Information on EC 3.1.4.38 - glycerophosphocholine cholinephosphodiesterase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.1.4.38
-
RECOMMENDED NAME
GeneOntology No.
glycerophosphocholine cholinephosphodiesterase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
sn-glycero-3-phosphocholine + H2O = glycerol + phosphocholine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
sn-glycero-3-phosphocholine cholinephosphohydrolase
No activity on sn-3-glycerophosphoethanolamine.
CAS REGISTRY NUMBER
COMMENTARY hide
60063-78-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
no activity in Streptomyces lividans
NBRC15675
-
-
Manually annotated by BRENDA team
no activity in Streptomyces lividans 1326
NBRC15675
-
-
Manually annotated by BRENDA team
isolation and identification, gene gpc-cp
UniProt
Manually annotated by BRENDA team
isolation and identification, gene gpc-cp
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl phosphocholine + H2O
4-nitrophenol + phosphocholine
show the reaction diagram
-
-
-
-
?
L-alpha-lysophosphatidylcholine + H2O
?
show the reaction diagram
lysophosphatidylcholine + H2O
?
show the reaction diagram
lysophosphatidylcholine + H2O
choline + 2-lysophosphatidate
show the reaction diagram
lysosphingomyelin + H2O
?
show the reaction diagram
p-aminophenylphosphocholine + H2O
p-aminophenol + choline phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenylphosphocholine + H2O
p-nitrophenol + choline phosphate
show the reaction diagram
sn-glycero-3-phosphocholine + H2O
?
show the reaction diagram
-
-
-
-
-
sn-glycero-3-phosphocholine + H2O
glycerol + choline phosphate
show the reaction diagram
sn-glycero-3-phosphocholine + H2O
glycerol + phosphocholine
show the reaction diagram
sn-glycerol-3-phosphate + H2O
glycerol + phosphate
show the reaction diagram
sn-glycerol-3-phosphocholine + H2O
glycerol + phosphocholine
show the reaction diagram
sn-glycerol-3-phosphoethanolamine + H2O
glycerol + phosphoethanolamine
show the reaction diagram
high activity
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
lysophosphatidylcholine + H2O
choline + 2-lysophosphatidate
show the reaction diagram
lysosphingomyelin + H2O
?
show the reaction diagram
sn-glycero-3-phosphocholine + H2O
?
show the reaction diagram
-
-
-
-
-
sn-glycero-3-phosphocholine + H2O
glycerol + phosphocholine
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Na+
11% activation at 2 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
-
3-mercaptobutanol
-
-
3-morpholinosydnonimine
-
-
ascorbate
-
oxidative inactivation of the Zn2+ -enzyme
carnitine
-
-
choline
-
competitive inhibitor
Co2+
80.6% inhibition at 2 mM
Cu2+
complete inhibition at 2 mM
cysteamine
-
-
dipropionylphosphatidylcholine
-
-
Fe2+
49.4% inhibition at 2 mM
hexyl-beta-glucoside
-
-
HO-radical-generator
-
5 mM H2O2 plus 5 mM KCl plus 0.5 units horseradish peroxidase
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Mn2+
20.5% inhibition at 2 mM
p-nitrophenylphosphate
-
competitive inhibitor
p-Nitrophenylphosphorylcholine
-
competitive inhibitor
phosphocholine
-
-
PMSF
21.2% inhibition at 2 mM
tellurite
-
inhibitory effect is greater on the Zn2+ -enzyme
tellurium tetrachloride
-
potent competitive inhibitor
Tetranitromethane
-
-
thiocholine
-
inhibitory effect is greater on the Co2+ -enzyme
thioglycerol
-
-
Zn2+
99.6% inhibition at 2 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
EDTA
13% activation at 2 mM
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
-
-
66.6
p-nitrophenylphosphate
-
-
0.0055 - 0.33
p-nitrophenylphosphocholine
0.3
p-nitrophenylthymidine
-
-
-
0.048 - 5
sn-glycero-3-phosphocholine
1.41
sn-glycerol-3-phosphocholine
pH 7.2, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
4-nitrophenyl phosphocholine
-
soluble isozyme, pH 8.0, 37°C
2.5
lysophosphatidylcholine
-
soluble isozyme, pH 8.0, 37°C
65
lysosphingomyelin
-
soluble isozyme, pH 8.0, 37°C
1
sn-glycero-3-phosphocholine
-
soluble isozyme, pH 8.0, 37°C
29
sn-glycerol-3-phosphocholine
pH 7.2, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
70
4-nitrophenyl phosphocholine
-
soluble isozyme, pH 8.0, 37°C
10
lysophosphatidylcholine
-
soluble isozyme, pH 8.0, 37°C
200
lysosphingomyelin
-
soluble isozyme, pH 8.0, 37°C
1
sn-glycero-3-phosphocholine
-
soluble isozyme, pH 8.0, 37°C
20.6
sn-glycerol-3-phosphocholine
pH 7.2, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0007 - 0.0015
tellurium tetrachloride
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.046
-
-
0.276
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-
3.2
-
purified native soluble isozyme, pH 8.0, 37°C, substrate 4-nitrophenyl phosphocholine
282
purified recombinant His-tagged enzyme, pH 7.2, 37°C
583
purified native enzyme, pH 7.2, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
narrow pH range near pH 7
9 - 11
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
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37 - 60
activity range with over 95% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
UNIPROT
ORGANISM
Mus musculus;
Q8DQ62
Streptococcus pneumoniae (strain ATCC BAA-255 / R6);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
-
monomeric conformation of the soluble isozyme, gel filtration
66000
native enzyme, gel filtration
70447
1 * 66000, SDS-PAGE, 1 * 70447, sequence calculation
74000
-
SDS-PAGE
75000
-
gel filtration
110000
170000
-
gel filtration
230000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
phosphoprotein
proteolytic modification
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10.5
purified extracellular enzyme, 30 min, stable at
730076
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 45
completely stable at
35 - 50
-
90% loss of activity at 50oC
45 - 65
-
62% loss of activity of the membrane bound enzyme after 1 h storage at 65oC; 90% loss of activity of the soluble enzyme after 1 h storage at 65oC; membrane bound enzyme is stable at 45oC
50
purified extracellular enzyme, 30 min, stable at
55
-
presence of Zn2+ increases heat stability
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from brain 396fold by heat treatment at 60°C, concanavalin A affinity chromatography, and hydroxylapatite chromatography, followed by dialysis, anion exchange chromatography and gel filtration
-
recombinant C-terminally His6-tagged enzyme from Streptomyces lividans strain 1326 by ammonium sulfate fractionation, nickel affinity and hydrophobic interaction chromatography, native extracellular enzyme 53fold from culture supernatant by ammonium sulfate fractionation, dialysis, anion exchange chromatography, and ultrafiltration, followed by hydrophobic interaction chromatography, ultrafiltration, two different steps of anion exxchange chromatography, ultrafiltration, gel filtration, ultrafiltration, cation exchange chromatography, and again ultrafiltration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene gpc-cp, DNA and amino acid sequence determination and analysis, sequence comparison and phyogenetic tree, peptide sequencing, molecular cloning in Escherichia coli strain HST08, recombinant expression of the C-terminally His6-tagged enzyme in enzyme-lacking Streptomyces lividans strain 1326 (NBRC15675)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics