Information on EC 3.1.3.31 - nucleotidase and Organism(s) Homo sapiens and UniProt Accession O75355

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Homo sapiens
UNIPROT: O75355
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
3.1.3.31
-
RECOMMENDED NAME
GeneOntology No.
nucleotidase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
nucleotide phosphohydrolase
A wide specificity for 2', 3'- and 5'- nucleotides; also hydrolyses glycerol phosphate and 4-nitrophenyl phosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
9033-33-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
highly expressed in glioblastoma stem-like cells compared with normal brain and neural stem cells. Knockdown of isoform E-NPP1 in cultured glioblastoma stem-like cells results in an overall downregulation of stem cell-associated genes, induction of differentiation into astrocytic cell lineage, impairment of sphere formation, in addition to increased cell death, accumulation of cells in G1/G0 cell cycle phase and sensitisation to chemotherapeutic treatment. Knockdown of E-NPP1 affects purine and pyrimidine metabolism. E-NPP1, by acting upstream of E2F1, is indispensable for the maintenance of glioblastoma stem-like cells in vitro and hence required to keep glioblastoma stem-like cells in an undifferentiated, proliferative state
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-UMP + H2O
deoxyuridine + phosphate
show the reaction diagram
-
-
-
?
3'-dUMP + H2O
deoxyuridine + phosphate
show the reaction diagram
-
i.e. 2'-deoxyuridine 3'-phosphate
-
?
3'-UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
?
5'-ATP + H2O
5'-ADP + phosphate
show the reaction diagram
-
-
-
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
show the reaction diagram
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
show the reaction diagram
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
show the reaction diagram
-
i.e. 2'-deoxyinosine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
show the reaction diagram
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dUMP + H2O
deoxyuridine + phosphate
show the reaction diagram
-
i.e. 2'-deoxyuridine 5'-phosphate
-
?
5'-UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
IDP + H2O
IMP + phosphate
show the reaction diagram
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
activation, 10% of Mg2+-activity
Mg2+
-
absolutely dependent on Mg2+, maximal activity at 5 mM Mg2+
Mn2+
-
activation, 10% of Mg2+-activity
Sr2+
-
can replace Ca2+
additional information
-
not activated by Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
deoxyuridine
-
hydrolysis of 5'-dUMP
NaF
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strong inhibitor
PO43-
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hydrolysis of 5'-dUMP
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22
2'-UMP
-
-
0.28
3'-dUMP
-
-
0.24
3'-UMP
-
-
3
5'-dAMP
-
-
3.3
5'-dGMP
-
-
4.4
5'-dIMP
-
-
2.6
5'-dUMP
-
-
17
5'-GMP
-
-
8.6
5'-IMP
-
-
7
5'-TMP
-
-
14
5'-UMP
-
-
1.3
p-nitrophenyl phosphate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
mechanism and subcellular location of NTPDase activation, block of the secretory transport with monensin or brefeldin A, or by targeting to the endoplasmic reticulum (ER) with a signal peptide, cell surface biotinylation, glycosidase sensitivity, fluorescence microscopy, results in contrast to previous report on CD39, NTPDase3 catalytically active in the ER or in the ER-Golgi intermediate compartment, terminal glycosylation in Golgi not essential for activity, wild-type NTPDase3 has probably ATPase activity in a post-ER but pre-Golgi compartment, ER-targeted NTPDase3 as potential tool to study the effects of ATP depletion on ER function under normal and stress conditions
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
-
substrate-dependent
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
NTPDase3 acquires nucleotidase activity as soon as it is natively folded in the ER
Manually annotated by BRENDA team
NTPDase3 activity in, ER-Golgi intermediate compartment (ERGIC)
Manually annotated by BRENDA team
integral plasma membrane proteins
Manually annotated by BRENDA team
PDB
SCOP
CATH
UNIPROT
ORGANISM
-
-
-
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
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2 * 22000, SDS-PAGE
90000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
7 potential N-glycosylation sites, at least one high-mannose or hybrid N-glycan in mature plasma membrane-localized protein, deglycosylation with peptide N-glycosidase
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method with 8% polyethylene glycol 4000, 0.2 M ammonium sulfate, 0.1 M sodium acetate, pH 4.8, and 10 mM CaCl2
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 0.5 mg/ml bovine serum albumin, several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose chromatography
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nickel-nitrilotriacetic acid-agarose chromatography and Sephacryl S-100 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression of NTPDase3 in COS-1 cells, pcDNA3 mammalian expression vector, co-transfection experiments, ER-targeted NTPDase3 construct generated by insertion mutagenesis, catalytically inactive G221A mutant of NTPDase3 as a control
expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells and COS cells
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expressed in Escherichia coli BL21(DE3) cells and COS-1 cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A287C
-
decreased activity
C257S
-
wild type-like activity
D228T
-
decreased dimer fomation tendency and decreased activity towards ADP compared to the wild type enzyme
D228T/K224N
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largely restores the ability to form dimers and shows increased ADPase activity compared to the wild type enzyme
E130Y
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super-active mutant
E130Y/K201M/E216M
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shows increased activity towards ADP
E130Y/K201M/T206K/T207E/E216M
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shows increased activity towards ADP
I170C
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decreased activity
I170E
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decreased dimer fomation tendency and decreased activity towards ADP compared to the wild type enzyme
I170K
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decreased dimer fomation tendency and decreased activity towards ADP compared to the wild type enzyme
S109C
-
decreased activity
S172C
-
decreased activity
S226C
-
decreased activity
S278C
-
decreased activity
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
highly expressed in glioblastoma stem-like cells compared with normal brain and neural stem cells. Knockdown of isoform E-NPP1 in cultured glioblastoma stem-like cells results in an overall downregulation of stem cell-associated genes, induction of differentiation into astrocytic cell lineage, impairment of sphere formation, in addition to increased cell death, accumulation of cells in G1/G0 cell cycle phase and sensitisation to chemotherapeutic treatment. Knockdown of E-NPP1 affects purine and pyrimidine metabolism. E-NPP1, by acting upstream of E2F1, is indispensable for the maintenance of glioblastoma stem-like cells in vitro and hence required to keep glioblastoma stem-like cells in an undifferentiated, proliferative state