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Enzyme Nomenclature
Information on EC 3.1.3.31 - nucleotidase
for references in articles please use BRENDA:EC3.1.3.31
Word Map on EC 3.1.3.31
- 3.1.3.31
- adp
- triphosphate
-
purinergic
-
diphosphohydrolase
- purine
- vascular
- platelet
- apyrase
- monophosphate
- diabetes
- arterial
- deaminase
- injury
- inflammation
- lymphocyte
- pyrophosphate
- bone
- pyrimidine
- calcification
-
ecto-nucleoside
-
synaptosomes
- ecto-atpase
- adpase
- suramin
-
tregs
-
3.6.1.5
- 5'-triphosphate
-
ecto-enzymes
-
adenosinergic
-
pseudoxanthoma
-
ppads
-
atp-induced
-
purinoceptors
-
surface-located
- atpgammas
-
hypophosphatemic
-
phosphohydrolysis
- rickets
- elasticum
-
alpha,beta-methylene
-
beta-methylene
-
tcf7l2
-
stippling
- medicine
-
nucleotide-mediated
-
atp-mediated
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
3.1.3.31
-
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RECOMMENDED NAME
GeneOntology No.
nucleotidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a nucleotide + H2O = a nucleoside + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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.
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CAS REGISTRY NUMBER
COMMENTARY
9033-33-4
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Col-0 wild-type, alx8 mutant, fry1-1 mutant, T-DNA insertional knockout mutant, normal growth conditions and drought stress
SwissProt
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-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
PAN proteins are not essential based on the robust growth of the panA panB double knockout strain. Deletion of genes encoding either PanA renders cells more sensitive to growth on organic versus inorganic nitrogen sources and hypo-osmotic stress and limits growth in the presence of L-canavanine
malfunction
-
PAN proteins are not essential based on the robust growth of the panA panB double knockout strain. Deletion of genes encoding either PanA renders cells more sensitive to growth on organic versus inorganic nitrogen sources and hypo-osmotic stress and limits growth in the presence of L-canavanine
-
physiological function
-
the native enzyme might be used by the parasite to control the levels of host extracellular nucleotides released by locally-damaged tissues in an effort to modulate immune intervention and inflammation
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
physiological function
-
the native enzyme might be used by the parasite to control the levels of host extracellular nucleotides released by locally-damaged tissues in an effort to modulate immune intervention and inflammation
-
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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
adenosine 3',5'-bisphosphate + H2O
AMP + phosphate
-
Golgi-resident gPAPP protein has 3'-phosphoadenosine 5'-phosphate-phosphatase activity, functional role of gPAPP protein in the formation of skeletal elements through endochondral ossification in mice
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
-
-
?
UDP + H2O
uridine + diphosphate
best substrate, the enzyme shows some specificity for uridine nucleotides
-
-
?
UTP + H2O
UMP + diphosphate
the enzyme shows some specificity for uridine nucleotides
-
-
?
2',3'-cyclic-AMP + H2O
adenosine + phosphate
-
isozyme NSP-I: 3% of the activity with 5'-AMP, isozyme NSP-II: 1% of the activity with 5'-AMP
-
?
2',3'-cyclic-AMP + H2O
adenosine + phosphate
-
5% of the activity of 3'-AMP, cytosolic enzyme
-
?
2'-AMP + H2O
adenosine + phosphate
-
isozyme NSP-I: 52% of the activity with 5'-AMP, isozyme NSP-II: 54% of the activity with 5'-AMP
-
?
2'-AMP + H2O
adenosine + phosphate
-
68% of the activity of 3'-AMP, cytosolic enzyme
-
?
2-naphthol phosphate + H2O
2-naphthol + phosphate
-
lysosomal enzyme
-
?
3'-AMP + H2O
adenosine + phosphate
-
isozyme NSP-I: 59% of the activity with 5'-AMP, isozyme NSP-II: 54% of the activity with 5'-AMP
-
?
3'-AMP + H2O
adenosine + phosphate
-
3.2% of the activity with 5'-dUMP
-
-
-
3'-CMP + H2O
cytidine + phosphate
-
2% of the activity with 5'-dUMP
-
?
3'-dAMP + H2O
3'-deoxyadenosine + phosphate
-
9.1% of the activity with 5'-dUMP
-
?
3'-dAMP + H2O
3'-deoxyadenosine + phosphate
-
131% of the activity of 3'-AMP, cytosolic enzyme
-
?
3'-dAMP + H2O
3'-deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 3'-phosphate
-
?
3'-dAMP + H2O
3'-deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 3'-phosphate
-
?
3'-dCMP + H2O
deoxycytidine + phosphate
-
i.e. 2'-deoxycytidine 3'-phosphate
-
?
3'-dCMP + H2O
deoxycytidine + phosphate
-
6.5% of the activity with 5'-dUMP
-
?
3'-dCMP + H2O
deoxycytidine + phosphate
-
101% of the activity of 3'-AMP, cytosolic enzyme
-
?
3'-dCMP + H2O
deoxycytidine + phosphate
-
i.e. 2'-deoxycytidine 3'-phosphate
-
?
3'-dCMP + H2O
deoxycytidine + phosphate
-
i.e. 2'-deoxycytidine 3'-phosphate
-
?
3'-dTMP + H2O
deoxythymidine + phosphate
-
113.7% of the activity with 5'-dUMP
-
?
3'-dTMP + H2O
deoxythymidine + phosphate
-
77% of the activity of 3'-AMP, cytosolic enzyme
-
?
3'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 3'-phosphate
-
?
3'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 3'-phosphate
-
?
3'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 3'-phosphate
-
?
3'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 3'-phosphate
-
?
3'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 3'-phosphate
-
?
3'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 3'-phosphate
-
?
3'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 3'-phosphate
-
?
3'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 3'-phosphate
-
?
3'-dUMP + H2O
deoxyuridine + phosphate
-
153.5% of the activity with 5'-dUMP
-
?
3'-GMP + H2O
guanosine + phosphate
-
49% of the activity of 3'-AMP, cytosolic enzyme
-
?
3'-UMP + H2O
uridine + phosphate
-
122.8% of the activity with 5'-dUMP
-
?
3'-UMP + H2O
uridine + phosphate
-
14% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-AMP + H2O
adenosine + phosphate
-
hydrolyzed by both isozymes NSP-I and NSP-II
-
?
5'-AMP + H2O
adenosine + phosphate
-
49% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-CMP + H2O
cytidine + phosphate
-
97% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
isozyme NSP-I: 90% of the activity with 5'-AMP, isozyme NSP-II: 101% of the activity with 5'-AMP
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
128% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dAMP + H2O
deoxyadenosine + phosphate
-
i.e. 2'-deoxyadenosine 5'-phosphate
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
-
7.8% of the activity with 5'-dUMP
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
-
i.e. 2'-deoxycytidine 5'-phosphate
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
-
i.e. 2'-deoxycytidine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
142% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dGMP + H2O
deoxyguanosine + phosphate
-
i.e. 2'-deoxyguanosine 5'-phosphate
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
-
i.e. 2'-deoxyinosine 5'-phosphate
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
-
46% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
-
i.e. 2'-deoxyinosine 5'-phosphate
-
?
5'-dIMP + H2O
deoxyinosine + phosphate
-
i.e. 2'-deoxyinosine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
77.7% of the activity with 5'-dUMP
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
60% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dTMP + H2O
deoxythymidine + phosphate
-
i.e. 2'-deoxythymidine 5'-phosphate
-
?
5'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 5'-phosphate
-
?
5'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 5'-phosphate
-
?
5'-dUMP + H2O
deoxyuridine + phosphate
-
28% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 5'-phosphate
-
?
5'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 5'-phosphate
-
?
5'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 5'-phosphate
-
?
5'-dUMP + H2O
deoxyuridine + phosphate
-
i.e. 2'-deoxyuridine 5'-phosphate
-
?
5'-GMP + H2O
guanosine + phosphate
-
31% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-IMP + H2O
inosine + phosphate
-
28% of the activity of 3'-AMP, cytosolic enzyme
-
?
5'-IMP + H2O
inosine + phosphate
-
13% of the activity with 5'-dUMP
-
?
5'-UMP + H2O
uridine + phosphate
-
isozyme NSP-I: 156% of the activity with 5'-AMP, isozyme NSP-II: 205% of the activity with 5'-AMP
-
?
5'-UMP + H2O
uridine + phosphate
-
8.2% of the activity with 5'-dUMP
-
?
5'-UMP + H2O
uridine + phosphate
-
22% of the activity of 3'-AMP, cytosolic enzyme
-
?
ADP + H2O
?
-
isozyme NSP-I: 58% of the activity with 5'-AMP, isozyme NSP-II: 51% of the activity with 5'-AMP
-
-
?
AMP + H2O
adenosine + phosphate
-
100% activity, 15fold preference for AMP over IMP
-
-
?
AMP + H2O
adenosine + phosphate
-
no inhibitory effects by fluoxetine and nortriptyline on AMP hydrolysis in cerebral cortex and hippocampus
-
-
?
AMP + H2O
adenosine + phosphate
-
no inhibitory effects by fluoxetine and nortriptyline on AMP hydrolysis in cerebral cortex and hippocampus
-
-
?
ATP + H2O
?
-
isozyme NSP-I: 17% of the activity with 5'-AMP, isozyme NSP-II: 1% of the activity with 5'-AMP
-
-
?
ATP + H2O
?
-
influence of tricyclic antidepressant on hydrolysis of ATP, affection of the ecto-nucleotidase pathway by fluoxetine and nortriptyline, extracellular adenosine levels can be modulated
-
-
?
ATP + H2O
?
-
influence of tricyclic antidepressant on hydrolysis of ATP, affection of the ecto-nucleotidase pathway by fluoxetine and nortriptyline, extracellular adenosine levels can be modulated
-
-
?
ATP + H2O
ADP + phosphate
18.2% compared to the activity with to ATP
-
-
?
ATP + H2O
ADP + phosphate
a model is proposed in which sampylated proteins associate with the PAN-A/1 AAA+ ATPase in proteasome-mediated proteolysis and/or protein remodeling
-
-
?
ATP + H2O
ADP + phosphate
18.2% compared to the activity with to ATP
-
-
?
ATP + H2O
ADP + phosphate
a model is proposed in which sampylated proteins associate with the PAN-A/1 AAA+ ATPase in proteasome-mediated proteolysis and/or protein remodeling
-
-
?
dsDNA 3' phosphate + H2O
dsDNA + phosphate
-
repair of DNA-damage
-
-
?
GTP + H2O
GDP + phosphate
24% compared to the activity with ATP
-
-
?
GTP + H2O
GDP + phosphate
24% compared to the activity with ATP
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
isozyme NSP-I: 51% of the activity with 5'-AMP, isozyme NSP-II: 33% of the activity with 5'-AMP
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
140% of the activity of 3'-AMP, cytosolic enzyme
-
?
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
Bothrops pradoi
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comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
very low rates of dephosphorylation with beta-glycerophosphate, D-ribose 5-phosphate and 4-nitrophenyl phosphate, while 3',5'-cyclic AMP is not hydrolysed significantly
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
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additional information
?
-
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substrate specificities of SurE, YfbR, and YjjG, overview
-
-
-
additional information
?
-
-
the enzyme prefers nucleoside triphosphates, no activity with AMP and diphosphate
-
-
-
additional information
?
-
-
the wild type enzyme does not efficiently hydrolyze ADP
-
-
-
additional information
?
-
nucleotidase activity of ER-targeted NTPDase3 decreases the efficiency of protein folding in ER
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
comparative analysis of nucleotidase activities of crude venoms in representative species
-
-
-
additional information
?
-
-
physiological significance for spleen cytoplasm in the reutilization of nucleotides, especially for thymidine and uridine nucleotides
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
AMP + H2O
adenosine + phosphate
-
100% activity, 15fold preference for AMP over IMP
-
-
?
dsDNA 3' phosphate + H2O
dsDNA + phosphate
-
repair of DNA-damage
-
-
?
UDP + H2O
uridine + diphosphate
Q8AVX8
best substrate, the enzyme shows some specificity for uridine nucleotides
-
-
?
UTP + H2O
UMP + diphosphate
Q8AVX8
the enzyme shows some specificity for uridine nucleotides
-
-
?
additional information
?
-
-
physiological significance for spleen cytoplasm in the reutilization of nucleotides, especially for thymidine and uridine nucleotides
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Cu2+
Mg2+
Mn2+
additional information
Ca2+
-
ADPase and ATPase activity depending on, Mg2+ is slightly preferred to Ca2+
Co2+
-
100-150 mM Mg2+ required for optimal activation, Mg2+ can be replaced by Mn2+ or Co2+
Mg2+
-
dephosphorylation of 3'(5')-dUMP, 3'(5')-dTMP and 3'-UMP more readily in presence
Mg2+
-
ADPase and ATPase activity depending on, Mg2+ is slightly preferred to Ca2+
Mg2+
-
100-150 mM Mg2+ required for optimal activation, Mg2+ can be replaced by Mn2+ or Co2+
Mn2+
-
100-150 mM Mg2+ required for optimal activation, Mg2+ can be replaced by Mn2+ or Co2+
additional information
-
dependent on divalent cations: SurE prefers Mn2+ to Co2+, Ni2+, and Mg2+, YfbR prefers Co2+ to Mn2+ and Cu2+, YjjG prefers Mg2+ to Mn2+ and Co2+, in descending orders, overview
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-N,N-diethyl-beta-gamma-dibromomethylene-D-adenosine-5-triphosphate
-
i.e. ARL67156, concentrations of 100-300 microM
beta,gamma-imidoATP
-
the inhibitory respond is blocked by 8-phenyltheophylline and superfusion with adenosine deaminase
fluoxetine
-
tricyclic antidepressant, acute and chronic treatment, concentrations of 100, 250, and 500 microM, decreases ATP (17.8%) hydrolysis in hippocampus, decreases ATP (25.5%) hydrolysis in the cerebral cortex, no inhibitory effects on AMP hydrolysis in cerebral cortex and hippocampus
NaN3
-
inhibits the enzyme from digestive gland by 36% at 0.01 mM, no inhibition of the enzyme from nervous ganglia
NEM
-
inhibits the enzyme from digestive gland by 45%, no inhibition of the enzyme from nervous ganglia
nortriptyline
-
tricyclic antidepressant, acute and chronic treatment, concentrations of 100, 250, and 500 microM, decreases ATP (16.3%) hydrolysis in the hippocampus, increases ATP (32.3%) hydrolysis in the cerebral cortex, no inhibitory effects on AMP hydrolysis in cerebral cortex and hippocampus
ATP
-
the inhibitory respond is blocked by 8-phenyltheophylline and superfusion with adenosine deaminase
additional information
-
inhibitory potency of nucleotides, overview, AMP is a poor inhibitor for SurE, YfbR, and YjjG, YjjG is not inhibitable by nucleotides
-
additional information
-
the nervous ganglia enzyme is not significantly affected by vanadate, levamisole, NaN3, the digestive gland enzyme is not affected by vanadate, levamisole, ouabain, and oligomycin
-
additional information
-
the organoselenium compounds 2-phenyl-1,2-benzisoselenazol-3(2H)-one (i.e. ebselen) or diphenyl diselenide counteract the glutamate-induced stimulation of ecto-nucleotide activities, concentrations of 0.3-3 microM
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
deoxythymidine 5'-phosphate p-nitrophenyl ester
-
activation of hydrolysis of 3'-dTMP
fluoxetine
-
tricyclic antidepressant, concentrations of 100, 250, and 500 microM, chronic treatment increases ADP (80.1%) and AMP (33.3%) hydrolysis, no alteration of enzyme activities by acute treatment
glutamate
-
increases nucleotide hydrolysis at low concentrations (10 and 100 microM), effect counteracted by 2-phenyl-1,2-benzisoselenazol-3(2H)-one (i.e. ebselen), that acts as glutathione peroxidase mimic, or by diphenyl diselenide
NaCl
-
the PAN-A/1 protein requires high salt for optimal ATPase activity and complex stability. At 1.4 M NaCl, the ATPase activity of PAN-A/1 is reduced to only 43% of activity in the presence of 2 M NaCl. Further reduction of NaCl concentrations to levels of 0.751 M NaCl result in PAN-A/1 protein with only 5-8% of the ATPase activity detected at 2 M NaCl
nortriptyline
-
tricyclic antidepressant, concentrations of 100, 250, and 500 microM, chronic treatment increases ATP (32.3%), ADP (51.8%), and AMP (59.5%) hydrolysis in the cerebral cortex, activation of ADP hydrolysis (49.8%) in acute treatment in cerebral cortex
additional information
-
the nervous ganglia enzyme is not significantly affected by vanadate, levamisole, NaN3, the digestve gland enzyme is not affected by vanadate, levamisole, ouabain, and oligomycin
-
additional information
-
the enzyme may possess a regulatory site topographically different from the catalytic site
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.023
3'-phosphoadenosine 5'-phosphate
-
recombinant protein, DELTA55 gPAPP mutant
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
characterization of mutants of the inositol polyphosphate 1-phosphatase SAL1, alx8 mutant, fry1-1 mutant and T-DNA insertional knockout mutant have markedly increased resistance to drought when water is withheld from soil-grown intact plants, effect of mutations in SAL1 by microarray and metabolom analysis, biomass at maturity, plant water use efficiency, stomatal index, morphology or aperture unaffected under well-water conditions, inactivation of SAL1 protein results in altered osmoprotectants, higher leaf relative water content and maintenance of viable tissues during prolonged water stress
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, higher levels of nucleotidase activity than in the genus Micurus, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, higher levels of nucleotidase activity than in the genus Micurus
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, higher levels of nucleotidase activity than in the genus Micurus, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, pyrophosphate assay reveals highest nucleotidase activity among tested venoms, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, higher levels of nucleotidase activity than in the genus Micurus, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, higher levels of nucleotidase activity than in the genus Micurus, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, higher levels of nucleotidase activity than in the genus Micurus, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, higher levels of nucleotidase activity than in the genus Micurus, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, higher levels of nucleotidase activity than in the genus Micurus, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, higher levels of nucleotidase activity than in the genus Micurus, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, nucleotidase activity determined by pyrophosphate assay, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, most intense bands in 5'-nucleotidase gels among the tested venoms, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, higher levels of nucleotidase activity than in the genus Micurus, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, higher levels of nucleotidase activity than in the genus Micurus, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, most intense bands in 5'-nucleotidase gels among the tested venoms
additional information
-
comparative analysis of nucleotidase activities of crude venoms, higher levels of nucleotidase activity than in the genus Micurus, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, higher levels of nucleotidase activity than in the genus Micurus, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, higher levels of nucleotidase activity than in the genus Micurus, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
Bothrops pradoi
-
comparative analysis of nucleotidase activities of crude venoms, higher levels of nucleotidase activity than in the genus Micurus, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, higher levels of nucleotidase activity than in the genus Micurus, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, higher levels of nucleotidase activity than in the genus Micurus, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, nucleotidase activities tested by pyrophosphate assay, no or minimal bands in zymographic analyses; comparative analysis of nucleotidase activities of crude venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, no or minimal bands in zymographic analyses of 5'-nucleotidase activities, lowest 5'-nucleotidase activity among Crotales; comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, minimal bands in zymographic analyses
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, minimal bands in zymographic analyses
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
additional information
-
comparative analysis of nucleotidase activities of crude venoms, nucleotidase activities tested by pyrophosphate assay and by zymographic analyses, similar nucleotidase activities but different banding pattern by zymography point to structural differences, omnipresence of nucleotidases reveals a role within the repertoire of enzymes involved in immobilization and death of preys
additional information
-
comparative analysis of nucleotidase activities of crude venoms, liberation of pyrophosphate or orthophosphate from AMP, ADP or ATP after incubation with selected venoms, 5'-nucleotidase activity of venoms determined by zymographic analyses, low activity levels, no banding in zymographic analyses
additional information
-
inactivation of gPAPP protein leads to neonatal lethality, lung abnormalities resembling atelectasis, and dwarfism characterized by aberrant cartilage morphology, undersulfated chondroitin in the absence of functional enzyme, loss of enzyme function leads to perturbations in the levels of heparan sulfate species in lung tissue and whole embryos, clearance of the nucleotide product of sulfotransferases within the Golgi plays an important role in glycosaminoglycan sulfation, unique genetic basis for chondrodysplasia
additional information
-
extracellular nucleotidase activity and ATP release upon deoxygenation, extracellular ATP determined with the luciferin-luciferase technique, increase of extracellular ATP in the presence of ectonucleotidase inhibitor reveals presence of ectonucleotidase activity, ATP release of erythrocytes not influenced by oxygenation degree
additional information
-
glutamate stimulates ecto-nucleotidase activities in cerebellar granule cells, increase of extracellular adenosine levels, the analyzed organoselenium compounds do not modify basal enzyme activities but they counteract the increase in the nucleotide hydrolysis produced by neurotoxic agents likely via their antioxidant properties
additional information
-
significant changes in NTPDase activities when the tricyclic antidepressants fluoxetine and nortriptyline are tested in vitro, affection of the ecto-nucleotidase pathway by modulating changes of extracellular adenosine levels
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
8.5
6
-
substrates 3'-UMP, 5'-UMP, 5'-dTMP, 3'-dCMP, 3'-CMP, 5'-dCMP, 3'-dAMP, 3'-AMP, 5'-IMP
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 60
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 50
-
25: about 70% of maximal activity, 50°C: about 10% of maximal activity
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
chondrocytes of costal cartilage and in the surrounding perichondrium, hypocellular with abnormal, fibrous-appearing structures
additional information
-
expression in, morphological differences in the absence of functional protein
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
type II orientation, entire catalytic core of the gPAPP protein resides within
NTPDase3 acquires nucleotidase activity as soon as it is natively folded in the ER
-
the enzyme is secreted from the 4th-stage larvae, it contains a putative signal sequence at the N-terminus
-
-
the enzyme is secreted from the 4th-stage larvae, it contains a putative signal sequence at the N-terminus
-
-
NTPDase3 activity in, ER-Golgi intermediate compartment (ERGIC)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dodecamer
oligomer
-
x * 35700, YjjG, SDS-PAGE and gel filtration, x * 41600, SurE, SDS-PAGE and gel filtration
additional information
-
SurE, YfbR, and YjjG show monomeric, dimeric, trimeric, and tetrameric forms, overview
dodecamer
-
PAN-A/1 is associated as a dodecamer with a configuration in TEM suggesting a complex of two stacked hexameric rings
dodecamer
-
PAN-A/1 is associated as a dodecamer with a configuration in TEM suggesting a complex of two stacked hexameric rings
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
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
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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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
serum albumin or dithiothreitol stabilizes cytosolic enzyme at 37°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is stabilized by 2 M NaCl with a decrease in activity at lower concentrations of salt that correlated with dissociation of the dodecamer into trimers to monomers. The PAN-A/1 complex is more stable in low salt buffer with KCl compared to NaCl based on ATPase activity assay
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, phosphocellulose column chromatography, and UltraPak TSK G4000gel filtration
-
Ni-NTA agarose chromatography
nickel-nitrilotriacetic acid-agarose chromatography and Sephacryl S-100 gel filtration
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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
expression of recombinant gPAPP protein using a baculovirus system, full-lenght protein and the DELTA55 gPAPP mutant, a secreted form that lacks the transmembrane domain
-
gene xapy, DNA and amino acid sequence determination and analysis, expression in HEK293 cells as functional secreted recombinant enzyme
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D228T
-
decreased dimer fomation tendency and decreased activity towards ADP compared to the wild type enzyme
D228T/K224N
-
largely restores the ability to form dimers and shows increased ADPase activity compared to the wild type enzyme
I170E
-
decreased dimer fomation tendency and decreased activity towards ADP compared to the wild type enzyme
I170K
-
decreased dimer fomation tendency and decreased activity towards ADP compared to the wild type enzyme
additional information
additional information
-
lack of the N-terminus leads to a soluble enzyme
additional information
lack of the N-terminus leads to a soluble enzyme
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
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