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Information on EC 3.1.4.2 - glycerophosphocholine phosphodiesterase
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3.1.4.2 glycerophosphocholine phosphodiesteraseIUBMB Comments
Also acts on sn-glycero-3-phosphoethanolamine.
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Word Map
- 3.1.4.2
- surfactant
- pulmonary
- influenza
- haemophilus
- pneumonia
- alveolar
- pneumococcal
- lectin
-
collectins
-
lavage
- children
- airway
-
bronchoalveolar
-
c-type
-
phid-cv
- otitis
-
interstitial
- infant
-
serotypes
- collagen
-
10-valent
-
non-typeable
- bal
-
agglutination
- nasopharyngeal
-
booster
-
mannose-binding
-
protein-d
-
conglutinin
-
clara
-
distress
-
surfactant-associated
- diagnostics
-
pneumolysin
-
mannan-binding
- toxoid
-
reactogenicity
- medicine
-
airspace
-
serotype-specific
-
spirometry
- emphysema
-
collagen-like
-
non-vaccine
-
dodecamers
-
lung-specific
-
glaxosmithkline
-
choline-binding
- proteinosis
-
opsonophagocytic
- biotechnology
-
lungen-6
-
srage
- drug development
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
protein d, gdpd5, glycerophosphodiesterase, gdpase, enpp6, glycerophosphocholine phosphodiesterase, gpx-pde, gdpd6, gpc diesterase, gpc:choline phosphodiesterase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GDE5
glycerolphosphorylcholine phosphodiesterase
-
-
-
-
glycerophosphinicocholine diesterase
-
-
-
-
glycerophosphocholinehydrolase
-
-
-
-
glycerophosphodiester phosphodiesterase
glycerophosphodiesterase
glycerylphosphorylcholinediesterase
-
-
-
-
GP-PDE
GPC diesterase
GPC:choline phosphodiesterase
GroPChoPDE
sn-glycero 3-phosphorylcholine diesterase
-
-
-
-
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sn-glycero-3-phosphocholine + H2O = choline + sn-glycerol 3-phosphate
also acts on sn-glycero 3-phosphoethanolamine
-
-
-
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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
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SYSTEMATIC NAME
IUBMB Comments
sn-glycero-3-phosphocholine glycerophosphohydrolase
Also acts on sn-glycero-3-phosphoethanolamine.
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CAS REGISTRY NUMBER
COMMENTARY
9025-85-8
-
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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
1,2,2-trimethylpropyl methylphosphonate + H2O
3,3-dimethylbutan-2-ol + methylphosphonate
-
-
-
-
ir
4-nitrophenyl ethylphosphonate + H2O
4-nitrophenyl + ethylphosphonate
-
-
-
-
ir
4-nitrophenyl methylphosphonate + H2O
4-nitrophenyl + methylphosphonate
-
-
-
-
ir
4-nitrophenyl phenyl phosphate + H2O
4-nitrophenol + phenyl phosphate
-
-
-
-
ir
4-nitrophenyl phenyl phosphonate + H2O
4-nitrophenol + phenyl phosphonate
-
-
-
-
ir
choline lysoplasmalogen + H2O
choline + 1-(1-alkenyl)-sn-glycero-3-phosphate
preferred substrate, i.e. 1-O-1'-(Z)-octadecenyl-2-hydroxy-sn-glycero-3-phosphocholine
-
-
?
ethanolamine lysoplasmalogen + H2O
ethanolamine + 1-(1-alkenyl)-sn-glycero-3-phosphate
modest activity, i.e. 1-O-1'-(Z)-octadecenyl-2-hydroxy-sn-glycero-3-phosphoethanolamine
-
-
?
ethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + ethyl phosphate
-
-
-
-
ir
isobutyl methylphosphonate + H2O
isobutanol + methylphosphonate
-
-
-
-
ir
isopropyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + isopropyl phosphate
-
-
-
-
ir
isopropyl methylphosphonate + H2O
isopropanol + methylphosphonate
-
-
-
-
ir
methyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + methyl phosphate
-
-
-
-
ir
O-ethyl S-[2-(ethylsulfanyl)ethyl] hydrogen thiophosphate + H2O
?
-
-
-
-
ir
p-nitrophenylphosphocholine + H2O
p-nitrophenol + phosphocholine
-
-
single enzyme utilizing both glycerophosphocholine and p-nitrophenylphosphocholine as substrates
?
polyglycerophosphate + H2O
glycerol + sn-glycerol 3-phosphate
-
exhibits a structural requirement for phosphodiester bonds between adjacent glycerol units
-
?
S-[2-(ethylsulfanyl)ethyl] O,O-dimethyl thiophosphate + H2O
?
-
-
-
-
ir
S-[2-(ethylsulfanyl)ethyl] O-methyl hydrogen thiophosphate + H2O
?
-
-
-
-
ir
S-[2-[bis(1-methylethyl)amino]ethyl] O-ethyl hydrogen thiophosphate + H2O
?
-
-
-
-
ir
sn-glycero-3-phosphocholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
-
?
sn-glycero-3-phosphoethanolamine + H2O
sn-glycerol-3-phosphate + ethanolamine
-
-
-
-
?
glycero-3-phosphoethanolamine + H2O
sn-glycerol-3-phosphate + ethanolamine
-
hydrolysis of the 3'-5' phosphodiester bond
-
-
?
glycero-3-phosphoethanolamine + H2O
sn-glycerol-3-phosphate + ethanolamine
-
also active on phosphomonoester, phosphodiester, phosphotriester and phosphorothiolate substrates
-
-
?
glycerophosphoethanolamine + H2O
glycerol 1,2-cyclic phosphate + ethanolamine
-
-
-
?
glycerophosphoethanolamine + H2O
glycerol 1,2-cyclic phosphate + ethanolamine
-
-
-
?
glycerophosphoinositol + H2O
inositol + glycerol 3-phosphate
-
preferred substrate of inositol-starved yeast
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
cellular phosphatidylcholine catabolic pathway
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
cellular phosphatidylcholine catabolic pathway
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
cellular phosphatidylcholine catabolic pathway
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
cellular phosphatidylcholine catabolic pathway
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
cellular phosphatidylcholine catabolic pathway
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
cellular phosphatidylcholine catabolic pathway
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
produces glycolysable substrates that may shift the metabolic activity to the glycolytic pathway
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
maintenance to intracellular osmotic balance
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
cellular phosphatidylcholine catabolic pathway
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
enzyme amount decreases in dietary choline deficiency
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
cellular phosphatidylcholine catabolic pathway
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
only found in autopsied tissue
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
exclusive substrates
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
?
sn-glycero 3-phosphorylethanolamine + H2O
?
-
cellular phosphatidyethanolamine catabolic pathway
-
-
?
sn-glycero 3-phosphorylethanolamine + H2O
?
-
cellular phosphatidyethanolamine catabolic pathway
-
-
?
sn-glycero 3-phosphorylethanolamine + H2O
?
-
cellular phosphatidyethanolamine catabolic pathway
-
-
?
sn-glycero 3-phosphorylethanolamine + H2O
sn-glycerol 3-phosphate + ethanolamine
-
-
-
?
sn-glycero 3-phosphorylethanolamine + H2O
sn-glycerol 3-phosphate + ethanolamine
-
-
-
?
sn-glycero 3-phosphorylethanolamine + H2O
sn-glycerol 3-phosphate + ethanolamine
-
-
-
?
sn-glycero 3-phosphorylethanolamine + H2O
sn-glycerol 3-phosphate + ethanolamine
-
-
-
?
sn-glycero 3-phosphorylethanolamine + H2O
sn-glycerol 3-phosphate + ethanolamine
-
-
-
?
sn-glycero 3-phosphorylethanolamine + H2O
sn-glycerol 3-phosphate + ethanolamine
-
-
-
?
sn-glycero 3-phosphorylethanolamine + H2O
sn-glycerol 3-phosphate + ethanolamine
-
-
-
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
-
-
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
-
-
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
specific substrate
-
-
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
-
-
-
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
-
-
-
?
additional information
?
-
-
glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into sn-glycerol-3-phosphate and the corresponding alcohols. AtGDPD1 and AtGDPDL1 hydrolyze glycerolphosphoglycerol, glycerophosphocholine and glycerophosphoethanolamine
-
-
?
additional information
?
-
-
GPX-PDE1 shows catalytic activity with glycerophosphocholine while GPX-PDE2 shows highest activity with glycerophosphoinositol
-
-
?
additional information
?
-
-
the enzyme shows no significant activity with glycerophosphoglycerol, GroPIns, and glycerophosphoserine as substrates
-
-
?
additional information
?
-
-
the enzyme shows no significant activity with glycerophosphoglycerol, GroPIns, and glycerophosphoserine as substrates
-
-
?
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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
glycero-3-phosphoethanolamine + H2O
sn-glycerol-3-phosphate + ethanolamine
-
hydrolysis of the 3'-5' phosphodiester bond
-
-
?
sn-glycero-3-phosphocholine + H2O
sn-glycerol 3-phosphate + choline
-
-
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
cellular phosphatidylcholine catabolic pathway
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
cellular phosphatidylcholine catabolic pathway
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
cellular phosphatidylcholine catabolic pathway
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
cellular phosphatidylcholine catabolic pathway
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
cellular phosphatidylcholine catabolic pathway
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
cellular phosphatidylcholine catabolic pathway
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
produces glycolysable substrates that may shift the metabolic activity to the glycolytic pathway
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
maintenance to intracellular osmotic balance
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
cellular phosphatidylcholine catabolic pathway
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
enzyme amount decreases in dietary choline deficiency
-
-
?
sn-glycero 3-phosphorylcholine + H2O
?
-
cellular phosphatidylcholine catabolic pathway
-
-
?
sn-glycero 3-phosphorylethanolamine + H2O
?
-
cellular phosphatidyethanolamine catabolic pathway
-
-
?
sn-glycero 3-phosphorylethanolamine + H2O
?
-
cellular phosphatidyethanolamine catabolic pathway
-
-
?
sn-glycero 3-phosphorylethanolamine + H2O
?
-
cellular phosphatidyethanolamine catabolic pathway
-
-
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
-
-
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
specific substrate
-
-
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
-
-
-
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
-
-
-
?
additional information
?
-
-
glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into sn-glycerol-3-phosphate and the corresponding alcohols. AtGDPD1 and AtGDPDL1 hydrolyze glycerolphosphoglycerol, glycerophosphocholine and glycerophosphoethanolamine
-
-
?
additional information
?
-
-
GPX-PDE1 shows catalytic activity with glycerophosphocholine while GPX-PDE2 shows highest activity with glycerophosphoinositol
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Cu2+
Mg2+
Mn2+
Zn2+
Ca2+
-
stimulation of glycero 3-phosphocholine breakdown, but decrease of glycerol 1,2-cyclic phosphate production
Ca2+
-
6-fold activation at 5 mM, 2-fold activation at 0.1 mM with sigmoidal kinetic charactaristics
Ca2+
the enzyme is activated in the presence of 0.5-10 mM Ca2+
Co2+
-
the enzyme shows maximum activity at very low concentrations (less than 0.05 mM) of Co2+
Mg2+
-
preferred cofactor. The enzyme activity increases with increasing concentrations of Mg2+ (up to 3 mM)
Mg2+
-
stimulation of glycero 3-phosphocholine breakdown, but decrease of glycerol 1,2-cyclic phosphate production
Mn2+
-
specific acitivity towards bis(4-nitrophenyl) phosphate is enhanced 4fold in presence of MnCl2
Mn2+
-
the enzyme shows maximum activity at very low concentrations (less than 0.05 mM) of Mn2+
Zn2+
-
activity of enzyme with Zn2+ 30 fold less than with Co2+ with substrate bis(p-nitro-phenyl)phosphate
Zn2+
-
specific acitivity towards bis(4-nitrophenyl) phosphate is enhanced 2fold in presence of ZnCl2
Zn2+
-
stimulation of glycero 3-phosphocholine breakdown, but decrease of glycerol 1,2-cyclic phosphate production
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-stearoyl-2-hydroxy-sn-glycero-3-phosphate
89.8% residual activity at 4 mM
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
-
glycero 3-phosphorylethanolamine
-
45% inhibition of choline formation in equimolar ratio to glycerophosphorylcholine
L-alpha-lysophosphatidylcholine
60.7% residual activity at 4 mM
L-alpha-lysophosphatidylethanolamine
50.9% residual activity at 4 mM
metal-binding agents
-
complete inhibition by EDTA and EGTA, EDDA inhibits competitve, urea and increasing temperature potentiate inhibitory effect by EDTA
-
tryptic digested cell walls
-
derived from various gram-positive bacteria and murein-sacculi from E. coli, 60% inhibition
-
additional information
glycerophosphocholine, CDP-choline, dithiothreitol, 2-mercaptoethanol, iodoacetamide, and phenylmethylsulfonyl fluoride have no effect on enzyme activity
-
L-alpha-glycerol 3-phosphate
-
higher inhition than in Loligo pealei or Mustelus canis
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
activator protein 18.5 kDa
-
2fold increase of activation, co-purified with the enzyme
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.28
glycerophosphocholine
-
addition of Ca2+ decreases Km and increases Vmax.
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.1
S-[2-[bis(1-methylethyl)amino]ethyl] O-ethyl hydrogen thiophosphate
-
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
glycerophosphoethanolamine pH 6.0, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.001
2
-
purified recombinant His-tagged GDE5, substrate is glycerophosphoethanolamine, pH 7.4, 37°C
additional information
-
enzymatic activity similar to that of GlpQ (glycerophosphodiester phosphodiesterase, EC 3.1.4.44) of Escherichia coli
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
found in all 127 Haemophilus influenzae strains, including encapsulated serotypes a-f and NT Haemophilus influenzae strains, number of Protein D molecules is estimated to be 2800 molecules per bacterial cell
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the cells show a 2-4fold activation of glycerophosphocholine-phosphodiesterase compared to control cells
brenda
additional information
additional information
-
the gene family displayed overlapping and yet distinguishable patterns of expression in roots, leaves and stems. And all AtGDPD genes, except for AtGDPD4, are transcriptionally active in flowers and siliques. Functional redundancy as well as specificity of GDPD genes
brenda
additional information
-
GPX-PDE1 and GPX-PDE2 are highly expressed in phosphate-deficient cluster roots, particularly in root hairs, epidermal cells, and vascular bundles
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
abundance of GPX-PDE2 protein is substantially greater in cell wall extracts of Pi-deficient plants as compared with Pi-sufficient plants
brenda
-
60% are colocalized with plasma membrane marker enzymes
brenda
-
looseley associated with outer side of plasma membrane
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the Arabidopsis GDPD family can be classified into canonical GDPD (AtGDPD1-6) and GDPD-like (AtGDPDL1-7) subfamilies
malfunction
metabolism
physiological function
additional information
-
a second glycerophosphodiesterase enzyme, MPN566, is catalytically inactive and its deletion does not cause an altered phenotype
malfunction
-
altered phosphatidylcholine metabolism in epithelial ovarian cancer cells leads to 2-4fold increased enzyme activity
malfunction
-
GDE5 expression is reduced in atrophied skeletal muscles in mice and decreasing GDE5 abundance promotes myoblastic differentiation, suggesting that decreased GDE5 expression has a counter-regulatory effect on the progression of skeletal muscleatrophy. Transgenic mice specifically overexpressing GDE5DELTAC471 in skeletal muscle have less type II fiber-rich skeletal muscle mass. Forced expression of full-length GDE5 in cultured myoblasts suppresses myogenic differentiation. Transgenic mice specifically expressing GDE5DELTAC471 in skeletal muscle show less skeletal muscle mass, especially type II fiber-rich muscle
malfunction
-
GPXPDE1 phosphate deficiency-induced expression is attenuated as photosynthate is deprived, while that of GPX-PDE2 is strikingly enhanced
malfunction
-
inactivation of the glpQ gene results in reduced growth in medium with glucose as the carbon source, in loss of hydrogen peroxide production when phosphatidylcholine is present, and in a complete loss of cytotoxicity towards HeLa cells, and the glpQ mutant strain exhibited a reduced gliding velocity, overview. The phenotype is reversible par complementation with the wild-type enzyme
malfunction
-
loss-of-function of the plastid-localized AtGDPD1 leads to a significant decrease in GDPD activity, sn-glycerol 3-phosphate content, phosphate content and seedling growth rate only under phophate starvation compared with the wild-type
malfunction
enzyme-deficient mice exhibit fatty liver and hypomyelination
malfunction
-
GDE5 expression is reduced in atrophied skeletal muscles in mice and decreasing GDE5 abundance promotes myoblastic differentiation, suggesting that decreased GDE5 expression has a counter-regulatory effect on the progression of skeletal muscleatrophy. Transgenic mice specifically overexpressing GDE5DELTAC471 in skeletal muscle have less type II fiber-rich skeletal muscle mass. Forced expression of full-length GDE5 in cultured myoblasts suppresses myogenic differentiation. Transgenic mice specifically expressing GDE5DELTAC471 in skeletal muscle show less skeletal muscle mass, especially type II fiber-rich muscle
-
metabolism
-
the GDPD-mediated lipid metabolic pathway may be involved in release of phosphate from phospholipids during phosphate starvation
physiological function
-
GDE5 selectively hydrolyzes glycerophosphocholine and controls skeletal muscle development. GDE5 negatively regulates skeletal muscle development even without GroPCho phosphodiesterase activity
physiological function
-
GlpQ is implicated in the control of gene expression, apparent regulation by GlpQ is exerted at the level of transcription. All genes subject to GlpQ-dependent control have a conserved potential cis-acting element upstream of the coding region. This element overlaps the promoter in the case of the genes that are repressed in a GlpQ-dependent manner and it is located upstream of the promoter for GlpQ-activated genes. GlpQ is central to the normal physiology and to pathogenicity of the minimal pathogen
physiological function
-
White lupin GPX-PDE1 and GPX-PDE2 are involved in the acclimation to Pi limitation by enhancing glycerophosphodiester degradation and mediating root hair development. Role for the two GPX-PDEs, GPX-PDE1 and GPX-PDE2, in root hair growth and development and in a phosphate stress-induced phospholipid degradation pathway in cluster roots
physiological function
-
the enzyme plays a role in low phosphate acclimation in rice
physiological function
-
GDE5 selectively hydrolyzes glycerophosphocholine and controls skeletal muscle development. GDE5 negatively regulates skeletal muscle development even without GroPCho phosphodiesterase activity
-
Show AA Sequence and Transmembrane Helices (3341 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
185700
-
electrospray ionisation mass spectrometry, under non-denaturing conditions, consistent with calculated mass of hexamer
30840
41820
-
calculated from DNA sequence encoding Protein D (346 amino acids), SDS-PAGE, Western Blot
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
-
three dimers stabilized by an inter-chain disulfide bond, alpha/beta-sandwich
dimer
-
alpha2, 2 * 60000-72000, sucrose density gradient centrifugation and SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
acylation of Protein D determines its hydrophobicity
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
C393A/C412S mutant apoenzyme in complex with sn-glycero-3-phosphocholine, vapor diffusion method, using 0.2 M NH4Cl, 0.1 M sodium acetate pH 5.0, 20% (w/v) PEG 6000
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C154A
the mutant enzyme shows severely reduced activity compared to the wild type enzyme
E143A
the mutant enzyme shows about 50% reduced activity compared to the wild type enzyme
E190A
the mutant enzyme shows severely reduced activity compared to the wild type enzyme
Y188A
the mutant enzyme shows severely reduced activity compared to the wild type enzyme
Y75A
the mutant enzyme shows severely reduced activity compared to the wild type enzyme
A55D
the enzyme activity of the mutant is remarkably decreased compared with that of wild type enzyme
A55N
the enzyme activity of the mutant is remarkably decreased compared with that of wild type enzyme
F211A
the enzyme activity of the mutant is remarkably decreased compared with that of wild type enzyme
N56D
the enzyme activity of the mutant is remarkably decreased compared with that of wild type enzyme
N56Q
the enzyme activity of the mutant is remarkably decreased compared with that of wild type enzyme
additional information
additional information
-
construction of isogenic Haemophilus influenzae mutant lacking the ability to express Protein D. effect on the middle ears of rats in an otitis model: Protein D is not essential for survival of Haemophilus influenzae in the middle ear of rats, Protein D enhances the severity of the disease, mutant effect on human nasopharyngeal tissue culture model: Protein D is involved in pathogenesis of upper respiratory tract infections due to NT Haemophilus influenzae, probably by enhancing functional and morphological damage to ciliated epithelial cells. NT Haemophilus influenzae probably avoids the immune system: Viable intracellular NT Haemophilus influenzae has been recovered from epithelial cells and macrophages from the adenoids of children undergoing adenoidectomy because of nasal obstruction, some strains can resist macrophage-mediated killing, Protein D expression promotes adherence and internalization of NT Haemophilus influenzae into human monocytic cells.
additional information
-
functional complementation of a DELTAgde1 yeast mutant with GPX-PDE2, buta with GPX-PDE1
additional information
-
GDE5 RNAi gene silencing results in an increase in intracellular sn-glycero-3-phosphocholine levels. Construction of a truncated GDE5 construct, GDE5DELTAC471, which contains a GP-PDE sequence identified in other GP-PDEs but lacks GroPCho phosphodiesterase activity, and it shows a similar inhibitory effect on myogenic differentiation like the full-length enzyme, overview
additional information
-
GDE5 RNAi gene silencing results in an increase in intracellular sn-glycero-3-phosphocholine levels. Construction of a truncated GDE5 construct, GDE5DELTAC471, which contains a GP-PDE sequence identified in other GP-PDEs but lacks GroPCho phosphodiesterase activity, and it shows a similar inhibitory effect on myogenic differentiation like the full-length enzyme, overview
-
additional information
-
generationof GlpQ and of MPN566 knockout strains, phenotypes, overview. The MPN566-deficient strain does not show an altered phenotype
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.1 - 9.8
enzyme activity is maintained between pH 4.1 and 9.8 at 4°C for 4 h
750552
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 37
the enzyme is stable between 4 and 37°C for 60 min at pH 8.0
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Resource Iso column chromatography, Mono Q column chromatography, PPG-600M column chromatography, Giga Cap Q-650M column chromatography, and Superdex 200 gel filtration
partial
recombinant C-terminally His6-tagged enzyme from Spodoptera frugiperda Sf9 cells by nickel affinity chromatography and gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of C-terminally His6-tagged enzyme in Spodoptera frugiperda Sf9 cells
-
genes glpQ and mpn566, expression of N-terminally Strep-tagged enzymes
-
GPX-PDE1 and GPX-PDE2, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression GST-tagged GPX-PDE2
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcripts of GPX-PDE2 accumulated to about 15fold higher in photosynthate-deprived plants than normal light/dark plants, and the stimulation is displayed in both roots and leaves
-
when plants are deprived of light by dark treatment for 24h, GPX-PDE1 transcripts in Pi-deficient roots are reversibly decreased by about 70% compared with under normal light/dark conditions. The expression level of GPX-PDE1 in leaf tissue is not affected
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
efficient selection system for the identification of phosphotriesterase mutants with enhanced catalytic properties for selected organophosphate substrates
diagnostics
-
increased enzyme activity due to altered phosphatidylcholine metabolism in epithelial ovarian cancer cells can serve as diagnostic marker, overview
drug development
-
possible vaccination, Protein D is immunogenic in human. Vaccine containing polysaccharides from 7 serotypes (each conjugated to CRM197, a nontoxic mutant of diphtheria toxin that is an immunogenically inactive carrier) shows high efficacy in young children. Experiments with rats: vaccination with Protein D induces high levels of serum IgG and IgA antibodies and significant bactericidal activity against homologous and heterologous strains (rat middle ear clearance model, rat pulmonary clearance model). Pronounced activity of Protein D antibodies is shown in the chinchilla acute otitis media model
medicine
enzyme inhibition represents a targeting strategy in the treatment of breast cancer
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Clarke, N.; Dawson, R.M.C.
Enzymic formation of glycerol 1:2-cyclic phosphate
Biochem. J.
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745-747
1976
Rattus sp.
brenda
Kusser, W.; Fiedler, F.
A novel glycerophosphodiesterase from Bacillus pumilus
FEBS Lett.
166
301-306
1984
Bacillus pumilus
brenda
Ross, B.M.; Sherwin, A.L.; Kish, S.J.
Multiple forms of the enzyme glycerophosphodiesterase are present in human brain
Lipids
30
1075-1081
1995
Homo sapiens
brenda
Anfuso, C.D.; Sipione S.; Lupo, G.; Alberghina, M.
Evolutionary comparison of enzyme activities of phosphatidylcholine metabolism in the nervous system of an invertebrate (Loligo pealei), lower vertebrate (Mustelus canis) and the rat
Comp. Biochem. Physiol. B
112
493-501
1995
Doryteuthis pealeii, Mustelus canis, Rattus sp.
brenda
Mitra, Y.; Chowdhury, M.
Ca2+ dependent activation of rat uterine glycerylphosphorylcholine diesterase: Presence of a positive modulator protein in uterine secretion
Mol. Cell. Biochem.
139
101-108
1994
Rattus sp.
brenda
Kwon, E.D.; Zablocki, K.; Jung, K.Y.; Peters, E.M.; Gaarcia-perez, A.; Burg, M.B.
Osmoregulation of GPC:choline phosphodiesterase in MDCK cells: different effects of urea and NaCl
Am. J. Physiol.
269
C35-C41
1995
Rattus sp.
brenda
Yuan, J.; Kanfer, J.N.
Purification and properties of a glycerophosphocholine phosphodiesterase from bovine brain myelin
Neurochem. Res.
19
43-48
1994
Bos taurus
brenda
Mitra, J.; Chowdhury, M.
Glycerylphosphorylcholine (GPC) diesterase related alterations in the oxygen consumption profile of rat spermatozoa in differing functional states
Int. J. Androl.
15
345-354
1992
Rattus sp.
brenda
Mitra, J.; Chowdhury, M
Purification and characterization of rat uterine glycerylphosphorylcholine diesterase and its tissue-specific induction by 17-beta-estradiol
Endocrinology
129
1147-1154
1991
Rattus sp.
brenda
Zablocki, K.; Miller, S.P.F.; Garcia-Perez, A.; Burg, M.B.
Accumulation of glycerophosphocholine (GPC) by renal cells: Osmotic regulation of GPC:choline phosphodiesterase
Proc. Natl. Acad. Sci. USA
88
7820-7824
1991
Canis lupus, Oryctolagus cuniculus
brenda
Kanfer, J.N.; McCartney, D.G.
GPC phosphodiesterase and phosphomonoesterase activities of renal cortex and medulla of control, antdiuresis and diuresis rats
FEBS Lett.
257
348-350
1989
Rattus sp.
brenda
Larson, T.J.; van Loo-Bhattacharya, A.T.
Purification and characterization of glpQ-encoded glycerophosphodiester phosphodiesterase from Escherichia coli K-12
Arch. Biochem. Biophys.
260
577-584
1988
Escherichia coli
brenda
Paltauf, F.; Zinser, E.; Daum, G.
Utilization of exogenous glycerophosphodiesters and glycerol 3-phosphate by inositol-starved yeast, Saccharomyces uvarum
Biochim. Biophys. Acta
835
322-330
1985
Saccharomyces uvarum
brenda
Spanner, S.; Ansell, G.B.
Activation of glycerophosphocholine phosphodiesterase in rat forebrain by Ca2+
Biochem. J.
208
845-850
1982
Rattus sp.
brenda
Trevathan, C.A.; Smibert, R.M.; George, H.A.
Lipid catabolism of cultivated treponemes
Can. J. Microbiol.
28
672-678
1982
Treponema denticola, Treponema minutum, Treponema phagedenis, Treponema refringens, Treponema vincentii
brenda
Gregg, M.R.; Spanner, S.; Ansell, G.B
Muscarinic receptor binding sites in the synaptosomal and microsomal fractions of bovine caudate nucleus
Biochem. Soc. Trans.
9
416-417
1981
Bos taurus
-
brenda
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 sp.
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 sp.
brenda
Lloyd-Davies, K.A.; Michell, R.H.; Coleman, R.
Glycerylphosphorylcholine phosphodiesterase in rat liver plasma membranes
Biochem. J.
127
36
1972
Rattus sp.
-
brenda
Lloyd-Davies, K.A.; Michell, R.H.; Coleman, R.
Glycerylphosphorylcholine phosphodiesterase in rat liver
Biochem. J.
127
357-368
1972
Rattus sp.
brenda
Baldwin, J.J.; Lanes, P.; Cornatzer, W.E.
Glycerylphosphorylcholine diesterase: Effects of metal-binding agents
Arch. Biochem. Biophys.
133
224-232
1969
Rattus sp.
brenda
Baldwin, J.J.; Cornatzer, W.E.
Glycerylphosphorylcholine diesterase: Effects of dietary choline deficiency
Biochim. Biophys. Acta
176
193-195
1969
Rattus sp.
brenda
Baldwin, J.J.; Cornatzer, W.E.
Rat kidney glycerylphosphorylcholine diesterase
Biochim. Biophys. Acta
164
195-204
1968
Rattus sp.
brenda
Hayaishi, O.; Kornberg, A.
Metabolism of phospholipides by bacterial enzymes
J. Biol. Chem.
206
647-663
1954
Serratia plymuthica
brenda
Van der Rest, B.; Boisson, A.M.; Gout, E.; Bligny, R.; Douce, R.
Glycerophosphocholine metabolism in higher plant cells. Evidence of a new glyceryl-phosphodiester phosphodiesterase
Plant Physiol.
130
244-255
2002
Daucus carota
brenda
Anfuso, C.D.; Sipione, S.; Lupo, G.; Ragusa, N.; Alberghina, M.
Characterization of glycerophosphocholine phosphodiesterase activity and phosphatidylcholine biosynthesis in cultured retinal microcapillary pericytes. Effect of adenosine and endothelin-1
Lipids
38
45-52
2003
Bos taurus
brenda
Fisher, E.; Almaguer, C.; Holic, R.; Griac, P.; Patton-Vogt, J.
Glycerophosphocholine-dependent growth requires Gde1p (YPL110c) and Git1p in Saccharomyces cerevisiae
J. Biol. Chem.
280
36110-36117
2005
Saccharomyces cerevisiae
brenda
Jackson, C.J.; Carr, P.D.; Kim, H.K.; Liu, J.W.; Ollis, D.L.
The purification, crystallization and preliminary diffraction of a glycerophosphodiesterase from Enterobacter aerogenes
Acta Crystallogr. Sect. F
62
659-661
2006
Klebsiella aerogenes
brenda
Ghanem, E.; Li, Y.; Xu, C.; Raushel, F.M.
Characterization of a phosphodiesterase capable of hydrolyzing EA 2192, the most toxic degradation product of the nerve agent VX
Biochemistry
46
9032-9040
2007
Klebsiella aerogenes
brenda
Jackson, C.J.; Carr, P.D.; Liu, J.W.; Watt, S.J.; Beck, J.L.; Ollis, D.L.
The structure and function of a novel glycerophosphodiesterase from Enterobacter aerogenes
J. Mol. Biol.
367
1047-1062
2007
Klebsiella aerogenes
brenda
Forsgren, A.; Riesbeck, K.; Janson, H.
Protein D of Haemophilus influenzae: a protective nontypeable H. influenzae antigen and a carrier for pneumococcal conjugate vaccines
Clin. Infect. Dis.
46
726-731
2008
Haemophilus influenzae
brenda
Iorio, E.; Ricci, A.; Bagnoli, M.; Pisanu, M.E.; Castellano, G.; Di Vito, M.; Venturini, E.; Glunde, K.; Bhujwalla, Z.M.; Mezzanzanica, D.; Canevari, S.; Podo, F.
Activation of phosphatidylcholine cycle enzymes in human epithelial ovarian cancer cells
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70
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2010
Homo sapiens
brenda
Okazaki, Y.; Ohshima, N.; Yoshizawa, I.; Kamei, Y.; Mariggio, S.; Okamoto, K.; Maeda, M.; Nogusa, Y.; Fujioka, Y.; Izumi, T.; Ogawa, Y.; Shiro, Y.; Wada, M.; Kato, N.; Corda, D.; Yanaka, N.
A novel glycerophosphodiester phosphodiesterase, GDE5, controls skeletal muscle development via a non-enzymatic mechanism
J. Biol. Chem.
285
27652-27663
2010
Mus musculus, Mus musculus C57BL/6
brenda
Cheng, Y.; Zhou, W.; El Sheery, N.I.; Peters, C.; Li, M.; Wang, X.; Huang, J.
Characterization of the Arabidopsis glycerophosphodiester phosphodiesterase (GDPD) family reveals a role of the plastid-localized AtGDPD1 in maintaining cellular phosphate homeostasis under phosphate starvation
Plant J.
66
781-795
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Arabidopsis thaliana
brenda
Cheng, L.; Bucciarelli, B.; Liu, J.; Zinn, K.; Miller, S.; Patton-Vogt, J.; Allan, D.; Shen, J.; Vance, C.P.
White lupin cluster root acclimation to phosphorus deficiency and root hair development involve unique glycerophosphodiester phosphodiesterases
Plant Physiol.
156
1131-1148
2011
Lupinus albus
brenda
Schmidl, S.R.; Otto, A.; Lluch-Senar, M.; Pinol, J.; Busse, J.; Becher, D.; Stuelke, J.
A trigger enzyme in Mycoplasma pneumoniae: impact of the glycerophosphodiesterase GlpQ on virulence and gene expression
PLoS Pathog.
7
e1002263
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Mycoplasma pneumoniae
brenda
Marchan, R.
GDPD5, a choline-generating enzyme and its novel role in tumor cell migration
Arch. Toxicol.
90
3143-3144
2016
Homo sapiens (Q8WTR4)
brenda
Matsumoto, Y.; Kashiwabara, N.; Oyama, T.; Murayama, K.; Matsumoto, H.; Sakasegawa, S.; Sugimori, D.
Molecular cloning, heterologous expression, and enzymatic characterization of lysoplasmalogen-specific phospholipase D from Thermocrispum sp.
FEBS Open Bio
6
1113-1130
2016
Thermocrispum sp. RD004668 (A0A0U4VTN7)
brenda
Mehra, P.; Pandey, B.K.; Verma, L.; Giri, J.
A novel glycerophosphodiester phosphodiesterase improves phosphate deficiency tolerance in rice
Plant Cell Environ.
42
1167-1179
2018
Oryza sativa
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
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