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Information on EC 3.1.4.46 - glycerophosphodiester phosphodiesterase and Organism(s) Homo sapiens
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3.1.4.46 glycerophosphodiester phosphodiesteraseIUBMB Comments
Broad specificity for glycerophosphodiesters; glycerophosphocholine, glycerophosphoethanolamine, glycerophosphoglycerol and bis(glycerophospho)-glycerol are hydrolysed.
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Word Map
- 3.1.4.46
- borrelia
- spirochete
- moraxella
- catarrhalis
- glycerophosphocholine
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nontypeable
- miyamotoi
-
gdpds
- hermsii
- glycerophosphoinositol
- glycerophosphodiesterase
- glycerophosphoethanolamine
-
nonacylated
-
six-transmembrane
- glycerophosphorylcholine
- medicine
- diagnostics
- environmental protection
- drug development
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
glycerophosphodiester phosphodiesterase, lipoprotein d, glpq2, igd-binding protein, glpq1, gpd protein, outer membrane protein d, pfgdpd, gpcpd1, ttgdpd, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
gene hpd protein
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-
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GlpQ
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-
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glycerophosphodiester phosphodiesterase
glycerophosphoryl diester phosphodiesterase
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-
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GPX-PDE
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-
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IGD-binding protein
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-
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IgD-binding protein D
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immunoglobulin D-binding protein
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phosphodiesterase, glycerophosphodiester
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phosphohydrolase GpdQ
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glycerophosphodiester phosphodiesterase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic diester
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-
-
-
PATHWAY SOURCE
PATHWAYS
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
glycerophosphodiester glycerophosphohydrolase
Broad specificity for glycerophosphodiesters; glycerophosphocholine, glycerophosphoethanolamine, glycerophosphoglycerol and bis(glycerophospho)-glycerol are hydrolysed.
CAS REGISTRY NUMBER
COMMENTARY
86280-59-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
-
-
?
sn-glycero-3-phosphoinositol + H2O
inositol + sn-glycerol 3-phosphate
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-
-
?
additional information
?
-
protein may act as a negative regulator in gene transcription mediated by the MAPK signaling pathways
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-
?
additional information
?
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-
protein may act as a negative regulator in gene transcription mediated by the MAPK signaling pathways
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-
?
additional information
?
-
isozyme GDE2-mediated hydrolysis of the RECK GPI anchor is not a phospholipase D-like hydrolysis, which suggests a different attack of the phosphodiester bond compared to that reported for the other GDE2 substrate sn-glycero-3-phosphocholine
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-
?
additional information
?
-
isozyme GDE2-mediated hydrolysis of the RECK GPI anchor is not a phospholipase D-like hydrolysis, which suggests a different attack of the phosphodiester bond compared to that reported for the other GDE2 substrate sn-glycero-3-phosphocholine
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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
sn-glycero-3-phosphocholine + H2O
choline + sn-glycerol 3-phosphate
-
-
-
?
sn-glycero-3-phosphoinositol + H2O
inositol + sn-glycerol 3-phosphate
-
-
-
?
additional information
?
-
protein may act as a negative regulator in gene transcription mediated by the MAPK signaling pathways
-
-
?
additional information
?
-
-
protein may act as a negative regulator in gene transcription mediated by the MAPK signaling pathways
-
-
?
additional information
?
-
isozyme GDE2-mediated hydrolysis of the RECK GPI anchor is not a phospholipase D-like hydrolysis, which suggests a different attack of the phosphodiester bond compared to that reported for the other GDE2 substrate sn-glycero-3-phosphocholine
-
-
?
additional information
?
-
isozyme GDE2-mediated hydrolysis of the RECK GPI anchor is not a phospholipase D-like hydrolysis, which suggests a different attack of the phosphodiester bond compared to that reported for the other GDE2 substrate sn-glycero-3-phosphocholine
-
-
?
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the isozyme GDPD5 is significantly overexpressed in highly malignant estrogen receptor negative compared to weakly malignant estrogen receptor positive human breast cancer cells and breast tumors from patients, GDPD5 expression in tumors and correlation to choline containing metabolite levels, overview
estrogen-sensitive weakly metastatic human breast cancer cells
estrogen-independent highly metastatic human breast cancer cells
mature motor neurons and not in undifferentiated progenitors
additional information
additional information
not detected in QGY, SK-Hep1, H1299, Hep3B, and Huh7 cell lines
additional information
-
not detected in QGY, SK-Hep1, H1299, Hep3B, and Huh7 cell lines
additional information
GDE2 is widely expressed, with relative low levels in the kidney and prostate
additional information
GDE2 is widely expressed, with relative low levels in the kidney and prostate
additional information
isozyme GDPD5 is ubiquitously expressed in human tissues
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
isozyme GDE2 contains a 43-amino acid intracellular N-terminal region, six transmembrane domains, an intracellular C-terminal domain of 82-amino acid residues and two 13-amino acid intracellular connecting loops between the transmembrane domains
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
the isozyme GDPD5 is a glycerophosphodiester phosphodiesterase that likely participates in regulating choline phospholipid metabolism in breast cancer, which possibly occurs in cooperation with choline kinase alpha and phosphatidylcholine-specific phospholipase D1
physiological function
evolution
the human glycerophosphodiester phosphodiesterase domain (GDPD) containing family consists of 5 isozymes, GDPD1-5
malfunction
ablating GDE2 expression in the spinal cord using small-interfering RNAs results in the loss of post-mitotic motor neurons and an increase in cell death
malfunction
isozyme GDE5 expression down-regulation in several types of skeletal muscle atrophies is induced by aging and denervation
malfunction
the enzyme encoded by glycerophosphodiester phosphodiesterase domain containing 5 is associated with breast cancer malignancy
physiological function
isozyme GDE2 is directly linked to cell differentiation, which triggers motor neuron differentiation, and it acts as an osmoregulated enzyme. GDE2 promotion of neurogenesis follows a different molecular mechanism compared to that postulated for GDE2 osmoregulation of kidney cells, overview. GDE2 up-regulation upon retinoic-acid treatment is sufficient to induce neurite formation that is blocked upon GDE2 downregulation by siRNAs. Isozmye GDE2 is involved in the regulation of neuronal transcriptional programs
physiological function
isozyme GDE5 inhibits skeletal muscle development independent of its enzymatic activity. Isozyme GDE5 expression in brain can contribute to variations in cortical surface area. Decreased isozyme GDE5 expression might represent an adaptation response to counteract the pathology, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
overexpression of GD4 in HEK-293 cells does not induce neurite formation or a change change in cell morphology
additional information
-
overexpression of GD4 in HEK-293 cells does not induce neurite formation or a change change in cell morphology
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
GDE2, maps to 11q13.4-13.5, and contains 17 exons and 16 introns, overexpression of a the tagged GDE2 in COS-7, HEK-293cells, and in HeLa cell endoplasmic reticulum, as well as at the plasma membrane, depending on cell confluence, with a predominant plasma-membrane localization in confluent
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
osmotic stress conditions resulting from high salt concentrations cause a decrease in the sioyzme GDE2 mRNA half-life, with the consequent lowering of GDE2 protein levels and a decrease in glycero-3-phosphocholine hydrolysis in transgenic murine mIMCD3 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yanaka, N.; Imai, Y.; Kawai, E.; Akatsuka, H.; Wakimoto, K.; Nogusa, Y.; Kato, N.; Chiba, H.; Kotani, E.; Omori, K.; Sakurai, N.
Novel membrane protein containing glycerophosphodiester phosphodiesterase motif is transiently expressed during osteoblast differentiation
J. Biol. Chem.
278
43595-43602
2003
Mus musculus (Q640M6), Mus musculus, Homo sapiens (Q9HCC8)
Lang, Q.; Zhang, H.; Li, J.; Yin, H.; Zhang, Y.; Tang, W.; Wan, B.; Yu, L.
Cloning and characterization of a human GDPD domain-containing protein GDPD5
Mol. Biol. Rep.
35
351-359
2007
Homo sapiens (Q8WTR4), Homo sapiens
Chang, P.A.; Shao, H.B.; Long, D.X.; Sun, Q.; Wu, Y.J.
Isolation, characterization and molecular 3D model of human GDE4, a novel membrane protein containing glycerophosphodiester phosphodiesterase domain
Mol. Membr. Biol.
25
557-566
2008
Homo sapiens (Q8N9F7), Homo sapiens
Corda, D.; Mosca, M.; Ohshima, N.; Grauso, L.; Yanaka, N.; Mariggio, S.
The emerging physiological roles of the glycerophosphodiesterase family
FEBS J.
281
998-1016
2014
Agrobacterium tumefaciens, Arabidopsis thaliana, Bacillus pumilus, Bacillus pumilus DSM 27, Bacillus subtilis (P54527), Borrelia hermsii (Q45201), Caldanaerobacter subterraneus subsp. tengcongensis, Escherichia coli (P09394), Escherichia coli (P10908), Haemophilus influenzae (Q06282), Haemophilus influenzae DSM 11121 (Q06282), Homo sapiens (Q8WTR4), Homo sapiens (Q9NPB8), Klebsiella aerogenes, Lupinus albus, Mus musculus, Musca domestica, Mycoplasma hyorhinis (E0TL71), Mycoplasma pneumoniae (P75367), Pasteurella multocida (Q79LP3), Plasmodium falciparum, Rattus norvegicus, Saccharomyces cerevisiae, Saccharomyces cerevisiae (Q02979), Staphylococcus aureus (Q99387), Streptomyces coelicolor, Thermotoga maritima, Treponema pallidum (O30405)
Cao, M.D.; Doepkens, M.; Krishnamachary, B.; Vesuna, F.; Gadiya, M.M.; Loenning, P.E.; Bhujwalla, Z.M.; Gribbestad, I.S.; Glunde, K.
Glycerophosphodiester phosphodiesterase domain containing 5 (GDPD5) expression correlates with malignant choline phospholipid metabolite profiles in human breast cancer
NMR Biomed.
25
1033-1042
2012
Homo sapiens (Q8WTR4)
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