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Information on EC 3.1.4.38 - glycerophosphocholine cholinephosphodiesterase
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3.1.4.38 glycerophosphocholine cholinephosphodiesteraseIUBMB Comments
No activity on sn-3-glycerophosphoethanolamine.
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Word Map
- 3.1.4.38
- lysophosphatidylcholine
- spla2-v
- lysophospholipids
-
3.1.4.2
-
arachidonic
- diagnostics
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
glycerophosphocholine cholinephosphodiesterase, glycerophosphocholine choline phosphodiesterase, gpc-cpde, l-3-glycerylphosphinicocholine cholinephosphohydrolase, gpc-cp, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alkaline lysosphingomyelinase
Co2+-glycerophosphocholine cholinphosphodiesterase
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-
-
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glycerophosphocholine choline phosphodiesterase
glycosylphosphatidylinositol-anchored alkaline hydrolase
GPC-CP
GPC-CP14
GPC-Cpde
GPI-anchored alkaline hydrolase
L-3-glycerylphosphinicocholine cholinephosphohydrolase
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-
-
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p-nitrophenylphosphocholine cholinphosphodiesterase
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-
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Zn2+-glycerophosphocholine cholinphosphodiesterase
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-
-
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Zn2+-GPC cholinphosphodiesterase
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sn-glycero-3-phosphocholine + H2O = glycerol + phosphocholine
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-
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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-
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SYSTEMATIC NAME
IUBMB Comments
sn-glycero-3-phosphocholine cholinephosphohydrolase
No activity on sn-3-glycerophosphoethanolamine.
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CAS REGISTRY NUMBER
COMMENTARY
60063-78-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
sn-glycerol-3-phosphoethanolamine + H2O
glycerol + phosphoethanolamine
high activity
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-
?
lysophosphatidylcholine + H2O
?
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first leaving group is acylglycerol, second is phosphocholine
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-
?
lysophosphatidylcholine + H2O
?
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first leaving group is acylglycerol, second is phosphocholine
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-
?
lysophosphatidylcholine + H2O
choline + 2-lysophosphatidate
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-
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?
lysosphingomyelin + H2O
?
-
best substrate of the soluble isozyme sGPC-Cpde. First leaving group is sphingosin, second is phosphocholine
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-
?
lysosphingomyelin + H2O
?
-
best substrate of the soluble isozyme sGPC-Cpde
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-
?
lysosphingomyelin + H2O
?
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best substrate of the soluble isozyme sGPC-Cpde. First leaving group is sphingosin, second is phosphocholine
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-
?
p-nitrophenylphosphocholine + H2O
p-nitrophenol + choline phosphate
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-
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r
p-nitrophenylphosphocholine + H2O
p-nitrophenol + choline phosphate
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-
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r
p-nitrophenylphosphocholine + H2O
p-nitrophenol + choline phosphate
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-
-
-
?
sn-glycero-3-phosphocholine + H2O
glycerol + choline phosphate
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-
-
-
r
sn-glycero-3-phosphocholine + H2O
glycerol + phosphocholine
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first leaving group is glycerol, second is phosphocholine
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-
?
sn-glycero-3-phosphocholine + H2O
glycerol + phosphocholine
the choline moiety of glycero-3-phosphocholine is incorporated into phosphocholine in an ENPP6-dependent manner both in vivo and in vitro
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-
?
sn-glycero-3-phosphocholine + H2O
glycerol + phosphocholine
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-
-
?
sn-glycero-3-phosphocholine + H2O
glycerol + phosphocholine
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-
-
?
sn-glycerol-3-phosphate + H2O
glycerol + phosphate
lower activity
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-
?
sn-glycerol-3-phosphate + H2O
glycerol + phosphate
lower activity
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-
?
sn-glycerol-3-phosphocholine + H2O
glycerol + phosphocholine
best substrate
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-
?
sn-glycerol-3-phosphocholine + H2O
glycerol + phosphocholine
best substrate
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-
?
additional information
?
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the soluble isozyme sGPC-Cpde is specific for lysosphingomyelin, displaying 1 to 2 orders of magnitude higher catalytic activity than towards sn-glycero-3-phosphocholine and lysophosphatidylcholine
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?
additional information
?
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the soluble isozyme sGPC-Cpde is specific for lysosphingomyelin, displaying 1 to 2 orders of magnitude higher catalytic activity than towards sn-glycero-3-phosphocholine and lysophosphatidylcholine
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-
?
additional information
?
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substrate specificity, overview. The enzyme exhibits specificity toward glycerol-3-phosphocholine and glycerol-3-phosphoethanolamine and hydrolyzes glycerol-3-phosphate and lysophosphatidylcholine. The enzyme shows no activity toward any diacylglycerophospholipids and little activity toward other glycerol-3-phosphodiesters and lysophospholipids, no activity with sn-glycerol-3-phosphoserine, L-alpha-lysophosphatidylinositol, L-alpha-lysophosphatidylserine, L-alpha-lysophosphatidylglycerol, 1,2-dipalmitoyl-sn-glycero-3-phosphocholine, 1,2-dimyristoyl-snglycero-3-phosphate, 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-rac-(1-glycerol), L-alpha-phosphatidylinositol, sphingomyelin, beta-acetyl-gamma-sn-hexadecyl-L-alpha-phosphatidylcholine, or 1-O-1'-(Z)-octadecenyl-2-hydroxy-sn-glycero-3-phosphoethanolamine, poor activity with 1-O-1'-(Z)-octadecenyl-2-hydroxy-sn-glycero-3-phosphocholine, L-alpha-lysophosphatidylethanolamine, or 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-L-serine
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-
?
additional information
?
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substrate specificity, overview. The enzyme exhibits specificity toward glycerol-3-phosphocholine and glycerol-3-phosphoethanolamine and hydrolyzes glycerol-3-phosphate and lysophosphatidylcholine. The enzyme shows no activity toward any diacylglycerophospholipids and little activity toward other glycerol-3-phosphodiesters and lysophospholipids, no activity with sn-glycerol-3-phosphoserine, L-alpha-lysophosphatidylinositol, L-alpha-lysophosphatidylserine, L-alpha-lysophosphatidylglycerol, 1,2-dipalmitoyl-sn-glycero-3-phosphocholine, 1,2-dimyristoyl-snglycero-3-phosphate, 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-rac-(1-glycerol), L-alpha-phosphatidylinositol, sphingomyelin, beta-acetyl-gamma-sn-hexadecyl-L-alpha-phosphatidylcholine, or 1-O-1'-(Z)-octadecenyl-2-hydroxy-sn-glycero-3-phosphoethanolamine, poor activity with 1-O-1'-(Z)-octadecenyl-2-hydroxy-sn-glycero-3-phosphocholine, L-alpha-lysophosphatidylethanolamine, or 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-L-serine
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-
?
additional information
?
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substrate specificity, overview. The enzyme exhibits specificity toward glycerol-3-phosphocholine and glycerol-3-phosphoethanolamine and hydrolyzes glycerol-3-phosphate and lysophosphatidylcholine. The enzyme shows no activity toward any diacylglycerophospholipids and little activity toward other glycerol-3-phosphodiesters and lysophospholipids, no activity with sn-glycerol-3-phosphoserine, L-alpha-lysophosphatidylinositol, L-alpha-lysophosphatidylserine, L-alpha-lysophosphatidylglycerol, 1,2-dipalmitoyl-sn-glycero-3-phosphocholine, 1,2-dimyristoyl-snglycero-3-phosphate, 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-rac-(1-glycerol), L-alpha-phosphatidylinositol, sphingomyelin, beta-acetyl-gamma-sn-hexadecyl-L-alpha-phosphatidylcholine, or 1-O-1'-(Z)-octadecenyl-2-hydroxy-sn-glycero-3-phosphoethanolamine, poor activity with 1-O-1'-(Z)-octadecenyl-2-hydroxy-sn-glycero-3-phosphocholine, L-alpha-lysophosphatidylethanolamine, or 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-L-serine
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
lysophosphatidylcholine + H2O
choline + 2-lysophosphatidate
-
-
-
-
?
lysosphingomyelin + H2O
?
-
best substrate of the soluble isozyme sGPC-Cpde
-
-
?
sn-glycero-3-phosphocholine + H2O
glycerol + phosphocholine
the choline moiety of glycero-3-phosphocholine is incorporated into phosphocholine in an ENPP6-dependent manner both in vivo and in vitro
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-
?
sn-glycero-3-phosphocholine + H2O
glycerol + phosphocholine
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-
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?
sn-glycero-3-phosphocholine + H2O
glycerol + phosphocholine
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-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Cu2+
Mn2+
Zn2+
additional information
Ca2+
-
Ca2+ is required for maximum activity in brain tissues not in myelin
additional information
the enzyme is metal ion-independent, no effect by 2 mm Mg2+ and K+
additional information
-
the enzyme is metal ion-independent, no effect by 2 mm Mg2+ and K+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
HO-radical-generator
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5 mM H2O2 plus 5 mM KCl plus 0.5 units horseradish peroxidase
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additional information
no inhibition by 2 mM SDS or DTT, poor inhibition by 2 mm iodoacetamide
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additional information
-
no inhibition by 2 mM SDS or DTT, poor inhibition by 2 mm iodoacetamide
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Multiple Sclerosis
Glycerylphosphocholine phosphocholine phosphodiesterase activity is reduced in multiple sclerosis plaques.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0007
tellurium tetrachloride
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pH 10, 20°C, hydrolysis of p-nitrophenylphosphocholine
0.0015
tellurium tetrachloride
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pH 10, 20°C, hydrolysis of sn-glycero-3-phosphocholine
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.2
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purified native soluble isozyme, pH 8.0, 37°C, substrate 4-nitrophenyl phosphocholine
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9 - 11
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
two forms of brain GPC-Cpde, a membrane-linked, mGPC-Cpde, and a soluble, sGPC-Cpde
brenda
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two forms of brain GPC-Cpde, a membrane-linked, mGPC-Cpde, and a soluble, sGPC-Cpde
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brenda
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autopsy of nonaffected white matter and Multiple sclerosis plaques
brenda
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the enzyme is expressed on the myelin membrane
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brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
two forms of brain GPC-Cpde, a membrane-linked, mGPC-Cpde, and a soluble, sGPC-Cpde
brenda
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two forms of brain GPC-Cpde, a membrane-linked, mGPC-Cpde, and a soluble, sGPC-Cpde
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brenda
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two forms of brain GPC-Cpde, a membrane-linked, mGPC-Cpde, and a soluble, sGPC-Cpde. The enzyme is solubilised by C-terminal proteolysis, releasing the GPI-anchor, the resulting soluble isozyme sGPCCpde exists in two conformations, a homodimer joined by a disulfide bridge linking C414 from each monomer, and a monomer resulting from proteolysis N-terminally to this disulfide bond
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brenda
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two forms of brain GPC-Cpde, a membrane-linked, mGPC-Cpde, and a soluble, sGPC-Cpde. The enzyme is solubilised by C-terminal proteolysis, releasing the GPI-anchor, the resulting soluble isozyme sGPCCpde exists in two conformations, a homodimer joined by a disulfide bridge linking C414 from each monomer, and a monomer resulting from proteolysis N-terminally to this disulfide bond
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-
brenda
additional information
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the truncated high mannose and bisected hybrid type glycans linked to N118 and N341 of the soluble isozyme sGPC-Cpde is a hallmark of glycans in lysosomal glycoproteins, subjected to GlcNAc-1-phosphorylation en route through the Golgi apparatus. The soluble isozyme sGPC-Cpde may originate from the lysosomes, suggesting that lysosomal sorting contributes to the level of membrane isozyme mGPC-Cpde on the myelin membrane
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brenda
additional information
-
the truncated high mannose and bisected hybrid type glycans linked to N118 and N341 of the soluble isozyme sGPC-Cpde is a hallmark of glycans in lysosomal glycoproteins, subjected to GlcNAc-1-phosphorylation en route through the Golgi apparatus. The soluble isozyme sGPC-Cpde may originate from the lysosomes, suggesting that lysosomal sorting contributes to the level of membrane isozyme mGPC-Cpde on the myelin membrane
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
evolution
the enzyme may be a member of the PLC/acid phosphatase protein superfamily, and the member of a distinct family, unlike glycerophosphocholine phosphodiesterase (EC 3.1.4.2) and alkaline phosphatase (EC 3.1.3.1)