonate
-
Substrates: -
Products: -
Products: -
?
ceramide phosphorylethanolamine
N-acylsphingosine + phosphorylethanolamine
-
Substrates: -
Products: -
Products: -
?
choline plasmalogen + H2O
?
Substrates: substrate of EC 3.1.4.3
Products: -
Products: -
?
diheptanoylphosphatidylcholine + H2O
diheptanoylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
dihexanoylphosphatidylcholine + H2O
dihexanoylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
dimyristoylphosphatidylcholine + H2O
dimyristoylglycerol + phosphorylcholine
-
Substrates: substrate in mixed micelles with sodium deoxycholate
Products: -
Products: -
?
egg lysophosphatidylcholine + H2O
monoacylglycerol + phosphorylcholine
Substrates: 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
Products: -
Products: -
?
glycerophosphorylcholine + H2O
glycerol + phosphorylcholine
Substrates: enzyme hydrolyzes GPC efficiently, measurement of GDE activity
Products: -
Products: -
?
L-alpha-lysophosphatidylcholine + H2O
?
Substrates: substrate of EC 3.1.4.3
Products: -
Products: -
?
lysoPAF + H2O
?
Substrates: lyso platelet activating factor, partially hydrolyzed
Products: -
Products: -
?
membrane form variant surface glycoproteins + H2O
soluble variant surface glycoprotein + sn-1,2-dimyristoylglycerol
p-nitrophenyl phenylphosphate + H2O
?
Substrates: pNPPP, classical NPP substrate
Products: -
Products: -
?
p-nitrophenyl phenylphosphate + H2O
p-nitrophenol + phenylphosphate
Substrates: pNPPP, classical NPP substrate
Products: -
Products: -
?
p-nitrophenyl phosphorylcholine + H2O
?
Substrates: recombinant NPP6 efficiently hydrolyzes the classical substrate for phospholipase C
Products: -
Products: -
?
p-nitrophenyl phosphorylcholine + H2O
? + p-nitrophenol
Substrates: pNPPC, classical NPP substrate
Products: -
Products: -
?
p-nitrophenyl phosphorylcholine + H2O
p-nitrophenol + phosphorylcholine
Substrates: pNPPC, classical NPP substrate, recombinant NPP6 efficiently hydrolyzes the classical substrate for phospholipase C
Products: -
Products: -
?
p-nitrophenylphosphoryl-choline + H2O
p-nitrophenol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
-
Substrates: specific for
Products: -
Products: -
?
phosphatidic acid + H2O
1,2-sn-diacylglycerol + phosphate
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + choline phosphate
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol-4,5-bisphosphate + H2O
?
-
Substrates: less efficient substrate
Products: -
Products: -
?
platelet activating factor + H2O
?
Substrates: PAF, partially hydrolyzed
Products: -
Products: -
?
sphingosylphosphorylcholine + H2O
?
Substrates: SPC, measurement of lysoPLC activity of NPP6 toward choline-containing phospholipids
Products: -
Products: -
?
1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + H2O
1,2-dihexanoyl-sn-glycerol + phosphoethanolamine
Substrates: -
Products: -
Products: -
?
1,2-dihexanoyl-sn-glycero-3-phosphoethanolamine + H2O
1,2-dihexanoyl-sn-glycerol + phosphoethanolamine
-
Substrates: less efficient substrate
Products: -
Products: -
?
1,2-dioleoylphosphatidylethanolamine + H2O
1,2-dioleoylglycerol + phosphorylethanolamine
-
Substrates: -
Products: -
Products: -
?
1,2-dioleoylphosphatidylethanolamine + H2O
1,2-dioleoylglycerol + phosphorylethanolamine
-
Substrates: -
Products: -
Products: -
?
1,2-dipalmitoylphosphatidylcholine + H2O
1,2-dipalmitoylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
1,2-dipalmitoylphosphatidylcholine + H2O
1,2-dipalmitoylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
1,2-dipalmitoylphosphatidylcholine + H2O
1,2-dipalmitoylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
1,2-dipalmitoylphosphatidylcholine + H2O
1,2-dipalmitoylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
1,2-dipalmitoylphosphatidylcholine + H2O
1,2-dipalmitoylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
1,2-dipalmitoylphosphatidylcholine + H2O
1,2-dipalmitoylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
1-acyl-2-linoleoyl-glycerophosphocholine
?
-
Substrates: -
Products: -
Products: -
?
1-acyl-2-linoleoyl-glycerophosphocholine
?
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-acyl-glycerophosphocholine
?
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-acyl-glycerophosphocholine
?
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-linoleoyl-glycerophosphocholine
?
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-2-linoleoyl-glycerophosphocholine
?
-
Substrates: -
Products: -
Products: -
?
1-palmitoyl-lysophosphatidylcholine + H2O
1-palmitoyl-sn-glycerol + phosphorylcholine
Substrates: -
Products: -
Products: -
?
1-palmitoyl-lysophosphatidylcholine + H2O
1-palmitoyl-sn-glycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphorycholine + H2O
4-nitrophenol + phosphorylcholine
Substrates: -
Products: -
Products: -
?
4-nitrophenyl phosphorycholine + H2O
4-nitrophenol + phosphorylcholine
Substrates: -
Products: -
Products: -
?
4-nitrophenylphosphorycholine + H2O
4-nitrophenol + phosphorylcholine
Substrates: -
Products: -
Products: -
?
4-nitrophenylphosphorycholine + H2O
4-nitrophenol + phosphorylcholine
Bacillus cereus HSL3
Substrates: -
Products: -
Products: -
?
4-nitrophenylphosphorycholine + H2O
4-nitrophenol + phosphorylcholine
Substrates: -
Products: -
Products: -
?
4-nitrophenylphosphorycholine + H2O
4-nitrophenol + phosphorylcholine
Substrates: -
Products: -
Products: -
?
4-nitrophenylphosphorylcholine + H2O
4-nitrophenol + phosphorylcholine
Substrates: -
Products: -
Products: -
?
4-nitrophenylphosphorylcholine + H2O
4-nitrophenol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
4-nitrophenylphosphorylcholine + H2O
4-nitrophenol + phosphorylcholine
Substrates: -
Products: -
Products: -
?
cardiolipin + H2O
phosphatidylglycerophosphate + 1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
cardiolipin + H2O
phosphatidylglycerophosphate + 1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
diacylglycerylphosphoryl monomethylethanolamine + H2O
?
-
Substrates: -
Products: -
Products: -
?
diacylglycerylphosphoryl monomethylethanolamine + H2O
?
-
Substrates: -
Products: -
Products: -
?
lysophosphatidylcholine + H2O
monoacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
lysophosphatidylcholine + H2O
monoacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
lysophosphatidylcholine + H2O
monoacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
lysophosphatidylcholine + H2O
monoacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
lysophosphatidylcholine + H2O
monoacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
lysophosphatidylcholine + H2O
monoacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
lysophosphatidylcholine + H2O
monoacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
membrane form variant surface glycoproteins + H2O
soluble variant surface glycoprotein + sn-1,2-dimyristoylglycerol
-
Substrates: -
Products: -
Products: -
?
membrane form variant surface glycoproteins + H2O
soluble variant surface glycoprotein + sn-1,2-dimyristoylglycerol
-
Substrates: -
Products: -
Products: -
?
p-nitrophenylphosphorylcholine + H2O
p-nitrophenol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
p-nitrophenylphosphorylcholine + H2O
p-nitrophenol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
p-nitrophenylphosphorylcholine + H2O
p-nitrophenol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
p-nitrophenylphosphorylcholine + H2O
p-nitrophenol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
p-nitrophenylphosphorylcholine + H2O
p-nitrophenol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
p-nitrophenylphosphorylcholine + H2O
p-nitrophenol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidic acid + H2O
?
-
Substrates: 9.04% of the activity with phosphatidylcholine
Products: -
Products: -
?
phosphatidic acid + H2O
?
-
Substrates: 9.04% of the activity with phosphatidylcholine
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: preferred substrate
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
Clostridium welchii
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: substrate from egg yolk
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: nonhemolytic PLC
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: hemolytic PLC
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: phosphatidylcholine and sphingomyelin are cleaved at equal rate
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
Substrates: substrate from egg yolk
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
Substrates: the enzyme shows cell-associated phosphatidylcholine-specific phospholipase C activity in vivo
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
Substrates: the enzyme shows cell-associated phosphatidylcholine-specific phospholipase C activity in vivo
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
?
Substrates: the phosphatidylcholinesterase activity of the enzyme is five-fold higher than the sphingomyelinase C activity
Products: -
Products: -
?
phosphatidylcholine + H2O
?
Substrates: the phosphatidylcholinesterase activity of the enzyme is five-fold higher than the sphingomyelinase C activity
Products: -
Products: -
?
phosphatidylcholine + H2O
?
Substrates: both PC and SM bind to a similar location of the phosphate-interacting and active sites residues
Products: -
Products: -
?
phosphatidylcholine + H2O
?
Substrates: both PC and SM bind to a similar location of the phosphate-interacting and active sites residues
Products: -
Products: -
?
phosphatidylethanolamine + H2O
1,2-diacyl-sn-glycerol + ethanolamine phosphate
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
1,2-diacyl-sn-glycerol + ethanolamine phosphate
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
1,2-diacyl-sn-glycerol + phosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
1,2-diacyl-sn-glycerol + phosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
1,2-sn-diacylglycerol + phosphoethanolamine
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
1,2-sn-diacylglycerol + phosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
1,2-sn-diacylglycerol + phosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + 1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + 1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + 1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
phosphorylethanolamine + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylglycerol + H2O
1,2-diacylglycerol + sn-glycerol-3-phosphate
-
Substrates: -
Products: -
Products: -
?
phosphatidylglycerol + H2O
1,2-diacylglycerol + sn-glycerol-3-phosphate
-
Substrates: -
Products: -
Products: -
?
phosphatidylglycerol + H2O
1,2-sn-diacylglycerol + sn-glycerol-3-phosphate
Substrates: -
Products: -
Products: -
?
phosphatidylglycerol + H2O
1,2-sn-diacylglycerol + sn-glycerol-3-phosphate
Substrates: -
Products: -
Products: -
?
phosphatidylinositol + H2O
1,2-sn-diacylglycerol + phosphoinositol
Substrates: -
Products: -
Products: -
?
phosphatidylinositol + H2O
1,2-sn-diacylglycerol + phosphoinositol
Substrates: -
Products: -
Products: -
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
-
Substrates: Ca2+-dependent activity
Products: -
Products: -
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol + H2O
inositol monophosphate + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol 4,5-bisphosphate + H2O
inositol 4,5-bisphosphate + phosphatidate
-
Substrates: Ca2+-independent activity
Products: -
Products: -
?
phosphatidylinositol 4,5-bisphosphate + H2O
inositol 4,5-bisphosphate + phosphatidate
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol 4,5-bisphosphate + H2O
inositol 4,5-bisphosphate + phosphatidate
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylserine + H2O
phosphorylserine + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylserine + H2O
phosphorylserine + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylserine + H2O
phosphorylserine + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylserine + H2O
phosphorylserine + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylserine + H2O
phosphorylserine + diacylglycerol
-
Substrates: nonhemolytic PLC
Products: -
Products: -
?
phosphatidylserine + H2O
phosphorylserine + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylserine + H2O
phosphorylserine + diacylglycerol
-
Substrates: -
Products: -
Products: -
?
sphingomyelin + H2O
ceramide + phosphocholine
-
Substrates: about 70% activity compared to 1,2-dioleoyl-sn-glycero-3-phosphocholine
Products: -
Products: -
?
sphingomyelin + H2O
ceramide + phosphocholine
-
Substrates: -
Products: -
Products: -
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
Substrates: when substrate is presented in a biological membrane, for example in the human red cell membrane or myelin sheath
Products: -
Products: -
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
sphingomyelin + H2O
ceramide + phosphorylcholine
Substrates: -
Products: -
Products: -
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
Substrates: hemolytic PLC
Products: -
Products: -
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
Substrates: phosphatidylcholine and sphingomyelin are cleaved at equal rate
Products: -
Products: -
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
-
Substrates: -
Products: -
Products: -
?
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
-
Substrates: -
Products: -
Products: -
?
sphingomyelin + H2O
N-acylsphingosine + choline phosphate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: PLCBC also catalyzes the hydrolysis of phosphatidylethanolamine and phosphatidylserine but with lower efficiency
Products: -
Products: -
?
additional information
?
-
-
Substrates: modeling of active site and reaction mechanism, development of two different reaction mechanism models, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme is not haemolytic for human erythrocytes and not involved in multinucleated giant cell formation or induction of apoptotic cell death
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is not haemolytic for human erythrocytes and not involved in multinucleated giant cell formation or induction of apoptotic cell death
Products: -
Products: -
?
additional information
?
-
-
Substrates: the release of Ca2+ from the intracellular calcium stores after application of ATP or carbachol is mediated by phospholipase C
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoform PC-PLC and reactive oxygen species are involved in chicken blastodisc differentiation to vascular endothelial cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoform PC-PLC plays an important role in regulating CD16 receptor membrane expression, the CD16-mediated cytolytic mechanism and CD16-triggered signal transduction
Products: -
Products: -
?
additional information
?
-
Substrates: release of nucleoside 5'-monophosphate from a variety of nucleotides and nucleotide derivatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: release of nucleoside 5'-monophosphate from a variety of nucleotides and nucleotide derivatives
Products: -
Products: -
?
additional information
?
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant enzyme hydrolyzes a broad phospholipid spectrum, including phosphatidylcholine, phosphatidylglycerol, and phosphatidylinositol, broad substrate preference
Products: -
Products: -
?
additional information
?
-
-
Substrates: the recombinant enzyme hydrolyzes a broad phospholipid spectrum, including phosphatidylcholine, phosphatidylglycerol, and phosphatidylinositol, broad substrate preference
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant enzyme hydrolyzes a broad phospholipid spectrum, including phosphatidylcholine, phosphatidylglycerol, and phosphatidylinositol, broad substrate preference
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme induces membrane fusion
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with phosphatidylinositol
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme induces membrane fusion
Products: -
Products: -
?
additional information
?
-
Substrates: release nucleoside 5'-monophosphate from a variety of nucleotides and nucleotide derivatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays a key role in the pathogenesis of bacterial infection
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays a key role in the pathogenesis of bacterial infection
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays a key role in the pathogenesis of bacterial infection
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays a key role in the pathogenesis of bacterial infection
Products: -
Products: -
?
additional information
?
-
-
Substrates: phospholipase C hydrolyzes phosphatidylethanolamine and phosphatidylcholine but not other glycerophospholipids
Products: -
Products: -
?
additional information
?
-
-
Substrates: phospholipase C hydrolyzes phosphatidylethanolamine and phosphatidylcholine but not other glycerophospholipids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme, when injected intradermally into the skin of sheep, elicits histopathological lesions virtually identical to that seen in naturally occuring fleecerot
Products: -
Products: -
?
additional information
?
-
-
Substrates: phospholipase C causes platelet aggregation in a concentration-dependent manner
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: phospholipase C plays a role in pathogenesis of infections by Pseudomonas aeruginosa
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme activity is necessary for PLC-induced inflammation
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: phosphatidylethanolamine, sphingomyelin, phosphatidylinositol and phosphatidylserine are hydrolyzed at less than 1% of the activity with phosphatidylcholine
Products: -
Products: -
?
additional information
?
-
-
Substrates: phosphatidylethanolamine, sphingomyelin, phosphatidylinositol and phosphatidylserine are hydrolyzed at less than 1% of the activity with phosphatidylcholine
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme induces cell cycle progression, overexpression of enzyme induces overexpression of cyclin D3
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is regulated through redox- and calcium-dependent manners in alveolar macrophage
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: interaction between PC-PLC and cell division cycle 20 homologue, Cdc20, initiating the degradation of PC-PLC by Cdc20-mediated ubiquitin proteasome pathway
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme prefers mixed micelle substrates to liposomal substrates. The rate-limiting steps of hydrolysis of mixed micelle 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine and emulsified lysophosphatidylcholine are the bulk step and the surface step, respectively
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme completely removes phosphatidylcholine and phosphatidylethanolamine from crude soybean oil at 80 °C
Products: -
Products: -
-
additional information
?
-
-
Substrates: mPC-PLC may play a role in the intercellular multiplication of Uronema marinum
Products: -
Products: -
?
additional information
?
-
-
Substrates: cPC-PLC may contribute to the parasite evasion against the host immune response
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with phosphatidylinositol and phosphatidylethanolamine
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-diacyl-sn-glycero-3-phosphatide + H2O
1,2-diacylglycerol + phosphate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenylphosphorylcholine + H2O
4-nitrophenol + phosphorylcholine
Substrates: -
Products: -
Products: -
?
membrane form variant surface glycoproteins + H2O
soluble variant surface glycoprotein + sn-1,2-dimyristoylglycerol
phosphatidylethanolamine + H2O
1,2-diacyl-sn-glycerol + phosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
membrane form variant surface glycoproteins + H2O
soluble variant surface glycoprotein + sn-1,2-dimyristoylglycerol
-
Substrates: -
Products: -
Products: -
?
membrane form variant surface glycoproteins + H2O
soluble variant surface glycoprotein + sn-1,2-dimyristoylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + choline phosphate
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: preferred substrate
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacyl-sn-glycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
Clostridium welchii
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-diacylglycerol + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
Substrates: the enzyme shows cell-associated phosphatidylcholine-specific phospholipase C activity in vivo
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
Substrates: the enzyme shows cell-associated phosphatidylcholine-specific phospholipase C activity in vivo
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylcholine + H2O
1,2-sn-diacylglycerol + phosphocholine
-
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
1,2-sn-diacylglycerol + phosphoethanolamine
Substrates: -
Products: -
Products: -
?
phosphatidylethanolamine + H2O
1,2-sn-diacylglycerol + phosphoethanolamine
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
phosphatidylinositol-bisphosphate + H2O
inositol 1,4,5-trisphosphate + 1,2-diacylglycerol
-
Substrates: -
Products: -
Products: -
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
sphingomyelin + H2O
ceramide + phosphorylcholine
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: PLCBC also catalyzes the hydrolysis of phosphatidylethanolamine and phosphatidylserine but with lower efficiency
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme is not haemolytic for human erythrocytes and not involved in multinucleated giant cell formation or induction of apoptotic cell death
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is not haemolytic for human erythrocytes and not involved in multinucleated giant cell formation or induction of apoptotic cell death
Products: -
Products: -
?
additional information
?
-
-
Substrates: the release of Ca2+ from the intracellular calcium stores after application of ATP or carbachol is mediated by phospholipase C
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoform PC-PLC and reactive oxygen species are involved in chicken blastodisc differentiation to vascular endothelial cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoform PC-PLC plays an important role in regulating CD16 receptor membrane expression, the CD16-mediated cytolytic mechanism and CD16-triggered signal transduction
Products: -
Products: -
?
additional information
?
-
Substrates: release of nucleoside 5'-monophosphate from a variety of nucleotides and nucleotide derivatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: release of nucleoside 5'-monophosphate from a variety of nucleotides and nucleotide derivatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme induces membrane fusion
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme induces membrane fusion
Products: -
Products: -
?
additional information
?
-
Substrates: release nucleoside 5'-monophosphate from a variety of nucleotides and nucleotide derivatives
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays a key role in the pathogenesis of bacterial infection
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays a key role in the pathogenesis of bacterial infection
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays a key role in the pathogenesis of bacterial infection
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays a key role in the pathogenesis of bacterial infection
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme, when injected intradermally into the skin of sheep, elicits histopathological lesions virtually identical to that seen in naturally occuring fleecerot
Products: -
Products: -
?
additional information
?
-
-
Substrates: phospholipase C causes platelet aggregation in a concentration-dependent manner
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: phospholipase C plays a role in pathogenesis of infections by Pseudomonas aeruginosa
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme activity is necessary for PLC-induced inflammation
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme induces cell cycle progression, overexpression of enzyme induces overexpression of cyclin D3
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is regulated through redox- and calcium-dependent manners in alveolar macrophage
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: interaction between PC-PLC and cell division cycle 20 homologue, Cdc20, initiating the degradation of PC-PLC by Cdc20-mediated ubiquitin proteasome pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: mPC-PLC may play a role in the intercellular multiplication of Uronema marinum
Products: -
Products: -
?
additional information
?
-
-
Substrates: cPC-PLC may contribute to the parasite evasion against the host immune response
Products: -
Products: -
?
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
Ba2+
Ca2+
Co2+
Fe2+
Fe3+
K+
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
Co2+
-
restores activity after o-phenanthroline-treatment
Mg2+
-
restores ability of Ca2+-inhibited PLC to hydrolyse sphingomyelin
Mn2+
-
restores activity after o-phenanthroline-treatment
Zn2+
-
phospholipase C is a trinuclear zinc enzyme, structure analysis, using also the crystal structure from PDB entry 1AH7, overview
Zn2+
zinc metalloenzyme, contains three essential Zn2+ in its N-terminal domain
Zn2+
-
zinc-dependent enzyme. His216 is required for coordinate binding of zinc
Zn2+
-
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
-
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.
INHIBITOR
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
Isopropanol
30% (v/v), 86.4% inhibition to % of control
methyl 5-[[(2-hydroxyphenyl)methyl]amino]-2-(morpholin-4-yl)benzoate
-
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
acetonitrile
30% (v/v), 70.3% inhibition to % of control
Al3+
-
Al3+-mediated plasma membrane rigidity decreases the enzyme activity
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
tricyclodecan-9-yl-xanthogenate
-
inhibition is associated with decrease of enzyme exposed on cell surface and accumulation of cytoplasmic enzyme in Golgi region; preincubation of NK cells with a PC-PLC inhibitor, tricyclodecan-9-yl-xanthogenate, strongly reduced NK-mediated cytotoxicity
-
tricyclodecan-9-yl-xanthogenate
-
i.e. D609, a specific inhibitor, significantly suppresses the (S)-3-methyl-2-phenyl-N-(1-phenylpropyl)-4-quinolinecarboxamide-induced current in type I nNOS neurons
-
tricyclodecan-9-yl-xanthogenate
-
i.e. D609, specific inhibitor, does not inhibit sphingomyelin synthase
-
tricyclodecan-9-yl-xanthogenate
-
i.e. D609, a specific inhibitor, prevents the development of acute hypoxic pulmonary hypertension in rats, and also inhibits pulmonary vasoconstriction induced with a generator of superoxide anions LY83583, but not the one induced with hydrogen peroxide
-
tricyclodecan-9-ylxanthogenate
i.e. D609; i.e. D609; i.e. D609; i.e. D609; i.e. D609; i.e. D609
tricyclodecan-9-ylxanthogenate
-
i.e. D609, a rather selective PC-PLC inhibitor
Triton X-100
30% (v/v), 68.5% inhibition to % of control
U-73122
-
inhibition of enzyme in single myocytes by 0.005 mM completely blocks rises in Ca2+ concentration induced by both carbachol and ATP
U-73122
PLC antagonist, abolishes all PLC activities of eggs ,blocks fertilization-induced egg activation; general PLC antagonist, abolishes all PLC activities of eggs, blocks fertilization-induced egg activation
additional information
-
PC-PLCBc inhibition is not due to the interaction of compounds with the phospholipase catalytic zinc atoms, but rather results from the inhibitor cationic group recognition by the PCPLCBc amino acids involved in choline lipid binding. Inhibitor design based on 2-aminohydroxamic acid PC-PLCBc inhibitors that block the enzyme by coordination of the zinc active site atoms present in PC-PLCBc, overview
-
additional information
-
excess diacylglycerol at pH 7.5 at approximately 12% inhibits the membrane fusion activity of the enzyme
-
additional information
U-73343, has no effect on egg activation; U-73343, has no effect on egg activation
-
additional information
U-73343, has no effect on egg activation; U-73343, has no effect on egg activation
-
additional information
-
no effect on activity by monosialic ganglioside GM3 and phospholipids
-
additional information
-
inhibition of enzyme leads to inhibition of IL-2 induced proliferation of cells
-
additional information
the catalytic activity of NPP6 toward p-nitrophenyl phosphorylcholine is partially inhibited by the divalent cations. Attempts are unsuccessful to recover the activity of EDTA treated NPP6 by adding various divalent cations
-
additional information
-
the catalytic activity of NPP6 toward p-nitrophenyl phosphorylcholine is partially inhibited by the divalent cations. Attempts are unsuccessful to recover the activity of EDTA treated NPP6 by adding various divalent cations
-
additional information
the enzymatic activity can be specifically inhibited by its propeptide added in trans
-
additional information
-
no inhibition by tricyclodecan-9-ylxanthogenate, i.e. D609
-
additional information
-
the recombinant enzyme is resistant to 20 mM CHAPS or 20 mM Triton X-100
-
additional information
-
no inhibition of enzymatic activity by Ca2+, inhibits haemolytic activity of the enzyme
-
additional information
-
inhibition of phosphatidylcholine-specific phospholipase C prevents the inhibition of gap junctional intercellular communication by 1-methylanthracene
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cholesterol
-
phospholipase C is enhanced by cholesterol and by lipids with an intrinsic negative curvature, e.g. phosphatidylethanolamine
guanine nucleotide-binding regulatory protein Gh
-
stimulating only in presence of GTPgammaS, lowers required Ca2+ concentration
-
guanine nucleotide-binding regulatory protein Ghalpha
-
stimulation in presence of aluminium fluoride, lowers required Ca2+ concentration
-
moxonidine
-
incubation of CHO cells stably expressing human imidazoline receptor antisera-selected protein IRAS for 5 min can induce an upregulation of isoform PC-PLC activity and an increase in the accumulation of reaction product diacylglycerol
phosphatidylethanolamine
-
phospholipase C is enhanced by cholesterol and by lipids with an intrinsic negative curvature, e.g. phosphatidylethanolamine
rilmenidine
-
incubation of CHO cells stably expressing human imidazoline receptor antisera-selected protein IRAS for 5 min can induce an upregulation of isoform PC-PLC activity and an increase in the accumulation of reaction product diacylglycerol
silica particle
-
enzyme activity in macrophage increases significantly upon exposure to silica particles. Increase in activity is inhibited by Mn(III)tetrakis(4-benzoic acid)porphyrin chloride
-
dimethyl sulfoxide
30% (v/v), activation to 133.4% of control
guanine nucleotide-binding protein G16alpha
-
subunit of cell surface receptor associated G-protein, PLC-beta 1, -beta 2 and -beta 3, half-maximal concentration needed for activation is 1nM, stimulating only in presence of GTP gamma S
-
guanine nucleotide-binding protein G16alpha
-
subunit of cell surface receptor associated G-protein, PLC-beta 1, -beta 2 and -beta 3, half-maximal concentration needed for activation is 1nM, stimulating only in presence of GTP gamma S
-
sodium deoxycholate
-
at concentrations up to 0.83mg/ml, optimal molar ratio of sodium deoxycholate to lecithin: 0.5
subunit of cell surface receptor associated G-protein
-
Gqa, subunit of cell surface receptor associated G-protein, PLC d1
-
subunit of cell surface receptor associated G-protein
-
Gqa, subunit of cell surface receptor associated G-protein, PLC d1
-
Triton X-100
in the presence of 0.05-0.5% and 0.1-0.2% (wt/vol) Triton X-100, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine and choline plasmalogen are efficiently hydrolyzed, respectively. Hydrolysis of lysophosphatidylcholine and choline lysoplasmalogen does not require Triton X-100, the hydrolytic activity is inhibited by more than 0.05% (wt/vol) Triton X-100
additional information
-
no effect on activity by monosialic ganglioside GM3 and phospholipids
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.271
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine
pH 5.0, 37°C
additional information
additional information
-
kinetic parameters depend on the physicochemical properties of substrate aggregates. Larger micelles with a ratio bile salt/lipid smaller than 5 show higher activity and shorter steady state duration of less than 4 min, smaller micelles with a ratio bile salt/lipid greater than 5 show lower activity and longer steady state of about 10 min
-
0.32
4-nitrophenylphosphorycholine
37°C, pH 7.2, wild-type enzyme
-
0.76
4-nitrophenylphosphorycholine
37°C, pH 7.2, mutant enzyme F96R/Q153P
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4000
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine
pH 5.0, 37°C
155
4-nitrophenylphosphorycholine
37°C, pH 7.2, wild-type enzyme
-
872
4-nitrophenylphosphorycholine
37°C, pH 7.2, mutant enzyme F96R/Q153P
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14800
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine
pH 5.0, 37°C
488
4-nitrophenylphosphorycholine
37°C, pH 7.2, wild-type enzyme
-
1155
4-nitrophenylphosphorycholine
37°C, pH 7.2, mutant enzyme F96R/Q153P
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.012
1-[hydroxy[2-(trimethylammonio)ethyl]amino]-1-oxododecan-2-aminium
-
pH and temperature not specified in the publication
0.026
1-[hydroxy[3-(trimethylammonio)propyl]amino]-1-oxododecan-2-aminium
-
pH and temperature not specified in the publication
0.0025
3-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]dodecanoyl]amino]-N,N,N-trimethylpropan-1-aminium
-
pH and temperature not specified in the publication
0.0025
tert-butyl (1-[(benzyloxy)[3-(dimethylamino)propyl]amino]-1-oxododecan-2-yl)carbamate
-
pH and temperature not specified in the publication
0.0064
tricyclodecan-9-yl-xanthogenate
pH and temperature not specified in the publication
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
1-[(benzyloxy)[2-(trimethylammonio)ethyl]amino]-1-oxododecan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.004
1-[(benzyloxy)[2-(trimethylammonio)ethyl]amino]-1-oxohexadecan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.004
1-[(benzyloxy)[2-(trimethylammonio)ethyl]amino]-1-oxoicosan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.032
1-[(benzyloxy)[3-(dimethylammonio)propyl]amino]-1-oxododecan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.05
1-[(benzyloxy)[3-(trimethylammonio)propyl]amino]-1-oxododecan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.1
1-[(benzyloxy)[3-(trimethylammonio)propyl]amino]-1-oxooctan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.04
1-[hydroxy[2-(trimethylammonio)ethyl]amino]-1-oxododecan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.002
1-[hydroxy[2-(trimethylammonio)ethyl]amino]-1-oxohexadecan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.004
1-[hydroxy[2-(trimethylammonio)ethyl]amino]-1-oxoicosan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.5
1-[hydroxy[2-(trimethylammonio)ethyl]amino]-1-oxooctan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.058
1-[hydroxy[3-(trimethylammonio)propyl]amino]-1-oxododecan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.1
1-[[3-(dimethylammonio)propyl](hydroxy)amino]-1-oxododecan-2-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.005
2-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]dodecanoyl]amino]-N,N,N-trimethylethanaminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.002
2-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]hexadecanoyl]amino]-N,N,N-trimethylethanaminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.003
2-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]icosanoyl]amino]-N,N,N-trimethylethanaminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.056
2-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]octanoyl]amino]-N,N,N-trimethylethanaminium
Bacillus cereus
-
pH and temperature not specified in the publication
1.97
2-[[4-(morpholin-4-yl)anilino]methyl]phenol
Bacillus cereus
pH 7.3, 37°C, one-phase system
0.004
3-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]dodecanoyl]amino]-N,N,N-trimethylpropan-1-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
0.078
3-[(benzyloxy)[2-[(tert-butoxycarbonyl)amino]octanoyl]amino]-N,N,N-trimethylpropan-1-aminium
Bacillus cereus
-
pH and temperature not specified in the publication
2.4
3-[[4-(morpholin-4-yl)anilino]methyl]phenol
Bacillus cereus
pH 7.3, 37°C, one-phase system
0.008
tert-butyl (1-[(benzyloxy)[3-(dimethylamino)propyl]amino]-1-oxododecan-2-yl)carbamate
Bacillus cereus
-
pH and temperature not specified in the publication
0.077
tert-butyl (1-[(benzyloxy)[3-(dimethylamino)propyl]amino]-1-oxooctan-2-yl)carbamate
Bacillus cereus
-
pH and temperature not specified in the publication
0.7
5-[[(2-fluorophenyl)methyl]amino]-2-(morpholin-4-yl)benzoic acid
Bacillus cereus
pH 7.3, 37°C, one-phase system
1.64
5-[[(2-fluorophenyl)methyl]amino]-2-(morpholin-4-yl)benzoic acid
Bacillus cereus
pH 7.3, 37°C, two-phase system
0.43
methyl 5-[[(2-fluorophenyl)methyl]amino]-2-(morpholin-4-yl)benzoate
Bacillus cereus
pH 7.3, 37°C, one-phase system
1.2
methyl 5-[[(2-fluorophenyl)methyl]amino]-2-(morpholin-4-yl)benzoate
Bacillus cereus
pH 7.3, 37°C, two-phase system
0.36
methyl 5-[[(2-hydroxyphenyl)methyl]amino]-2-(morpholin-4-yl)benzoate
Bacillus cereus
pH 7.3, 37°C, one-phase system
1.15
methyl 5-[[(2-hydroxyphenyl)methyl]amino]-2-(morpholin-4-yl)benzoate
Bacillus cereus
pH 7.3, 37°C, two-phase system
0.17
O-(octahydro-1H-4,7-methanoinden-5-yl) hydrogen carbonodithioate
Bacillus cereus
pH 7.3, 37°C, one-phase system
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1268
-
substrate: phosphatidylinositol-4,5-bisphosphate, PLC d1 with poly-His-tail, no significant change of activity after cleavage of poly-His-tail, expression at 16°C for 72 h
404
-
substrate: phosphatidylinositol-4,5-bisphosphate, PLC d3 with poly-His-tail, no significant change of activity after cleavage of poly-His-tail, expression at 16°C for 72 h
additional information
additional information
-
assay of enzyme in presence of organic solvent, two-phase-system
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
7 - 8
7.5
7.5 - 8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 7
-
pH 4.5: about 60% of maximal activity, pH 7.0: about 60% of maximal activity, mPC-PLC
5.5 - 7
pH 5.5: about 45% of maximal activity, pH 7.0: about 50% of maximal activity
6.5 - 7.5
-
pH 6.5: about 65% of maximal activity, pH 7.5: about 80% of maximal activity, cPC-PLC
6.5 - 8.5
-
pH 6.5: about 50% of maximal activity, pH 8.5: about 50% of maximal activity
7 - 9
pH 7.0: about 40% of maximal activity, pH 9.0: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
50
additional information
additional information
comparison of the secreted hemolytic activities of MFN1032 and the plcC mutants at various growth temperatures
additional information
-
comparison of the secreted hemolytic activities of MFN1032 and the plcC mutants at various growth temperatures
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 45
15°C: about 65% of maximal activity, 45°C: about 65% of maximal activity
25 - 70
25°C: about 50% of maximal activity, 70°C: about 65% of maximal activity
35 - 60
-
35°C: about 50% of maximal activity, 60°C: about 50% of maximal activity
60 - 90
60°C: about 55% of maximal activity, 90°C: about 50% of maximal activity, wild-type enzyme
70 - 100
70°C: about 60% of maximal activity, 100°C: about 25% of maximal activity, mutant enzyme F96R/Q153P
80 - 90
substrate: 4-nitrophenylphosphorylcholine, similar enzymatic activity at 80, 85, and 90 °C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.4
6.7
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme, displays activities of EC 3.1.4.3 and EC 3.1.4.4
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
isoforms phosphatidylcholine-specific phospholipase C, i.e. PC-PLC, and phosphatidylinositol-specific phospholipase C, i.e. PI-PLC
-
-
brenda
glutamate decarboxylase 67-green fluorescent protein, GAD67-GFP, knock-in mice
-
-
brenda
-
-
-
brenda
isoform PlcHR2, bifunctional phospholipase C and sphingomyelinase
-
-
brenda
phospholipase C production by urinary tract isolates is significantly greater than that by lung, blood, or other isolates
-
-
brenda
recombinant enzyme, production in Schizosaccharomyces pombe
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
in vitro vasculogenesis model. Activities of both Ca2+-dependent and independent isoform PC-PLC and the level of reactive oxygen species are elevated during the endothelial differentiation of the blastodisc. Ca2+-independent PC-PLC undergoes an increase in 24 h, then decreases gradually with the cell differentiation, while Ca2+-dependent PC-PLC is almost not changed during the process
brenda
-
a rat hepatoma cell line established from N-nitrosodiethyla-mine-induced Wistar rat hepatoma
brenda
-
stably expressing human imidazoline receptor antisera-selected protein IRAS
brenda
-
different cell lines of epithelial ovarian cancer cells (EOC) compared with nontumoral (normal or immortalized) counterparts (EONT)
brenda
-
substantial intracellular amounts of isoform PC-PLC in all lymphoid subsets
brenda
segment-specific expression pattern of NPP6 in nephrons shown
brenda
-
isoforms NPC1a, NPC1b, NPC4 and NPC6, expanded leaf
brenda
additional information
-
suppression of isoform PC-PLC inhibits apoptosis in young cells, but not in senescent cells, and depresses reactive oxygen species levels in both young and senescent cells
brenda
-
monocyte-derived macrophage, enzyme is activated by HIV-1 R5 gp120 interaction with CCR5 and is required for NF-kB-mediated chemokine CCL2 production triggered by R5 gp120
brenda
-
suppression of isoform PC-PLC in presence of basic fibroblast growth factor can induce neuronal differentiation accompanied by increase in viability of differentiated cells. The resting membrane potential of the differentiated cells gradually decreases, but the mitochondrial membrane potential rises with increasing inhibition time
brenda
-
high level of enzyme expression on the outer membrane surface. Identification of two subsets of cells, CD56dimPC-PLCbright and CD56brightPC-PLClow/-, corresponding to distinct subsets with cytolytic and immunoregulatory function. Enzyme expression level on the membrane closely correlates with that of the CD16 receptor
brenda
higher in seedling hypocotyls and lower in seedling roots
brenda
additional information
-
overlapping expression pattern of NPC genes in root, stem, leaf, flower, and silique
brenda
additional information
-
no detection of enzyme expression on CD4+ and CD8+ T lymphocytes
brenda
additional information
no expression of NPP6 detectable in heart, stomach, placenta, intestine, and leukocyte
brenda
additional information
-
no expression of NPP6 detectable in heart, stomach, placenta, intestine, and leukocyte
brenda
additional information
no expression of NPP6 detectable in Modulla oblongata and uterus
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
after activation by IL-2, cytoplasmic enzyme translocates to outer cell surface, mechanism
brenda
-
colocalization of PC-PLC with the ER, mainly within the Golgi apparatus in NK-resting cells. A much more extended colocalization of PC-PLC with the ER marker is observed in NK-activated cells, in which the enzyme is not exclusively confined to the Golgi region
brenda
-
brenda
-
colocalization of PC-PLC with the ER, mainly within the Golgi apparatus in NK-resting cells. A much more extended colocalization of PC-PLC with the ER marker is observed in NK-activated cells, in which the enzyme is not exclusively confined to the Golgi region
brenda
-
brenda
-
brenda
additional information
-
after activation by IL-2, cytoplasmic enzyme translocates to outer cell surface, mechanism
brenda
-
IL-2-dependent distribution between cytoplasm and ectoplasmic membrane surface in human NK cells
brenda
-
-
-
brenda
IVB Dot/Icm secretion type. The secreted enzyme activity depends upon an intact type II secretion system
-
brenda
-
IVB Dot/Icm secretion type. The secreted enzyme activity depends upon an intact type II secretion system
-
-
brenda
-
high level of enzyme expression on the outer membrane surface of natural killer cells. Enzyme expression level on the membrane closely correlates with that of the CD16 receptor
brenda
-
ectoplasmic, IL-2-dependent distribution between cytoplasm and ectoplasmic membrane surface in human NK cells
brenda
-
brenda
-
association of isoform PC-PLC with CD16 receptor, partial accumulation of both in lipid rafts. Antibody-mediated CD16 cross-linking results in an about twofold increase in PC-PLC enzyme activity within 10 min
brenda
-
deoxycholic acid induces both Ca2+ release from internal stores and persistent Ca2+ entry at the plasma membrane. The increased Ca2+ entry stimulates vigorous recruitment of conventional protein kinase C isoforms to the plasma membrane
brenda
additional information
-
epifluorescence, CLSM, and flow cytometry experiments demonstrate that PC-PLC is expressed both in cytoplasmic compartments and on the outer cell surface of either resting or activated NK cells
-
brenda
additional information
the enzyme sequence contains no signal peptide
-
brenda
additional information
-
the enzyme sequence contains no signal peptide
-
brenda
additional information
-
the enzyme sequence contains no signal peptide
-
-
brenda
additional information
-
phosphatidylcholine phospholipase C compartmentalization and enzymatic activity is regulated by a 24-amino-acid propeptide, Cys28-Ser51. During intracytosolic multiplication, bacteria accumulate the proform of PC-PLC at their membrane-cell-wall interface, whereas during cell-to-cell spread vacuolar acidification leads to maturation and rapid translocation of PCPLC across the cell wall in a manner that is dependent on Mpl, the metalloprotease of Listeria
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
evolution
malfunction
metabolism
physiological function
additional information
drug target
-
the enzyme can be a potential and new therapeutic target for epilepsy, and pharmacological manipulation of specific PLC isoform may prove therapeutically fruitful in the treatment of epilepsy
drug target
-
the enzyme could be an anticancer target, a potential drug target to treat cardiovascular diseases, or a potential neurotherapeutic target
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 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
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
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
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
-
the enzyme is linked to the progression of many pathological conditions, including cancer, atherosclerosis, inflammation and neuronal cell death
malfunction
deletion of AaPLC1 leads to the decrease of appressorium formation and infected hyphae. The degree of reduction varies between the different types of waxes, with the strongest response to pear wax. AaPLC1 mutation causes pleiotropic effects on fungal biological function, including growth deficiency, changes in stress tolerance, weakening of pathogenicity to the host, as well as destruction of mycotoxin synthesis
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
-
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
-
metabolism
-
membrane lipid formation, turnover, and recycling in Sinorhizobium meliloti, 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
-
(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
-
model of metabolism regulation carried out by plant cell phospholipases, overview
metabolism
-
model of metabolism regulation carried out by plant cell phospholipases, 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
-
the enzyme acts as a negative regulator in abscisic acid and brassinolide signaling pathways
metabolism
-
the enzyme is critically involved in multiple aspects of GABAergic functions
metabolism
the enzyme plays a pivotal role in hydrolyzing phospholipids, releasing diacylglycerol an essential second messenger
metabolism
-
the enzyme that catalyzes the formation of the important secondary messengers phosphocholine and diacylglycerol from phosphatidylcholine
metabolism
the enzyme hydrolyzes major membrane phospholipids to release diacylglycerol, a potent lipid-derived messenger regulating cell functions
metabolism
the enzyme that catalyzes the formation of the important secondary messengers phosphocholine and diacylglycerol from phosphatidylcholine
metabolism
phosphatidylinositol 4,5-bisphosphate level is regulated by cholesterol via PLC1 expression in the brain. High-cholesterol diet decreases the level of phosphatidylinositol 4,5-bisphosphate by enhancing the expression of phospholipase C (PLCbeta1) in rat brain
metabolism
-
the enzyme plays a pivotal role in hydrolyzing phospholipids, releasing diacylglycerol an essential second messenger
-
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
PLCbeta is probably not involved in egg activation
physiological function
PLC activity from eggs contributes to Chaetopterus egg activation and PLCgamma may play an important role during this biological process
physiological function
-
PC-PLC is an important enzyme that plays a key role in a variety of cellular events and lipid homoeostases
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
-
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
-
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
-
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
-
at least one PC-PLC is a plant signaling enzyme in brassinolide signal transduction and, as shown earlier, in elicitor signal transduction
physiological function
-
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 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 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
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
-
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
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
-
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'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
-
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
-
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
-
the enzyme is critical for (N-formyl-Met-Leu-Phe + cytochalasin B)-stimulated eosinophil leukotriene synthesis and degranulation. It likely plays a key role in cellular signaling, including the eosinophilic allergic inflammatory response
physiological function
-
the enzyme confers lipid-mediated signaling during the salt stress response. Downregulation of GlNPC3 expression by virus-induced gene silencing in G. littoralis reduces the expression levels of some stress-related genes, such as SnRK2, P5SC5, TPC1, and SOS1. GlNPC3 and GlNPC3-mediated membrane lipid change play a positive role in the response of Glehnia littoralis to a saline environment
physiological function
-
key enzyme in the intracellular signaling pathway. It regulates various neuronal functions including neuronal development, synaptic transmission, and plasticity in the brain
physiological function
-
the major phospholipase C enzymes are highly expressed in the brain, including PLCbeta and PLCgamma, are directly and indirectly linked to epileptogenesis
physiological function
fundamental roles in plant growth and development
physiological function
two major virulence factors, broad-range phospholipase C (LmPC-PLC) and the pore-forming toxin listeriolysin (LLO), enable the Listeria monocytogenes to spread in the host by destroying cell membranes. The phospholipase activity of LmPC-PLC facilitates the pore-forming activity of LLO and affects themorphology of LLO oligomerization on lipidmembranes, revealing the multifaceted synergy of the two virulence factors
physiological function
phospholipase C genes differentially regulate the growth, stress response, pathogenicity, and secondary metabolism of Alternaria alternata
physiological function
AaPLC2 has some effects on stress response and mycotoxin production
physiological function
AaPLC3 has some effects on stress response and mycotoxin production
physiological function
role of the bacterial enzyme in pathogenesis. The enzyme (LmPlcB) is activated when Listeria monocytogenes reaches the acidic environment of late endosomes-lysosomes, aiding bacterial escape toward the cytosol and cell-to cell propagation
physiological function
role of the bacterial enzyme in pathogenesis. When Clostridium perfringens reaches a certain density in soft tissues and the enzyme (CpPLC) is produced, this toxin induces endothelial damage and platelet aggregation, which favors ischemia, thus providing an optimal environment for bacterial growth
physiological function
-
the enzyme is not mitogenic for murine mesenteric lymph node cells but synergizes with interleukin 2 in inducing a strong proliferative response
physiological function
role of the bacterial enzyme in pathogenesis. PaPlcH secreted by Pseudomonas aeruginosa, hydrolyzes target phospholipids where the infection is being established, helps bacteria to obtain substrates from the host, and triggers signaling pathways that lead to inflammation
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
-
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
-
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
-
role of the bacterial enzyme in pathogenesis. When Clostridium perfringens reaches a certain density in soft tissues and the enzyme (CpPLC) is produced, this toxin induces endothelial damage and platelet aggregation, which favors ischemia, thus providing an optimal environment for bacterial growth
-
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
-
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
-
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
-
role of the bacterial enzyme in pathogenesis. PaPlcH secreted by Pseudomonas aeruginosa, hydrolyzes target phospholipids where the infection is being established, helps bacteria to obtain substrates from the host, and triggers signaling pathways that lead to inflammation
-
physiological function
-
two major virulence factors, broad-range phospholipase C (LmPC-PLC) and the pore-forming toxin listeriolysin (LLO), enable the Listeria monocytogenes to spread in the host by destroying cell membranes. The phospholipase activity of LmPC-PLC facilitates the pore-forming activity of LLO and affects themorphology of LLO oligomerization on lipidmembranes, revealing the multifaceted synergy of the two virulence factors
-
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
-
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
-
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
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 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
-
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
development and optimisation of a matrix assisted laser desorption ionisation time-of-flight (MALDI-TOF) mass spectrometry-based assay to monitor phosphatidylcholine-specific phospholipase C activity
additional information
the Rap1A GTPase activates PLCepsilon at the perinuclear membrane. Activation of PLCepsilon by the Gbetagamma heterodimer at multiple membranes
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
-
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
-
Show AA Sequence and Transmembrane Helices (6661 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
150000
23000
28500
35000
38000
40000
-
two PC-PLC isoforms, 40 and 66 kDa. The same PC-PLC isoforms are also detected in some leukemia cells, such as K562 and DAUDI. In U937 cells only the 40 kDa isoform is detected
66000
72800
-
x * 72800, truncated recombinant protein with His6-tag, SDS-PAGE
78000
66000
-
two PC-PLC isoforms, 40 and 66 kDa. The same PC-PLC isoforms are also detected in some leukemia cells, such as K562 and DAUDI
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
oligomer
polymer
additional information
dimer
2 * 28000, SDS-PAGE, presence of monomers, dimers and higher order oligomers (with impaired enzymatic activity)
dimer
-
2 * 28000, SDS-PAGE, presence of monomers, dimers and higher order oligomers (with impaired enzymatic activity)
-
monomer
1 * 28000, SDS-PAGE, presence of monomers, dimers and higher order oligomers (with impaired enzymatic activity)
monomer
-
1 * 28000, SDS-PAGE, presence of monomers, dimers and higher order oligomers (with impaired enzymatic activity)
-
oligomer
x * 28000, SDS-PAGE, presence of monomers, dimers and higher order oligomers (with impaired enzymatic activity)
oligomer
-
x * 28000, SDS-PAGE, presence of monomers, dimers and higher order oligomers (with impaired enzymatic activity)
-
polymer
-
identical subunits of 31000-43000 Da, gel filtration, SDS-PAGE, multiple forms
polymer
-
identical subunits of 31000-43000 Da, gel filtration, SDS-PAGE, multiple forms
-
additional information
the enzyme contains a central phosphoesterase domain, a DUF756 domain, a conserved region and a conserved Asp-Arg pair, and some isozymes contain a signal peptide, domain structure, overview
additional information
the enzyme contains a central phosphoesterase domain, a DUF756 domain, a conserved region and a conserved Asp-Arg pair, and some isozymes contain a signal peptide, domain structure, overview
additional information
the enzyme contains a central phosphoesterase domain, a DUF756 domain, a conserved region and a conserved Asp-Arg pair, and some isozymes contain a signal peptide, domain structure, overview
additional information
the enzyme contains a central phosphoesterase domain, a DUF756 domain, a conserved region and a conserved Asp-Arg pair, and some isozymes contain a signal peptide, domain structure, overview
additional information
the enzyme contains a central phosphoesterase domain, a DUF756 domain, a conserved region and a conserved Asp-Arg pair, and some isozymes contain a signal peptide, domain structure, overview
additional information
the enzyme contains a central phosphoesterase domain, a DUF756 domain, a conserved region and a conserved Asp-Arg pair, and some isozymes contain a signal peptide, domain structure, overview
additional information
-
secondary and tertiary structure analysis of the enzyme at different pH values from pH 2.0-7.5, overview
additional information
-
the enzyme contains a central phosphoesterase domain, a DUF756 domain, a conserved region and a conserved Asp-Arg pair, and some isozymes contain a signal peptide, domain structure, overview
additional information
-
physical association of isoform PC-PLC with CD16 receptor, partial accumulation of both in lipid rafts
additional information
-
the enzyme contains a central phosphoesterase domain, a DUF756 domain, a conserved region and a conserved Asp-Arg pair, and some isozymes contain a signal peptide, domain structure, overview
additional information
-
the enzyme contains a central phosphoesterase domain, a DUF756 domain, a conserved region and a conserved Asp-Arg pair, and some isozymes contain a signal peptide, domain structure, overview
additional information
-
the enzyme contains a central phosphoesterase domain, a DUF756 domain, a conserved region and a conserved Asp-Arg pair, and some isozymes contain a signal peptide, domain structure, overview
additional information
-
the enzyme contains a central phosphoesterase domain, a DUF756 domain, a conserved region and a conserved Asp-Arg pair, and some isozymes contain a signal peptide, domain structure, overview
additional information
-
the enzyme contains a central phosphoesterase domain, a DUF756 domain, a conserved region and a conserved Asp-Arg pair, and some isozymes contain a signal peptide, domain structure, overview
additional information
-
the enzyme contains a central phosphoesterase domain, a DUF756 domain, a conserved region and a conserved Asp-Arg pair, and some isozymes contain a signal peptide, domain structure, overview
additional information
-
the enzyme contains a central phosphoesterase domain, a DUF756 domain, a conserved region and a conserved Asp-Arg pair, and some isozymes contain a signal peptide, domain structure, overview
additional information
-
the enzyme contains a central phosphoesterase domain, a DUF756 domain, a conserved region and a conserved Asp-Arg pair, and some isozymes contain a signal peptide, domain structure, overview
additional information
-
the enzyme contains a central phosphoesterase domain, a DUF756 domain, a conserved region and a conserved Asp-Arg pair, and some isozymes contain a signal peptide, domain structure, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
serine-phosphorylation of enzyme after treatment with IL-2, phosphorylation is abolished after MAPK inhibition
proteolytic modification
proteolytic modification
sequence shows a mature polypeptide of 700 amino acids plus a signal peptide of 34 amino acids
proteolytic modification
sequence shows a mature polypeptide of 705 amino acids plus a signal peptide of 35 amino acids
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion method at 18 °C, crystal structure is determined at a resolution of 2.1 A
2.1 A resolution for phosphate inhibited PLC, 2.8 A resolution for iodide and iodate-inhibited PLC, R-factor of 20.3%
-
crystal structure of a complex between the enzyme and a competitive inhibitor. 1.9 A resolution, R-factor of 15.7%
-
crystallized in space group P212121 with two molecules, molA and molB, in the asymmetric unit, whose structures are determined at 2 A resolution
sitting drop vapor diffusion technique at 16°C, 2.5 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E430A
mutation reduces activity to about 35% of wild-type activity
F431N
mutation reduces activity to about 25% of wild-type activity
I437N
mutation reduces activity to about 90% of wild-type activity
M438N
mutation reduces activity to about 15% of wild-type activity
N176A
mutation reduces activity to about 20% of wild-type activity
N176A/E430A
mutation reduces activity to about 30% of wild-type activity
up
the enzyme is induced by 24-epibrassinolide signalling, auxin, cytokinin, phosphate deficiency, abscisic acid, and salt stress. NPC4 does demonstrate a positive response to Botrytis cinerea, Golovinomyces orontii, Pseudomonas syringae and Phytophthora infestans treatment
W252A
mutation reduces activity to about 45% of wild-type activity
F66W
F66Y
-
the mutant enzyme can remove up to 90% of phosphatidylethanolamine while retaining its efficiency at hydrolyzing phosphatidylcholine
F96R/Q153P
compared to the wild-type enzyme, the mutant enzyme exhibits significantly improved thermal properties, including higher temperature optima (90°C) and better thermal stability. It displays 4.94 times kcat and 2.37 times kcat/Km as much as the wild-type, as well as improved substrate adaptability
F96R/Q153P
Bacillus cereus HSL3
-
compared to the wild-type enzyme, the mutant enzyme exhibits significantly improved thermal properties, including higher temperature optima (90°C) and better thermal stability. It displays 4.94 times kcat and 2.37 times kcat/Km as much as the wild-type, as well as improved substrate adaptability
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more |
isoform Plc-2 inactivation mutant shows decreased extracellular enzyme activity. Plc-2 is involved in plaque formationand has a significant role in host cell cytotoxicity
D293S
-
reduced hemolytic activity, reduced cytotoxic and myotoxic activities, reduced activity against p-nitrophenylphosphorylcholine, increased dependence on Ca2+
D305G
-
reduced hemolytic activity, reduced cytotoxic and myotoxic activities, significantly increased activity against p-nitrophenylphosphorylcholine
H148G
-
pretreatment of the inactive mutant H148G losing PLC and SMase activities does not affect the production of NO and tumor necrosis factor-alpha in lipopolysaccharide-stimulated RAW264.7 cells
K330E
-
reduced hemolytic activity, reduced cytotoxic and myotoxic activities
hNPP6-ex
truncated form of hNPP6, cDNA for the extracellular domain of hNPP6, amino acids 1-421
D251V
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
D314V
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
D63V
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
E286A
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
F167A
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
F244A
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
F253A
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
H166N
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
H179N
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
H247N
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
H257N
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
H284N
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
H409N
site-directed mutagenesis, the mutant enzyme shows similar catalytic activity as the wild-type enzyme
R265Q
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
R326Q
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
R365Q
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
S336A
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
Y156A
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
D63V
-
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
-
F167A
-
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
-
H166N
-
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
-
Y156A
-
site-directed mutagenesis, the mutant enzyme shows reduced catalytic activity compared to the wild-type enzyme
-
C143S
-
the mutant shows increased activity compared to the wild type enzyme
C168S
-
the mutant shows decreased activity compared to the wild type enzyme
C28A/C29A/D30A
-
site-directed mutagenesis, the mutation has no effect on PC-PLC maturation
D30A/E31A
-
site-directed mutagenesis, the mutation decreases the efficacy of PC-PLC processing to 75% of wild-type level
E31A
-
site-directed mutagenesis, the mutation has no effect on PC-PLC maturation
E31A/Y32A/L33A
-
site-directed mutagenesis, the mutation decreases the efficacy of PC-PLC processing to 42% of wild-type level
H56Y
-
the activity of the mutant is comparable to the wild type enzyme
L33A
-
site-directed mutagenesis, the mutation decreases the efficacy of PC-PLC processing to 54% of wild-type level
P36A
-
site-directed mutagenesis, the mutation decreases the efficacy of PC-PLC processing to 82% of wild-type level
Q34A/T35A
-
site-directed mutagenesis, the mutation has no effect on PC-PLC maturation
Q34A/T35A/P36A
-
site-directed mutagenesis, the mutation decreases the efficacy of PC-PLC processing to 79% of wild-type level
Q34K/T35P
-
site-directed mutagenesis, the mutation has no effect on PC-PLC maturation
Y32A
-
site-directed mutagenesis, the mutation decreases the efficacy of PC-PLC processing to 68% of wild-type level
mNPP6-ex
truncated form of hNPP6, cDNA for the extracellular domain of mNPP6 with Myc tag at the carboxyl terminus
T178A
-
site-directed mutagenesis, hydrolytically inactive mutant. The PlcHR 2 T178A mutant is also unable to induce vesicle aggregation or release intravesicular aqueous contents in contrast to the wild-type enzyme
additional information
F66W
-
the mutant enzyme can remove up to 90% of phosphatidylethanolamine while retaining its efficiency at hydrolyzing phosphatidylcholine
additional information
-
amino acid sequence differs from that of strain SBUG516 by substitution D173E
additional information
-
amino acid sequence differs from that of strain SBUG516 by substitution E173D
additional information
-
amino acid sequence differs from that of strain SBUG516 by substitution D173E
-
additional information
-
amino acid sequence differs from that of strain SBUG516 by substitution E173D
-
additional information
-
amino acid sequence differs from that of strain SBUG516 by substitution D173E
-
additional information
-
amino acid sequence differs from that of strain SBUG516 by substitution E173D
-
additional information
isoform Plc-1 inactivation mutant shows decreased extracellular enzyme activity. Plc-1 has no effect on plaque-forming efficinecy, but increases the efficiency of isoform Plc-2 to form plaques
additional information
-
isoform Plc-1 inactivation mutant shows decreased extracellular enzyme activity. Plc-1 has no effect on plaque-forming efficinecy, but increases the efficiency of isoform Plc-2 to form plaques
additional information
-
separate expression of amino- and C-terminal fragments of enzyme, requirements for reconstitution of enzyme activity and activation by Gbetagamma
additional information
construction of enzyme knock-out mutants, of PlcC alone, or double PlcC/PlcA or PlcC/PlcB and triple PlcC/PlcA/PlcB mutants. Complementation of plcC knock-out mutants with wild-type plcC in trans restores the cell-associated enzyme activity defect
additional information
-
construction of enzyme knock-out mutants, of PlcC alone, or double PlcC/PlcA or PlcC/PlcB and triple PlcC/PlcA/PlcB mutants. Complementation of plcC knock-out mutants with wild-type plcC in trans restores the cell-associated enzyme activity defect
additional information
-
construction of enzyme knock-out mutants, of PlcC alone, or double PlcC/PlcA or PlcC/PlcB and triple PlcC/PlcA/PlcB mutants. Complementation of plcC knock-out mutants with wild-type plcC in trans restores the cell-associated enzyme activity defect
-
additional information
-
construction and generation of PC-PLC propeptide deletion mutants
additional information
plcC-deficient mutants to determine whether PlcC contributes to the hemolytic activity of MFN1032. Construction of a plcC-overexpressing MFN1032 clone: MFN1036
additional information
-
plcC-deficient mutants to determine whether PlcC contributes to the hemolytic activity of MFN1032. Construction of a plcC-overexpressing MFN1032 clone: MFN1036
additional information
-
construction of a series of fragments, N-terminal Gbetagamma binding region in first 180 amino acids of enzyme, amino acids 150-180 are required for interaction with Gbetagamma, mutations in this region reduce binding capacity and ability to be activated by Gbetagamma
additional information
-
overexpression of enzyme induces overexpression of cyclin D3
additional information
-
generation of a SMc00171-deficient mutant, which is inactive with phosphatidylcholine. SMc00171 restores phosphatidylcholine and phosphatidylethanolamine degradation in a smc00171-deficient mutant
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
20
-
pH values between 5.0-9.0, stable for 2 hours, pH values between 6.0-7.0, 95% of activity remains after 24 hours
24
-
for 60 min, recombinant PLC delta 1 and delta 3 with poly-His-tail, no loss of activity
37
45
50
70
76
-
for 6 min, with 0.1 mM free Zn2+: loss of 21% of activity, without Zn2+: loss of 63% of activity
95
100
-
for 5 min, in 2 M guanidinium chloride, no loss of activity after dialysis against Zn2+-containing buffer
100
-
almost complete restoration of activity of enzyme deactivated at 60-70°C
37
-
for 30 min, recombinant PLC delta 1 and delta 3 with poly-His-tail, no loss of activity
95
50 h, the enzyme keeps a significant fraction of secondary structure
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1,10-phenanthroline, denaturation
activity is unaffected by treatment with 0.1% solutions of trypsin, deoxyribonuclease and ribonuclease
-
guanidinium chloride, denaturation at a concentration of 1-2 M, reversible by free Zn2+
-
sodium dodecyl sulfate
sodium dodecyl sulfate, enzyme resistant to denaturation in presence of 1 mM Zn2+
-
the enzyme is unstable, it can be stabilized by addition of sorbitol to 60% w/w in 25 mM Tris/HCl buffer, pH 7.2
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
chloroform
-
assay of enzyme in presence of organic solvent, two-phase-system
diethyl ether
ethyl alcohol
diethyl ether
-
assay of enzyme in presence of organic solvent, two-phase-system
ethyl alcohol
-
inhibitory at concentrations above 2%
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or 4°C, 0.3 M triethanolamine or 0.05 M Tris-HCl, pH 7, stable for up to 12 months
-
-20°C, buffer B, purified recombinant PLC d1 and d3 with poly-His-tail, activity stable over 2 years, more than 15 freeze/thaw cycles between -20°C and 4°C reduce activity by 10-20%
-
-20°C, in barbital-buffered saline, pH 7.4, 1 mM ZnSO4, stable for more than one year
-
-20°C, in Na2B4O7/HCl buffer, pH 7.5, 40% glycerol, no loss of activity after 6 months
-
-20°C, more than 1-2 mg purified enzyme/ml, stable for at least 3 months
-
-70°C, buffer containing 5% glycerol and 0,1% sucrose monolaureate, stable for less than 2 weeks
-
-80C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography, gel filtration, 2500fold purification from culture filtrate
-
ammonium sulfate fractionation, ion-exchange chromatography, affinity chromatography, greater than 99% pure, 94fold
-
ammonium sulfate precipitation and chitin resin column chromatography
-
ammonium sulfate precipitation, ethanol precipitate, protamine sulfate supernatant, gel filtration, ion-exchange chromatography, 450fold, approximately 98% pure
-
C-1and C-2: dialysis, isoelectric focusing and column chromatography, C-1: 1510foldfold, C-2: 1330fold, both to homogeneity
-
gel filtration, ion-exchange chromatography, 3645fold, apparently pure
-
ion-exchange chromatography, fractionation by manganous chloride, ammonium sulfate precipitation steps
-
method for production of recombinant enzyme in Schizosaccharomyces pombe
-
mono Q ion exchange chromatography column and eluted with a linear gradient of NaCl (0-2 M) using the deltaKTA system
partial
purification of Gh-PLC complex, gel filtration, ion-exchange chromatography
-
recombinant PLC d1 and D3 with poly-His-tail at the amino terminus, metal ion affinity chromatography
-
recombinant PLC d1 and D3 without poly-His-tail at the amino terminus, cation exchange HPLC and phosphocellulose chromatography
-
recombinant PLC-beta 1a 58fold, recombinant PLC-beta 1b 47fold, HPLC, affinity chromatography, reverse phase chromatography
-
mono Q ion exchange chromatography column and eluted with a linear gradient of NaCl (0-2 M) using the deltaKTA system
mono Q ion exchange chromatography column and eluted with a linear gradient of NaCl (0-2 M) using the deltaKTA system
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coexpressed in Pichia pastoris with molecular chaperone PDI (protein disulfide isomerases)
expression in Escherichia coli
expression in Escherichia coli. Overexpression of GlNPC3 in Arabidopsis thaliana increases salt tolerance compared to wild-type plants. GlNPC3-overexpressing plants have longer roots and higher fresh and dry masses under the salt treatment
-
gene lpg0012 or plcC, DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21, subcloning in Escherichia coli strain DH5alpha. Expression of Strep-tagged enzyme mutants H179N and S336A does not yield any detectable protein
mpcA and mpcB are individually cloned in Mycobacterium smegmatis
PCR product cloned using the original TA cloning Kit, subcloned into the pCR2.1 vector
phylogenetic analysis
production of the recombinant protein in Escherichia coli is no more successful because of frequent inclusion bodies and accumulation of inactive phospholipase C in the periplasmic space
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of gene NPC4 in root tips is highly induced by NaCl, maximum expression from 3 h to 6 h after the salt treatment dependent on salt concentration
isoforms NPC1a and NPC1b are up-regulated under the treatments of low-phosphate and salt, up-regulated at 1 h and 2 h but then down-regulated under the drought treatment. Under abscisic acid treatment, isoforms NPC1a, NPC2a, NPC2b, NPC3a and NPC3b are up-regulated. Expression of isoforms NPC4, NPC6a and NPC6b is up-regulated under salt treatment. Isoforms NPC6a, NPC6b, NPC6c, and NPC6d are up-regulated at the beginning but then down-regulated under drought treatment
-
isoforms PLCG1 and PLCG2 expression increase at approximately 1-6 h post-lipopolysaccharide injection
-
the enzyme expression is induced by drought, salt, cold, dark, abscisic acid, brassinolide, methyl jasmonate, and gibberellic acid treatments
-
the enzyme is induced by 24-epibrassinolide signalling, auxin, and cytokinin. Expression level of NPC3 is increased 14.6fold after 2 h in seedlings subjected to 37°C heat stress. NPC3 does demonstrate a positive response to Botrytis cinerea, Golovinomyces orontii, Pseudomonas syringae and Phytophthora infestans treatment
the enzyme is induced by phosphate deficiency
the enzyme is upregulated during infection of Acanthamoeba castellanii amoebae and macrophages
under abscisic acid treatment, isoforms NPC1b, NPC6a and NPC6b are down-regulated. Isoforms NPC2a, NPC2b, NPC6a, NPC6b, NPC6c and NPC6d are down-regulated under the treatments of low-phosphate and salt. Isoforms NPC3a and GhNPC3b are both down-regulated under salt treatment. Expression of isoform NPC4 is down-regulated under drought treatment
-
expression of gene NPC4 in root tips is highly induced by NaCl, maximum expression from 3 h to 6 h after the salt treatment dependent on salt concentration
expression of gene NPC4 in root tips is highly induced by NaCl, maximum expression from 3 h to 6 h after the salt treatment dependent on salt concentration
-
-
the enzyme is upregulated during infection of Acanthamoeba castellanii amoebae and macrophages
the enzyme is upregulated during infection of Acanthamoeba castellanii amoebae and macrophages
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
guanidinium chloride causes denaturation at a concentration of 1-2 M, reversible by free Zn2+
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
drug development
-
elucidation of the mechanisms responsible for aberrant phosphatidylcholine metabolism in cancer cells may allow identification of novel biomarkers of tumor progression and design of new targeted anticancer therapies
food industry
medicine
pharmacology
-
phospholipase C is considered to be one of key enzymes for the design of drug delivery system using the endocytosis route, because PLC can catalyze the membrane fusion between cell membranes and phospholipid vehicles (liposomes)
analysis
-
synthesis of fluorogenic analogue of phosphatidylcholine 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, and use as direct substrate for real-time measurement of enzyme activity. Substrate for both phospholipases C and D and lysophospholipase D, no substrate for Bacillus cereus PI-PLC or Clostridium perfringens PC-PLC
analysis
enzymatic measurement of choline plasmalogen using PLD684 and phospholipase B
food industry
-
the enzyme is used in vegetable oil refining by enzymatic phospholipid removal (degumming )
food industry
the enzyme is a candidate for industrial-scale enzymatic oil degumming at high temperatures
food industry
the enzyme may possess great potential in crude oil refining industry. It reduces the phosphorus of crude soybean oil by 93.3%
food industry
the enzyme is a candidate in oil refining industry. The application of the enzyme (TtPLC) in crude soybean oil degumming process significantly reduces the residual phosphorus content from 135.4 mg/kg to 7.9 mg/kg
food industry
facilitated by its excellent thermal properties, F96R/Q153P shows great potential application in food processing industries such as enzymatic degumming under extreme high temperatur
food industry
-
the enzyme is a candidate in oil refining industry. The application of the enzyme (TtPLC) in crude soybean oil degumming process significantly reduces the residual phosphorus content from 135.4 mg/kg to 7.9 mg/kg
-
food industry
Bacillus cereus HSL3
-
facilitated by its excellent thermal properties, F96R/Q153P shows great potential application in food processing industries such as enzymatic degumming under extreme high temperatur
-
medicine
-
inactivation of thromboplastin, potential therapeutic value in cases of intravascular coagulation
medicine
-
isoform PC-PLC plays a critical role in the silica-associated inflammatory response of alveolar macrophage
medicine
-
tumor suppressor PTEN is involved in both phospholipase C and phospholipase D activation pathways. Pathogenesis of Cowden syndrome and Bannayan-Riley-Ruvalcaba syndrome has further aspects beyond activating the PI3K pathway
medicine
-
chemokine CCL2, i.e. MCP-1, enhances HIV-1 replication. Enzyme isoform PC-PLC is activated by HIV-1 R5 gp120 interaction with CCR5 and is required for NF-kB-mediated CCL2 production triggered by R5 gp120 in monocyte-derived macrophages
EXTERNAL LINKS (specific for EC-Number 3.1.4.3)
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Release 2026.1 (March 2026)
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