Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,2,2-trimethylpropyl methylphosphonate + H2O
3,3-dimethylbutan-2-ol + methylphosphonate
-
Substrates: -
Products: -
ir
4-nitrophenyl ethylphosphonate + H2O
4-nitrophenyl + ethylphosphonate
-
Substrates: -
Products: -
ir
4-nitrophenyl methylphosphonate + H2O
4-nitrophenyl + methylphosphonate
-
Substrates: -
Products: -
ir
4-nitrophenyl phenyl phosphate + H2O
4-nitrophenol + phenyl phosphate
-
Substrates: -
Products: -
ir
4-nitrophenyl phenyl phosphonate + H2O
4-nitrophenol + phenyl phosphonate
-
Substrates: -
Products: -
ir
4-nitrophenylphosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
ir
bis(4-nitrophenyl) phosphate + H2O
4-nitrophenol + phosphate
-
Substrates: -
Products: -
ir
bis(p-nitro-phenyl)phosphate + H2O
?
-
Substrates: -
Products: -
?
choline lysoplasmalogen + H2O
choline + 1-(1-alkenyl)-sn-glycero-3-phosphate
Substrates: preferred substrate, i.e. 1-O-1'-(Z)-octadecenyl-2-hydroxy-sn-glycero-3-phosphocholine
Products: -
?
diethyl phosphate + H2O
ethanol + ethyl phosphate
-
Substrates: -
Products: -
ir
dimethyl 4-nitrophenyl phosphate + H2O
?
-
Substrates: -
Products: -
ir
dimethyl phosphate + H2O
methanol + methyl phosphate
-
Substrates: -
Products: -
ir
ethanolamine lysoplasmalogen + H2O
ethanolamine + 1-(1-alkenyl)-sn-glycero-3-phosphate
Substrates: modest activity, i.e. 1-O-1'-(Z)-octadecenyl-2-hydroxy-sn-glycero-3-phosphoethanolamine
Products: -
?
ethyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + ethyl phosphate
-
Substrates: -
Products: -
ir
ethyl demeton S
?
-
Substrates: -
Products: -
?
ethyl methyl 4-nitrophenyl phosphate + H2O
?
-
Substrates: -
Products: -
ir
ethyl methylphosphonate + H2O
ethanol + methylphosphonate
-
Substrates: -
Products: -
ir
glycero-3-phosphoethanolamine + H2O
sn-glycerol-3-phosphate + ethanolamine
glycerophosphocholine + H2O
glycerol 1,2-cyclic phosphate + choline
-
Substrates: -
Products: -
?
glycerophosphocholine + H2O
sn-glycerol 3-phosphate + choline
-
Substrates: -
Products: -
?
glycerophosphoethanolamine + H2O
?
glycerophosphoethanolamine + H2O
glycerol 1,2-cyclic phosphate + ethanolamine
glycerophosphoglycerol + H2O
glycerol + glycerol 3-phosphate
-
Substrates: -
Products: -
?
glycerophosphoinositol + H2O
inositol + glycerol 3-phosphate
glycerophosphoserine + H2O
L-serine + glycerol 3-phosphate
-
Substrates: -
Products: -
?
glycerophosphoserine + H2O
serine + glycerol 3-phosphate
-
Substrates: -
Products: -
?
isobutyl methylphosphonate + H2O
isobutanol + methylphosphonate
-
Substrates: -
Products: -
ir
isopropyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + isopropyl phosphate
-
Substrates: -
Products: -
ir
isopropyl methylphosphonate + H2O
isopropanol + methylphosphonate
-
Substrates: -
Products: -
ir
methyl 4-nitrophenyl phosphate + H2O
4-nitrophenol + methyl phosphate
-
Substrates: -
Products: -
ir
O-ethyl S-[2-(ethylsulfanyl)ethyl] hydrogen thiophosphate + H2O
?
-
Substrates: -
Products: -
ir
p-nitrophenylphosphocholine + H2O
p-nitrophenol + phosphocholine
-
Substrates: -
Products: single enzyme utilizing both glycerophosphocholine and p-nitrophenylphosphocholine as substrates
?
paraoxon + H2O
4-nitrophenol + diethyl phosphate
-
Substrates: -
Products: -
ir
phenyl methylphosphonate + H2O
phenol + methylphosphonate
-
Substrates: -
Products: -
ir
polyglycerophosphate + H2O
glycerol + sn-glycerol 3-phosphate
-
Substrates: exhibits a structural requirement for phosphodiester bonds between adjacent glycerol units
Products: -
?
S-[2-(ethylsulfanyl)ethyl] O,O-dimethyl thiophosphate + H2O
?
-
Substrates: -
Products: -
ir
S-[2-(ethylsulfanyl)ethyl] O-methyl hydrogen thiophosphate + H2O
?
-
Substrates: -
Products: -
ir
S-[2-[bis(1-methylethyl)amino]ethyl] O-ethyl hydrogen thiophosphate + H2O
?
-
Substrates: -
Products: -
ir
sn-glycero 3-phosphorylcholine + H2O
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
sn-glycero 3-phosphorylethanolamine + H2O
?
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
sn-glycerol 3-phosphate + choline
-
Substrates: -
Products: -
?
sn-glycero-3-phosphoethanolamine + H2O
sn-glycerol-3-phosphate + ethanolamine
-
Substrates: -
Products: -
?
sn-glycero-3-phosphoinositol + H2O
sn-glycerol-3-phosphate + inositol
-
Substrates: -
Products: -
?
additional information
?
-
glycero-3-phosphoethanolamine + H2O

sn-glycerol-3-phosphate + ethanolamine
-
Substrates: hydrolysis of the 3'-5' phosphodiester bond
Products: -
?
glycero-3-phosphoethanolamine + H2O
sn-glycerol-3-phosphate + ethanolamine
-
Substrates: also active on phosphomonoester, phosphodiester, phosphotriester and phosphorothiolate substrates
Products: -
?
glycerophosphoethanolamine + H2O

?
-
Substrates: -
Products: -
?
glycerophosphoethanolamine + H2O
?
-
Substrates: -
Products: -
?
glycerophosphoethanolamine + H2O
?
-
Substrates: -
Products: -
?
glycerophosphoethanolamine + H2O
?
-
Substrates: -
Products: -
?
glycerophosphoethanolamine + H2O

glycerol 1,2-cyclic phosphate + ethanolamine
-
Substrates: -
Products: -
?
glycerophosphoethanolamine + H2O
glycerol 1,2-cyclic phosphate + ethanolamine
-
Substrates: -
Products: -
?
glycerophosphoinositol + H2O

inositol + glycerol 3-phosphate
-
Substrates: -
Products: -
?
glycerophosphoinositol + H2O
inositol + glycerol 3-phosphate
-
Substrates: -
Products: -
?
glycerophosphoinositol + H2O
inositol + glycerol 3-phosphate
-
Substrates: preferred substrate of inositol-starved yeast
Products: -
?
sn-glycero 3-phosphorylcholine + H2O

?
-
Substrates: cellular phosphatidylcholine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
Substrates: cellular phosphatidylcholine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
Substrates: cellular phosphatidylcholine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
Substrates: cellular phosphatidylcholine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
Substrates: cellular phosphatidylcholine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
Substrates: cellular phosphatidylcholine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
Substrates: produces glycolysable substrates that may shift the metabolic activity to the glycolytic pathway
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
Substrates: maintenance to intracellular osmotic balance
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
81114, 95130, 95131, 95132, 95134, 95135, 95141, 95144, 95146, 95147, 95148, 95149, 95150, 95151 Substrates: cellular phosphatidylcholine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
Substrates: enzyme amount decreases in dietary choline deficiency
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
Substrates: cellular phosphatidylcholine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylcholine + H2O

sn-glycerol 3-phosphate + choline
-
Substrates: -
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
Substrates: -
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
Substrates: -
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
Substrates: -
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
Substrates: -
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
Substrates: only found in autopsied tissue
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
Substrates: -
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
Substrates: -
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
81114, 95130, 95132, 95134, 95135, 95137, 95141, 95144, 95146, 95147, 95148, 95149, 95150, 95151 Substrates: -
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
Substrates: exclusive substrates
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
Substrates: -
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
Substrates: -
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
Substrates: -
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
Substrates: -
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
Substrates: -
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
Substrates: -
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
sn-glycerol 3-phosphate + choline
-
Substrates: -
Products: -
?
sn-glycero 3-phosphorylethanolamine + H2O

?
-
Substrates: cellular phosphatidyethanolamine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylethanolamine + H2O
?
-
Substrates: cellular phosphatidyethanolamine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylethanolamine + H2O
?
-
Substrates: cellular phosphatidyethanolamine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylethanolamine + H2O

sn-glycerol 3-phosphate + ethanolamine
-
Substrates: -
Products: -
?
sn-glycero 3-phosphorylethanolamine + H2O
sn-glycerol 3-phosphate + ethanolamine
-
Substrates: -
Products: -
?
sn-glycero 3-phosphorylethanolamine + H2O
sn-glycerol 3-phosphate + ethanolamine
-
Substrates: -
Products: -
?
sn-glycero 3-phosphorylethanolamine + H2O
sn-glycerol 3-phosphate + ethanolamine
-
Substrates: -
Products: -
?
sn-glycero 3-phosphorylethanolamine + H2O
sn-glycerol 3-phosphate + ethanolamine
-
Substrates: -
Products: -
?
sn-glycero-3-phosphocholine + H2O

choline + sn-glycerol 3-phosphate
Substrates: -
Products: -
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
Substrates: -
Products: -
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
Substrates: specific substrate
Products: -
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
Substrates: -
Products: -
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
additional information

?
-
-
Substrates: glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into sn-glycerol-3-phosphate and the corresponding alcohols. AtGDPD1 and AtGDPDL1 hydrolyze glycerolphosphoglycerol, glycerophosphocholine and glycerophosphoethanolamine
Products: -
?
additional information
?
-
-
Substrates: physiological role of enzyme
Products: -
?
additional information
?
-
-
Substrates: GPX-PDE1 shows catalytic activity with glycerophosphocholine while GPX-PDE2 shows highest activity with glycerophosphoinositol
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows no significant activity with glycerophosphoglycerol, GroPIns, and glycerophosphoserine as substrates
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows no significant activity with glycerophosphoglycerol, GroPIns, and glycerophosphoserine as substrates
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
glycero-3-phosphoethanolamine + H2O
sn-glycerol-3-phosphate + ethanolamine
-
Substrates: hydrolysis of the 3'-5' phosphodiester bond
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
sn-glycero 3-phosphorylethanolamine + H2O
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
sn-glycero-3-phosphocholine + H2O
sn-glycerol 3-phosphate + choline
-
Substrates: -
Products: -
?
additional information
?
-
sn-glycero 3-phosphorylcholine + H2O

?
-
Substrates: cellular phosphatidylcholine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
Substrates: cellular phosphatidylcholine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
Substrates: cellular phosphatidylcholine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
Substrates: cellular phosphatidylcholine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
Substrates: cellular phosphatidylcholine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
Substrates: cellular phosphatidylcholine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
Substrates: produces glycolysable substrates that may shift the metabolic activity to the glycolytic pathway
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
Substrates: maintenance to intracellular osmotic balance
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
81114, 95130, 95131, 95132, 95134, 95135, 95141, 95144, 95146, 95147, 95148, 95149, 95150, 95151 Substrates: cellular phosphatidylcholine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
Substrates: enzyme amount decreases in dietary choline deficiency
Products: -
?
sn-glycero 3-phosphorylcholine + H2O
?
-
Substrates: cellular phosphatidylcholine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylethanolamine + H2O

?
-
Substrates: cellular phosphatidyethanolamine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylethanolamine + H2O
?
-
Substrates: cellular phosphatidyethanolamine catabolic pathway
Products: -
?
sn-glycero 3-phosphorylethanolamine + H2O
?
-
Substrates: cellular phosphatidyethanolamine catabolic pathway
Products: -
?
sn-glycero-3-phosphocholine + H2O

choline + sn-glycerol 3-phosphate
Substrates: -
Products: -
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
Substrates: specific substrate
Products: -
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
Substrates: -
Products: -
?
additional information

?
-
-
Substrates: glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into sn-glycerol-3-phosphate and the corresponding alcohols. AtGDPD1 and AtGDPDL1 hydrolyze glycerolphosphoglycerol, glycerophosphocholine and glycerophosphoethanolamine
Products: -
?
additional information
?
-
-
Substrates: physiological role of enzyme
Products: -
?
additional information
?
-
-
Substrates: GPX-PDE1 shows catalytic activity with glycerophosphocholine while GPX-PDE2 shows highest activity with glycerophosphoinositol
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
-
the Arabidopsis GDPD family can be classified into canonical GDPD (AtGDPD1-6) and GDPD-like (AtGDPDL1-7) subfamilies
additional information
-
a second glycerophosphodiesterase enzyme, MPN566, is catalytically inactive and its deletion does not cause an altered phenotype
drug target

silencing or pharmacologically inhibiting glycerophosphodiesterase EDI3 using dipyridamole in ER-HER2 + cells resistant to HER2-targeted therapy decreases cell viability in vitro and tumour growth in vivo
drug target
-
since PfGDPD-mediated procurement of choline is indispensable for normal phosphatidylcholine biosynthesis and asexual blood stage development in the parasite, it may represent a potential new drug target
drug target
-
since PfGDPD-mediated procurement of choline is indispensable for normal phosphatidylcholine biosynthesis and asexual blood stage development in the parasite, it may represent a potential new drug target
-
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
-
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
-
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
-
GPXPDE1 phosphate deficiency-induced expression is attenuated as photosynthate is deprived, while that of GPX-PDE2 is strikingly enhanced
malfunction
enzyme-deficient mice exhibit fatty liver and hypomyelination
malfunction
-
loss of the enzyme (PfGDPD) prevents de novo PC synthesis
malfunction
inhibition of GDE5 suppressed the formation of lipid droplets, which is accompanied by the decreased expression of adipocyte differentiation markers. The decreased GDE5 expression suppresses mitotic clonal expansion of preadipocytes. Decreased GDE5 expression results in accumulation of intracellular glycerophosphocholine but does not affect phosphatidylcholine synthesis. mRNAs of proteoglycans and transporters for organic osmolytes are significantly upregulated and intracellular amino acids and urea levels are altered in response to GDE5 inhibition. Reduction of GDE5 expression increases lactate dehydrogenase release from preadipocytes
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
-
loss of the enzyme (PfGDPD) prevents de novo PC synthesis
-
metabolism

-
the GDPD-mediated lipid metabolic pathway may be involved in release of phosphate from phospholipids during phosphate starvation
metabolism
the enzyme participates in choline metabolism
metabolism
-
PfGDPD-mediated procurement of choline is indispensable for normal phosphatidylcholine biosynthesis
metabolism
-
PfGDPD-mediated procurement of choline is indispensable for normal phosphatidylcholine biosynthesis
-
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
-
GDE5 selectively hydrolyzes glycerophosphocholine and controls skeletal muscle development. GDE5 negatively regulates skeletal muscle development even without GroPCho phosphodiesterase activity
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
the enzyme drives tumor cell migration
physiological function
glycerophosphodiesterase EDI3 directly influences choline and phospholipid metabolism
physiological function
-
the enzyme is indispensable for blood stage parasite proliferation and is required for trophozoite development
physiological function
GDE5 is actively involved in glycerophosphocholine/choline metabolism in 3T3-L1 adipocytes
physiological function
-
GDE5 selectively hydrolyzes glycerophosphocholine and controls skeletal muscle development. GDE5 negatively regulates skeletal muscle development even without GroPCho phosphodiesterase activity
-
physiological function
-
the enzyme is indispensable for blood stage parasite proliferation and is required for trophozoite development
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Clarke, N.; Dawson, R.M.C.
Enzymic formation of glycerol 1:2-cyclic phosphate
Biochem. J.
153
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
Cancer Res.
70
2126-2135
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
2011
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
2011
Mycoplasmoides 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
Okazaki, Y.; Nakamura, K.; Takeda, S.; Yoshizawa, I.; Yoshida, F.; Ohshima, N.; Izumi, T.; Klein, J.; Kumrungsee, T.; Sands, J.; Yanaka, N.
GDE5 inhibition accumulates intracellular glycerophosphocholine and suppresses adipogenesis at a mitotic clonal expansion stage
Am. J. Physiol. Cell Physiol.
316
C162-C174
2019
Mus musculus (Q8C0L9)
brenda
Ramaprasad, A.; Burda, P.C.; Calvani, E.; Sait, A.J.; Palma-Duran, S.A.; Withers-Martinez, C.; Hackett, F.; Macrae, J.; Collinson, L.; Gilberger, T.W.; Blackman, M.J.
A choline-releasing glycerophosphodiesterase essential for phosphatidylcholine biosynthesis and blood stage development in the malaria parasite
eLife
11
e82207
2022
Plasmodium falciparum, Plasmodium falciparum B11
brenda
Keller, M.; Rohlf, K.; Glotzbach, A.; Leonhardt, G.; Lueke, S.; Derksen, K.; Demirci, O.e.; Goecener, D.; AlWahsh, M.; Lambert, J.; Lindskog, C.; Schmidt, M.; Brenner, W.; Baumann, M.; Zent, E.; Zischinsky, M.L.; Hellwig, B.; Madjar, K.; Rahnenfuehrer, J.; Overbeck, N.; Reinders, J.; Cadenas, C.; Hengstler, J.G.; Edlund, K.; Marchan, R.
Inhibiting the glycerophosphodiesterase EDI3 in ER-HER2+ breast cancer cells resistant to HER2-targeted therapy reduces viability and tumour growth
J. Exp. Clin. Cancer Res.
42
25
2023
Homo sapiens (Q9NPB8)
brenda