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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphocholine + H2O
4-nitrophenol + phosphocholine
-
-
-
-
?
L-alpha-lysophosphatidylcholine + H2O
?
lysophosphatidylcholine + H2O
?
lysophosphatidylcholine + H2O
choline + 2-lysophosphatidate
lysosphingomyelin + H2O
?
p-aminophenylphosphocholine + H2O
p-aminophenol + choline phosphate
-
-
-
-
?
p-nitrophenylphosphocholine + H2O
p-nitrophenol + choline phosphate
sn-glycero-3-phosphocholine + H2O
?
-
-
-
-
?
sn-glycero-3-phosphocholine + H2O
glycerol + choline phosphate
sn-glycero-3-phosphocholine + H2O
glycerol + phosphocholine
sn-glycerol-3-phosphate + H2O
glycerol + phosphate
sn-glycerol-3-phosphocholine + H2O
glycerol + phosphocholine
sn-glycerol-3-phosphoethanolamine + H2O
glycerol + phosphoethanolamine
high activity
-
-
?
additional information
?
-
L-alpha-lysophosphatidylcholine + H2O
?
-
-
-
?
L-alpha-lysophosphatidylcholine + H2O
?
-
-
-
?
lysophosphatidylcholine + H2O
?
-
first leaving group is acylglycerol, second is phosphocholine
-
-
?
lysophosphatidylcholine + H2O
?
-
first leaving group is acylglycerol, second is phosphocholine
-
-
?
lysophosphatidylcholine + H2O
choline + 2-lysophosphatidate
-
-
-
-
?
lysophosphatidylcholine + H2O
choline + 2-lysophosphatidate
-
-
-
-
?
lysosphingomyelin + H2O
?
-
best substrate of the soluble isozyme sGPC-Cpde
-
-
?
lysosphingomyelin + H2O
?
-
best substrate of the soluble isozyme sGPC-Cpde. First leaving group is sphingosin, second is phosphocholine
-
-
?
lysosphingomyelin + H2O
?
-
best substrate of the soluble isozyme sGPC-Cpde
-
-
?
lysosphingomyelin + H2O
?
-
best substrate of the soluble isozyme sGPC-Cpde. First leaving group is sphingosin, second is phosphocholine
-
-
?
p-nitrophenylphosphocholine + H2O
p-nitrophenol + choline phosphate
-
-
-
-
r
p-nitrophenylphosphocholine + H2O
p-nitrophenol + choline phosphate
-
-
-
-
?
p-nitrophenylphosphocholine + H2O
p-nitrophenol + choline phosphate
-
-
-
-
r
p-nitrophenylphosphocholine + H2O
p-nitrophenol + choline phosphate
-
-
-
-
?
sn-glycero-3-phosphocholine + H2O
glycerol + choline phosphate
-
-
-
-
r
sn-glycero-3-phosphocholine + H2O
glycerol + choline phosphate
-
-
-
-
?
sn-glycero-3-phosphocholine + H2O
glycerol + choline phosphate
-
-
-
-
r
sn-glycero-3-phosphocholine + H2O
glycerol + choline phosphate
-
-
-
-
r
sn-glycero-3-phosphocholine + H2O
glycerol + phosphocholine
-
first leaving group is glycerol, second is phosphocholine
-
-
?
sn-glycero-3-phosphocholine + H2O
glycerol + phosphocholine
-
-
-
?
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
-
-
?
sn-glycero-3-phosphocholine + H2O
glycerol + phosphocholine
-
-
-
?
sn-glycero-3-phosphocholine + H2O
glycerol + phosphocholine
-
-
-
?
sn-glycerol-3-phosphate + H2O
glycerol + phosphate
lower activity
-
-
?
sn-glycerol-3-phosphate + H2O
glycerol + phosphate
lower activity
-
-
?
sn-glycerol-3-phosphocholine + H2O
glycerol + phosphocholine
best substrate
-
-
?
sn-glycerol-3-phosphocholine + H2O
glycerol + phosphocholine
best substrate
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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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66.6
4-nitrophenyl phosphate
-
-
0.034
4-nitrophenyl phosphocholine
-
soluble isozyme, pH 8.0, 37°C
2
lysophosphatidylcholine
-
soluble isozyme, pH 8.0, 37°C
0.005
lysosphingomyelin
-
soluble isozyme, pH 8.0, 37°C
0.074
p-aminophenylphosphocholine
-
-
0.0055 - 0.33
p-nitrophenylphosphocholine
0.3
p-nitrophenylphosphorylthymidine
-
-
0.048 - 5
sn-glycero-3-phosphocholine
1.41
sn-glycerol-3-phosphocholine
pH 7.2, 37°C
0.0055
p-nitrophenylphosphocholine
-
Zn2+ is required for maximum activity
0.009 - 0.015
p-nitrophenylphosphocholine
-
-
0.016
p-nitrophenylphosphocholine
-
-
0.33
p-nitrophenylphosphocholine
-
-
0.048
sn-glycero-3-phosphocholine
-
-
0.2
sn-glycero-3-phosphocholine
-
-
2
sn-glycero-3-phosphocholine
-
-
5
sn-glycero-3-phosphocholine
-
soluble isozyme, pH 8.0, 37°C
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-
22-34% of activity
brenda
-
25% of activity
brenda
-
-
brenda
-
-
-
-
brenda
-
-
brenda
-
two forms of brain GPC-Cpde, a membrane-linked, mGPC-Cpde, and a soluble, sGPC-Cpde
brenda
-
two forms of brain GPC-Cpde, a membrane-linked, mGPC-Cpde, and a soluble, sGPC-Cpde
-
brenda
-
myelin
brenda
-
-
brenda
-
8-27% activity in microsomes
brenda
-
44-50% activity in myelin
brenda
-
myelin
brenda
-
75% of activity
brenda
-
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
-
brenda
-
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
-
-
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
-
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
-
-
brenda
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glycoprotein
-
truncated high mannose and bisected hybrid type glycans are linked to N118 and N341 of the soluble isozyme sGPC-Cpde, a hallmark of glycans in lysosomal glycoproteins, subjected to GlcNAc-1-phosphorylation en route through the Golgi apparatus. All the four N-glycosylation sites N100KS, N118GS, N341ST and N406GS in the soluble isozyme sGPC-Cpde are occupied, mainly with endo H-sensitive glycans, QTOF-MS-MS analysis
glycoprotein
-
truncated high mannose and bisected hybrid type glycans are linked to N118 and N341 of the soluble isozyme sGPC-Cpde, a hallmark of glycans in lysosomal glycoproteins, subjected to GlcNAc-1-phosphorylation en route through the Golgi apparatus. All the four N-glycosylation sites N100KS, N118GS, N341ST and N406GS in the soluble isozyme sGPC-Cpde are occupied, mainly with endo H-sensitive glycans, QTOF-MS-MS analysis
-
phosphoprotein
-
truncated high mannose and bisected hybrid type glycans are linked to N118 and N341 of the soluble isozyme sGPC-Cpde, a hallmark of glycans in lysosomal glycoproteins, subjected to GlcNAc-1-phosphorylation en route through the Golgi apparatus
phosphoprotein
-
truncated high mannose and bisected hybrid type glycans are linked to N118 and N341 of the soluble isozyme sGPC-Cpde, a hallmark of glycans in lysosomal glycoproteins, subjected to GlcNAc-1-phosphorylation en route through the Golgi apparatus
-
proteolytic modification
-
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 as 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
proteolytic modification
-
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 as 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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Abra, R.M.; Quinn, P.J.
Some characteristics of sn-glycero 3-phosphocholine diesterases from rat brain
Biochim. Biophys. Acta
431
631-639
1976
Rattus norvegicus
brenda
Abra, R.M.; Quinn, P.J.
A novel pathway for phosphatidylcholine catabolism in rat brain homogenates
Biochim. Biophys. Acta
380
436-441
1975
Rattus norvegicus
brenda
Janzen, L.; Tourtellotte, W.W.; Kanfer J.N.
Glycerylphosphocholine phosphocholine phosphodiesterase activity is reduced in multiple sclerosis plaques
Exp. Neurol.
109
243-246
1990
Homo sapiens
brenda
Sok D.E.; Kim, M.R.
Characterization of a Zn(2+)-requiring glycerophosphocholine cholinephosphodiesterase possessing p-nitrophenylphosphocholine phosphodiesterase activity
Biochem. J.
286
435-440
1992
Mus musculus
brenda
Monge, M.; Yuan, J.; Cabon, F.; Zalc, B.; Kanfer, J.N.
Glycerophosphoryl-cholinephosphocholine phosphodiesterase activity during the differentiation of glial progenitor cells
J. Neurosci. Res.
36
441-445
1993
Rattus norvegicus
brenda
Sok D.E.; Kim, M.R.
Brain myelin-bound Zn(2+)-glycerophosphocholine cholinephosphodiesterase is a glycosylphosphatidylinositol-anchored enzyme of two different molecular forms
Neurochem. Res.
19
97-103
1994
Mus musculus
brenda
Sok D.E.
Properties of a Zn(2+)-glycerophosphocholine cholinephosphodiesterase from bovine brain membranes
Neurochem. Res.
21
1193-1199
1996
Bos taurus
brenda
Lee, J.Y.; Kim, M.R.; Kim, Y.B.; Myung, P.K.; Sok, D.E.
Interaction of divalent metal ions with Zn(2+)-glycerophosphocholine cholinephosphodiesterase from ox brain
Neurochem. Res.
22
1471-1476
1997
Bos taurus
brenda
Sok, D.E.
Ascorbate-induced oxidative inactivation of Zn2+-glycerophosphocholine cholinephosphodiesterase
J. Neurochem.
70
1167-1174
1998
Bos taurus
brenda
Sok, D.E.
Active site of brain Zn2+-glycerophosphocholine cholinephosphodiesterase and regulation of enzyme activity
Neurochem. Res.
23
1061-1067
1998
Bos taurus
brenda
Lee, J.Y.; Kim, M.R.; Sok, D.E.
Release of GPI-anchored Zn2+-glycerophosphocholine cholinephosphodiesterase as an amphiphilic form from bovine brain membranes by bee venom phospholipase A2
Neurochem. Res.
24
1043-1050
1999
Bos taurus
brenda
Kanfer, J.N; McCartney, D.G.
Glycerophosphorylcholine phosphocholine phosphodiesterase activity of rat brain myelin
J. Neurosci. Res.
24
231-240
1989
Rattus norvegicus
brenda
Kanfer, J.N; McCartney, D.G.
Regional and developmental estimations of glycerophosphorylcholine phosphodiesterase activities in rat brain
Dev. Neurosci.
11
26-29
1989
Rattus norvegicus
brenda
Sok, D.E.; Kim, M.R.
Selective inhibition of Zn2+-glycerophosphocholine cholinephosphodiesterase by tellurium tetrachloride
Biochem. J.
284
641-643
1992
Mus musculus
-
brenda
Sugimori, D.; Ogasawara, J.; Okuda, K.; Murayama, K.
Purification, characterization, molecular cloning, and extracellular production of a novel bacterial glycerophosphocholine cholinephosphodiesterase from Streptomyces sanglieri
J. Biosci. Bioeng.
117
422-430
2014
no activity in Streptomyces lividans, Streptomyces sanglieri (U6C6H1), Streptomyces sanglieri, no activity in Streptomyces lividans 1326, Streptomyces sanglieri A14 (U6C6H1)
brenda
Greiner-Tollersrud, L.; Berg, T.; Stensland, H.M.; Evjen, G.; Greiner-Tollersrud, O.K.
Bovine brain myelin glycerophosphocholine choline phosphodiesterase is an alkaline lysosphingomyelinase of the eNPP-family, regulated by lysosomal sorting
Neurochem. Res.
38
300-310
2013
Bos taurus, Bos taurus Norwegian Red Cattle
brenda
Morita, J.; Kano, K.; Kato, K.; Takita, H.; Sakagami, H.; Yamamoto, Y.; Mihara, E.; Ueda, H.; Sato, T.; Tokuyama, H.; Arai, H.; Asou, H.; Takagi, J.; Ishitani, R.; Nishimasu, H.; Nureki, O.; Aoki, J.
Structure and biological function of ENPP6, a choline-specific glycerophosphodiester-phosphodiesterase
Sci. Rep.
6
20995
2016
Mus musculus (Q8BGN3)
brenda