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ADP + H2O
AMP + phosphate
ATP + 2 H2O
AMP + 2 phosphate
ATP + H2O
ADP + phosphate
CDP + H2O
CMP + phosphate
CTP + 2 H2O
CMP + 2 phosphate
-
-
-
-
?
CTP + H2O
CDP + phosphate
3.8% of the specific activity with GDP
-
-
?
dADP + H2O
dAMP + phosphate
dCDP + H2O
dCMP + phosphate
low activity
-
-
?
dGDP + H2O
dGMP + phosphate
dTDP + H2O
dTMP + phosphate
GDP + H2O
GMP + phosphate
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
IDP + H2O
IMP + phosphate
ITP + 2 H2O
IMP + 2 phosphate
-
-
-
-
?
ITP + H2O
IDP + phosphate
6% of the specific activity with GDP
-
-
?
TDP + H2O
TMP + phosphate
TPP + H2O
thiamine phosphate + phosphate
UDP + H2O
UMP + phosphate
UDP + H2O
UMP + phosphate + H+
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
?
UTP + H2O
UDP + phosphate
additional information
?
-
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
ADPase activity of GS52 is consistently more than 1.5fold higher than the ATPase activity
-
-
?
ADP + H2O
AMP + phosphate
24.4% of the specific activity with GDP
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
no activity
-
-
?
ADP + H2O
AMP + phosphate
-
weak activity
-
?
ADP + H2O
AMP + phosphate
-
weak activity
-
?
ADP + H2O
AMP + phosphate
-
weak activity
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
high activity
-
-
?
ADP + H2O
AMP + phosphate
high activity
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
best substrate
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
best substrate
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
best substrate
-
-
?
ADP + H2O
AMP + phosphate
best substrate
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
ADPase activity of GS52 is consistently more than 1.5fold higher than the ATPase activity
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
sequential dephosphorylation of ATP to ADP and then AMP
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
CDP + H2O
CMP + phosphate
12.9% of the specific activity with GDP
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
?
CDP + H2O
CMP + phosphate
-
weak activity
-
?
CDP + H2O
CMP + phosphate
-
weak activity
-
?
CDP + H2O
CMP + phosphate
-
weak activity
-
?
CDP + H2O
CMP + phosphate
-
43% of the activity with IDP, enzyme type B. 8% of the activity with IDP, enzyme type L
-
?
CDP + H2O
CMP + phosphate
hydrolyzes nucleoside 5'-diphosphates in the order: UDP, GDP, IDP, GDP
-
-
?
CDP + H2O
CMP + phosphate
moderate activity
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
?
CDP + H2O
CMP + phosphate
higher activity
-
-
?
dADP + H2O
dAMP + phosphate
low activity
-
-
?
dADP + H2O
dAMP + phosphate
very low activity
-
-
?
dGDP + H2O
dGMP + phosphate
low activity
-
-
?
dGDP + H2O
dGMP + phosphate
very low activity
-
-
?
dTDP + H2O
dTMP + phosphate
-
weak activity
-
?
dTDP + H2O
dTMP + phosphate
-
14% of the activity with IDP, type L enzyme
-
?
GDP + H2O
GMP + phosphate
-
110% of the activity with IDP
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
best substrate
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
95% of the activity with IDP, enzyme type B and enzyme type L
-
?
GDP + H2O
GMP + phosphate
-
type L enzyme chiefly works in the degradation of nucleoside diphosphates
-
-
?
GDP + H2O
GMP + phosphate
hydrolyzes nucleoside 5'-diphosphates in the order: UDP, GDP, IDP, GDP
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
moderate activity
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
moderate activity
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
very low activity
-
-
?
GDP + H2O
GMP + phosphate
very low activity
-
-
?
GDP + H2O
GMP + phosphate
very low activity
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
4.4% of the specific activity with GDP
-
-
?
GTP + H2O
GDP + phosphate
weak activity
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
-
?
IDP + H2O
IMP + phosphate
55.5% of the specific activity with GDP
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
?
IDP + H2O
IMP + phosphate
hydrolyzes nucleoside 5'-diphosphates in the order: UDP, GDP, IDP, GDP
-
-
?
IDP + H2O
IMP + phosphate
low activity
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
?
TDP + H2O
TMP + phosphate
-
-
-
?
TDP + H2O
TMP + phosphate
moderate activity
-
-
?
TDP + H2O
TMP + phosphate
moderate activity
-
-
?
TPP + H2O
thiamine phosphate + phosphate
-
-
-
?
TPP + H2O
thiamine phosphate + phosphate
-
is hydrolyzed twice as efficiently as nucleoside diphosphates
-
?
TPP + H2O
thiamine phosphate + phosphate
-
64% of the activity with IDP, enzyme type B. 4% of the activity with IDP, enzyme type L
-
?
UDP + H2O
UMP + phosphate
-
90% of the activity with UDP
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
19.8% of the specific activity with GDP
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
59% of activity with IDP, enzyme type B. 88% of the activity with IDP, enzyme type L
-
?
UDP + H2O
UMP + phosphate
hydrolyzes nucleoside 5'-diphosphates in the order: UDP, GDP, IDP, GDP
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
best substrate
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UTP + H2O
UDP + phosphate
1.2% of the specific activity with GDP
-
-
?
UTP + H2O
UDP + phosphate
-
-
-
-
?
UTP + H2O
UDP + phosphate
-
-
-
-
?
UTP + H2O
UDP + phosphate
weak activity
-
-
?
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY1 exhibits a clear preference towards substrate UDP, supporting previous reports indicating that it functions as UDP/GDPase
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY1 exhibits a clear preference towards substrate UDP, supporting previous reports indicating that it functions as UDP/GDPase
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY2 exhibits a clear preference towards the substrate UDP/GDP, supporting previous reports indicating that it functions as UDP/GDPase
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY2 exhibits a clear preference towards the substrate UDP/GDP, supporting previous reports indicating that it functions as UDP/GDPase
-
-
-
additional information
?
-
-
GS52 enzyme exhibits broad substrate specificity, but its activity on pyrimidine nucleotides and diphosphate nucleotides is significantly higher than on ATP due to low specificity for the adenine base within the substrate binding pocket of the enzyme. No hydrolytic activity with AMP
-
-
?
additional information
?
-
no activity with ATP
-
-
?
additional information
?
-
-
no activity with ATP
-
-
?
additional information
?
-
-
NTPDase1 hydrolyzes ATP and ADP at a similar rate
-
-
?
additional information
?
-
-
the enzyme specifically binds to P2Y1 and P2Y2 receptors
-
-
?
additional information
?
-
-
the enzyme specifically binds to P2Y1 and P2Y2 receptors
-
-
?
additional information
?
-
-
NTPDase1 hydrolyzes ATP and ADP at a similar rate
-
-
?
additional information
?
-
the enzyme may support glycosylation reactions related to quality control in the endoplasmic reticulum
-
-
?
additional information
?
-
no activity with ADP, nucleoside 5'-triphosphates are hydrolyzed to a minor extend, no hydrolysis of nucleoside 5'-monophosphates
-
-
?
additional information
?
-
-
NTPDase1 hydrolyzes ATP and ADP at a similar rate
-
-
?
additional information
?
-
purified SA1684 protein has Mn2+- or Co2+-dependent hydrolyzing activity against nucleoside diphosphates. The enzyme shows or poor activity with NTPS or NMPs, substrate specificity, overview
-
-
-
additional information
?
-
-
purified SA1684 protein has Mn2+- or Co2+-dependent hydrolyzing activity against nucleoside diphosphates. The enzyme shows or poor activity with NTPS or NMPs, substrate specificity, overview
-
-
-
additional information
?
-
purified SA1684 protein has Mn2+- or Co2+-dependent hydrolyzing activity against nucleoside diphosphates. The enzyme shows or poor activity with NTPS or NMPs, substrate specificity, overview
-
-
-
additional information
?
-
the TTHA1091 protein does not possess ADK activity but instead possesses adenosine diphosphatase (ADPase) activity
-
-
-
additional information
?
-
the enzyme encoded by TTHA1091 shows degradation of ADP to AMP and thus possesses adenosine diphosphatase (ADPase) activity, but it does not catalyse the phosphorylation of adenosine when ATP or ADP are used as phosphate donors. The ADPase activity is specific for ADP and CDP. No or poor activity with UDP, TDP, and dCDP, substrate specificity, overview
-
-
-
additional information
?
-
the TTHA1091 protein does not possess ADK activity but instead possesses adenosine diphosphatase (ADPase) activity
-
-
-
additional information
?
-
the enzyme encoded by TTHA1091 shows degradation of ADP to AMP and thus possesses adenosine diphosphatase (ADPase) activity, but it does not catalyse the phosphorylation of adenosine when ATP or ADP are used as phosphate donors. The ADPase activity is specific for ADP and CDP. No or poor activity with UDP, TDP, and dCDP, substrate specificity, overview
-
-
-
additional information
?
-
the TTHA1091 protein does not possess ADK activity but instead possesses adenosine diphosphatase (ADPase) activity
-
-
-
additional information
?
-
the enzyme encoded by TTHA1091 shows degradation of ADP to AMP and thus possesses adenosine diphosphatase (ADPase) activity, but it does not catalyse the phosphorylation of adenosine when ATP or ADP are used as phosphate donors. The ADPase activity is specific for ADP and CDP. No or poor activity with UDP, TDP, and dCDP, substrate specificity, overview
-
-
-
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Cd2+
-
Cd2+ can partially replace Mn2+, 16%, for TPPase activity. For GDPase activity Ca2+ can be partially replaced by Cd2+, 38%
Manganese
-
metalloenzyme contains 0.9 mol zinc and 0.1 mol manganese per mol of 65000 Da subunit
Zinc
-
metalloenzyme contains 0.9 mol zinc and 0.1 mol manganese per mol of 65000 Da subunit
Ca2+
-
required
Ca2+
-
10 mM, stimulation
Ca2+
-
the most effective activating divalent cation
Ca2+
activates, slightly more effective than Mg2+
Ca2+
-
can partially replace Mg2+ in activation
Ca2+
-
increases hydrolysis of IDP
Ca2+
-
in presence of Mn2+ the activity of the enzyme on the substrates is in decreasing order: GDP, TPP, IDP, UDP, CDP
Ca2+
dependent on. AT 0.5 mM UDP, maximal activity is obtained at 1 mM Ca2+, higher Ca2+ concentrations reduce catalytic activity
Co2+
-
required
Co2+
-
Co2+ can partially replace Mn2+, 20%, for TPPase activity. For GDPase activity Ca2+ can be partially replaced by Co2+, 55%
Mg2+
-
required
Mg2+
-
10 mM, stimulation
Mg2+
activates, slightly less effective than Ca2+
Mg2+
-
increases hydrolysis of IDP
Mg2+
-
in presence of Mn2+ the activity of the enzyme on the substrates is in decreasing order: GDP, IDP, TPP, UDP, CDP
Mg2+
-
divalent cation required, maximum activity with Mg2+, half-maximal activity at 0.4 mM MgCl2
Mn2+
-
required
Mn2+
-
10 mM, stimulation
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
in presence of Mn2+ the activity of the enzyme on the substrates is in decreasing order: TPP, IDP, GDP, UDP, CDP, dTDP
Mn2+
-
increases hydrolysis of IDP
Mn2+
dependent on, activates at 0.5-12.5 mM
Zn2+
-
20% of the activity with Mg2+
Zn2+
-
Zn2+ can partially replace Mn2+, 4%, for TPPase activity. For GDPase activity Ca2+ can be partially replaced by Zn2+, 23%
additional information
-
activating cations in descending effectivity order: Ca2+, Mg2+, Ni2+, Co2+ = Mn2+ = Cd2+, Zn2+ = Cu2+ for ATPase activity, and Ca2+, Mg2+, Ni2+ = Co2+, Mn2+ = Cu2+, Cd2+ = Zn2+ for ADPase activity
additional information
insensitive to Mg2+
additional information
no or very poor activation by Cu2+, Ni2+, Zn2+, Mg2+, and Ca2+ at 0.5 mM
additional information
-
no or very poor activation by Cu2+, Ni2+, Zn2+, Mg2+, and Ca2+ at 0.5 mM
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1,10-phenanthroline
-
2 mM, 66% inhibition
2,2'-bipyridyl
-
2 mM, 64% inhibition
ADP
-
1 mM, 27% inhibition of thiamin-diphosphatase activity, competitive
Ca2+
about 90% inhibition at 10 mM
chlorpromazine
-
1 mM, 15% inhibition
GDP
substrate inhibition at high concentration
GDPbetaS
a non-hydrolyzable analogue of GDP
GTPgammaS
a non-hydrolyzable analogue of GTP
IMP
-
slight competitive inhibition of thiamin-diphosphatase activity
Mg2+
complete inhibition at 10 mM
Mn2+
complete inhibition at 10 mM
NEM
-
1 mM, 16% inhibition
Promethazine
-
1 mM, 15% inhibition
pyridoxal 5'-phosphate
-
1 mM, 43% inhibition of thiamin-diphosphatase activity, competitive
UDP
substrate inhibition at high concentration
AMP
-
slight competitive inhibition of thiamin-diphosphatase activity
AMP
-
0.07 mM, , 50% inhibition, type B enzyme
ATP
-
IC50 for isoenzyme 1 is 6.5 mM, IC50 for isoenzyme 2 is 4.0 mM
ATP
-
slight competitive inhibition of thiamin-diphosphatase activity
ATP
-
inhibits enzyme form A and B2 from mitochondria
diphosphate
-
complete inhibition at 1 mM, 61% inhibition at 0.06 mM
diphosphate
-
0.5 mM, 50% inhibition
EDTA
-
-
EDTA
-
complete inhibition at 1 M
EDTA
-
0.1 mM, complete inhibition
F-
-
100 mM KF, 33% inhibition
F-
-
50 mM NaF, more than 80% inhibition
H2O2
-
in the presence of H2O2, UDPase activity is lower than that of GDPase. GDPase activity significantly decreases at high concentrations. Inverse relationship between the decline in UDPase activity and the increase in the concentration of H2O2
H2O2
-
in the presence of H2O2, UDPase activity is lower than that of GDPase. GDPase activity significantly decreases at high concentrations. Inverse relationship between the decline in UDPase activity and the increase in the concentration of H2O2
H2O2
-
in the presence of H2O2, UDPase activity is lower than that of GDPase. GDPase activity significantly decreases at high concentrations. Inverse relationship between the decline in UDPase activity and the increase in the concentration of H2O2
H2O2
-
in the presence of H2O2, UDPase activity is lower than that of GDPase. GDPase activity significantly decreases at high concentrations. Inverse relationship between the decline in UDPase activity and the increase in the concentration of H2O2
menadione
-
-
menadione
-
UDPase activity increases at lower concentrations of the oxidant and decreases at higher concentrations
menadione
-
UDPase activity increases at lower concentrations of the oxidant and decreases at higher concentrations
superoxide
-
GDPase activity significantly decreases at high concentrations
superoxide
-
GDPase activity significantly decreases at high concentrations
superoxide
-
GDPase activity significantly decreases at high concentrations
superoxide
-
GDPase activity significantly decreases at high concentrations
additional information
-
no inhibition by 10 mM ascorbate, 80 mM molybdate, 20 mM KF or 10 mM vanadate
-
additional information
-
GDPase and UDPase activities are generally affected by H2O2 and the superoxide ion generated by menadione
-
additional information
-
GDPase and UDPase activities are generally affected by H2O2 and the superoxide ion generated by menadione
-
additional information
-
GDPase and UDPase activities are generally affected by H2O2 and the superoxide ion generated by menadione
-
additional information
the ADPase activity is inhibited by divalent cations
-
additional information
-
GDPase and UDPase activities are generally affected by H2O2 and the superoxide ion generated by menadione
-
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Adenocarcinoma, Mucinous
Ultrastructural cytochemistry of human gastric cancer: electron microscopic observations of five organellae marker enzymes.
Adenoma, Pleomorphic
Phosphatase enzymes. Cytochemical study of pleomorphic adenoma and normal human salivary glands.
Alzheimer Disease
[Electron-cytochemical study of microglia in Alzheimer's disease and senile dementia]
Avitaminosis
[Enzyme activity of thiamine diphosphate biosynthesis and degradation in the mouse liver in the dynamics of B1 avitaminosis development]
Bone Resorption
Thiamine pyrophosphatase activity in the Golgi apparatus of calcitonin-treated osteoclasts.
Brain Diseases
The cytochemistry of anoxic and anoxicischemic encephalopathy in rats. III. Alterations in the neuronal Golgi apparatus identified by nucleoside diphosphatase activity.
Brain Ischemia
Postischemic alterations in ultrastructural cytochemistry of neuronal Golgi apparatus.
Carcinoma, Hepatocellular
Comparative studies on nucleoside diphosphatase of rat ascites hepatoma and rat liver: activity level, purification and properties.
Carcinoma, Hepatocellular
[Various enzymes of isolated nuclear membranes and cell nuclei of the liver and hepatoma 27 of rats]
Dehydration
On the involvement of the Golgi apparatus and GERL in processing of secretion products and some enzyme activities in the rat pituitary mammotroph.
Dementia
Loss of endoplasmic reticulum-associated enzymes in affected brain regions in Huntington's disease and Alzheimer-type dementia.
Huntington Disease
Loss of endoplasmic reticulum-associated enzymes in affected brain regions in Huntington's disease and Alzheimer-type dementia.
Infections
Cytochemical localization of ATP diphosphohydrolase from Leishmania (Viannia) braziliensis promastigotes and identification of an antigenic and catalytically active isoform.
Infections
Novel Nucleoside Diphosphatase Contributes to Staphylococcus aureus Virulence.
Leishmaniasis
Cytochemical localization of ATP diphosphohydrolase from Leishmania (Viannia) braziliensis promastigotes and identification of an antigenic and catalytically active isoform.
Neoplasm Metastasis
A novel photoelectrochemical immunosensor by integration of nanobody and ZnO nanorods for sensitive detection of nucleoside diphosphatase kinase-A.
Neoplasm Metastasis
Genome-wide mRNA and microRNA profiling of the NCI 60 cell-line screen and comparison of FdUMP[10] with fluorouracil, floxuridine, and topoisomerase 1 poisons.
Neoplasms
A novel photoelectrochemical immunosensor by integration of nanobody and ZnO nanorods for sensitive detection of nucleoside diphosphatase kinase-A.
Neoplasms
ENTPD5: identification of splicing variants and their impact on cancer survival.
Neoplasms
Fully human anti-CD39 antibody potently inhibits ATPase activity in cancer cells via uncompetitive allosteric mechanism.
Neoplasms
Histochemical observations on NDPase and TPPase in cerebral tumours.
Neoplasms
Overexpression of CD39 in hepatocellular carcinoma is an independent indicator of poor outcome after radical resection.
Neoplasms
Phosphatase enzymes. Cytochemical study of pleomorphic adenoma and normal human salivary glands.
Neoplasms
Sialyltransferase and nucleoside diphosphatase as markers for tumor monitoring.
Neoplasms
Ticlopidine in its prodrug form is a selective inhibitor of human NTPDase1.
Neoplasms
[Ultracytochemical study of the nucleoside phosphatase activity of nuclei of epithelial cells of the gastric mucosa and of stomach cancer cells in humans]
Peripheral Arterial Disease
Aberrant Circulating Levels of Purinergic Signaling Markers are Associated with Several Key Aspects of Peripheral Atherosclerosis and Thrombosis.
Pulmonary Disease, Chronic Obstructive
Is the purinergic pathway involved in the pathology of COPD? Decreased lung CD39 expression at initial stages of COPD.
Reperfusion Injury
Contribution of E-NTPDase1 (CD39) to renal protection from ischemia-reperfusion injury.
Scrapie
Ultrastructural cytochemical studies of cerebral microvasculature in scrapie infected mice.
Stomach Neoplasms
Ultrastructural cytochemical study of enzymes expressed by signet ring cells in gastric cancer.
Stomach Neoplasms
Ultrastructural cytochemistry of human gastric cancer: electron microscopic observations of five organellae marker enzymes.
Thrombosis
Ticlopidine in its prodrug form is a selective inhibitor of human NTPDase1.
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NTPDase3 in cells from the stratified esophageal and forestomach epithelia, and in some enteroendocrine cells of the gastric antrum. NTPDase3 and -2 are coexpressed within the myenteric and submucosal plexuses, as well as in the nerve terminals of the smooth muscle layer and mucosa
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restricted to the canalicular membrane domain of hepatocytes
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ascites hepatoma AH-66 cells
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NTPDase1 and NTPDase2
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NTPDase1 and NTPDase2
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oviductal and uterine, endothelium, NTPDase1 is located especially in the lamina propria mucosae and uterine blood vessel endothelium
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oviductal and uterine, endothelium, NTPDase1 is located especially in the lamina propria mucosae and uterine blood vessel endothelium
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enzyme type L and enzyme type B
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NTPDase3
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NTPDase3
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epithelium, NTPDase1
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epithelium, NTPDase1
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NTPDase1 in epididymal, NTPDase3 in secretory
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NTPDase1 in epididymal, NTPDase3 in secretory
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NTPDase1 in epididymal, NTPDase3 in secretory
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while all cell layers of the esophagus express NTPDase3, NTPDase3 localization in the forestomach is limited to the basal cell layer
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while all cell layers of the esophagus express NTPDase3, NTPDase3 localization in the forestomach is limited to the basal cell layer
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endothelium and hepatic central vein
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endothelium and hepatic central vein
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expression of isozymes NTPDase1, -2, and -8 in distinct liver compartments in normal and fibrotic rat liver
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expression of isozymes NTPDase1, -2, and -8 in distinct liver compartments in normal and fibrotic rat liver
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interstitial, NTPDase1
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interstitial, NTPDase1
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NTPDase1
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NTPDase1
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serous acinar cells of parotid glands
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serous acinar cells of parotid glands
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parenchyma, NTPDase1 and NTPDase2, the latter in association with connective tissue. NTPDase3 is located in the apical pole of the epithelial cells lining the lumen of the secretory portion of the prostate gland
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parenchyma, NTPDase1 and NTPDase2, the latter in association with connective tissue. NTPDase3 is located in the apical pole of the epithelial cells lining the lumen of the secretory portion of the prostate gland
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NTPDase3 in epithelial cells in serous acini of salivary glands and mucous acini and duct cells of sublingual salivary glands
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NTPDase3 in epithelial cells in serous acini of salivary glands and mucous acini and duct cells of sublingual salivary glands
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NTPDase1
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NTPDase1
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NTPDase1
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of tunica muscularis and blood vessels of the muscular layer of oviductal serosa, NTPDase1
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of tunica muscularis and blood vessels of the muscular layer of oviductal serosa, NTPDase1
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of tunica muscularis and blood vessels of the muscular layer of oviductal serosa, NTPDase1
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round, NTPDase6
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round, NTPDase6
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NTPDase1
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NTPDase1
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NTPDase1
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additional information
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tissue localization of isozymes, overview
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additional information
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specific localization of NTPDase3 in the digestive system, by semiquantitative RT-PCR, immunohistochemistry, and in situ activity assay, detailed overview
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specific localization of NTPDase3 in the digestive system, by semiquantitative RT-PCR, immunohistochemistry, and in situ activity assay, detailed overview
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additional information
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tissue localization of isozymes, overview
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additional information
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tissue localization of isozymes, overview
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additional information
enzyme tissue localization by in situ immunohistochemistry, overview
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additional information
enzyme tissue localization by in situ immunohistochemistry, overview
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evolution
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GS52 is a member of the NTPDase/apyrase family
evolution
the enzyme is a family member of the COG1839 family, defined as adenosine-specific kinase family based on structural analysis and the adenosine-binding ability
evolution
the enzyme is a family member of the COG1839 family, defined as adenosine-specific kinase family based on structural analysis and the adenosine-binding ability
evolution
the SA1684 gene product carries theDUF402domain, which is found in RNA-binding proteins, and has amino acid sequence similarity with a nucleoside diphosphatase, Streptomyces coelicolor SC4828 protein
evolution
the seven member Arabidopsis apyrase family contains representatives in each clade and are clustered into the AtAPY1-2 clade I (GDA1-like), the AtAPY3-6 (clade II) and AtAPY7 in clade III. The clade I (GDA-like) Arabidopsis members (AtAPY1 andAtAPY2) form a distinct clade with the other characterized plant apyrases, human apyrases and the yeast GDA1 enzyme. The protein structure of the seven Arabidopsis apyrase proteins outline the apyrase conserved domain GDA1_CD39 and predicted transmembrane helices
evolution
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the enzyme is a family member of the COG1839 family, defined as adenosine-specific kinase family based on structural analysis and the adenosine-binding ability
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evolution
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the SA1684 gene product carries theDUF402domain, which is found in RNA-binding proteins, and has amino acid sequence similarity with a nucleoside diphosphatase, Streptomyces coelicolor SC4828 protein
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evolution
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the enzyme is a family member of the COG1839 family, defined as adenosine-specific kinase family based on structural analysis and the adenosine-binding ability
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evolution
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the enzyme is a family member of the COG1839 family, defined as adenosine-specific kinase family based on structural analysis and the adenosine-binding ability
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evolution
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the enzyme is a family member of the COG1839 family, defined as adenosine-specific kinase family based on structural analysis and the adenosine-binding ability
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evolution
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the enzyme is a family member of the COG1839 family, defined as adenosine-specific kinase family based on structural analysis and the adenosine-binding ability
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evolution
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the enzyme is a family member of the COG1839 family, defined as adenosine-specific kinase family based on structural analysis and the adenosine-binding ability
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evolution
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the enzyme is a family member of the COG1839 family, defined as adenosine-specific kinase family based on structural analysis and the adenosine-binding ability
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malfunction
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macrophages isolated from NTPDase1-null mice are devoid of all ADPase and most ATPase activities when compared with wild type macrophages. NTPDase1-null macrophages exposed to millimolar concentrations of ATP are more susceptible to cell death, release more interleukin-1beta and interleukin-18 after TLR2 or TLR4 priming, and incorporate the fluorescent dye Yo-Pro-1 more efficiently (suggestive of increased pore formation) than wild type cells
malfunction
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nucleotide hydrolysis is impaired in the wall of Entpd1-/- vessels compared with Entpd1+/+ aortas, which display significant ADPase and ATPase activity
malfunction
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the mean glial Ca2+ response to ATP was significantly larger in the presence of an NTPDase inhibitor
malfunction
enzyme knock-out mice recapitulate the desbuquois dysplasia type 1 phenotype
malfunction
immunochemical and genetic suppression of AtAPY1 and AtAPY2 results in an increase in extracellular ATP
malfunction
the SA1684-deletion mutant exhibits drastically decreased virulence in a silkworm (Bombyx mori) infection model, in which the LD50 against silkworm larvae is more than 10times that of the parent strain. The SA1684-deletion mutant also exhibits decreased exotoxin production and colony-spreading ability. Introduction of wild-type SA1684 to the SA1684-deletion mutant restores the hemolysin production, nuclease production, and the colony-spreading activity
malfunction
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the SA1684-deletion mutant exhibits drastically decreased virulence in a silkworm (Bombyx mori) infection model, in which the LD50 against silkworm larvae is more than 10times that of the parent strain. The SA1684-deletion mutant also exhibits decreased exotoxin production and colony-spreading ability. Introduction of wild-type SA1684 to the SA1684-deletion mutant restores the hemolysin production, nuclease production, and the colony-spreading activity
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malfunction
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the mean glial Ca2+ response to ATP was significantly larger in the presence of an NTPDase inhibitor
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malfunction
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nucleotide hydrolysis is impaired in the wall of Entpd1-/- vessels compared with Entpd1+/+ aortas, which display significant ADPase and ATPase activity
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metabolism
plasma membrane-bound NTPDases, namely NTPDase1/CD39, NTPDase2/CD39L1, and NTPDase8, represent the major liver ectonucleotidase activities
metabolism
roles of the Arabidopsis thaliana apyrase family in regulating endomembrane NDP/NMP homoeostasis, overview. The AtAPY1-6 Arabidopsis thaliana enzymes all exhibit classic apyrase-like NTPase and/or NDPases activities, with an absence of NMP activity
metabolism
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the organism shows a basic mechanism to cope with oxidative stress, suggesting that the pathogen might activate mechanisms for UDPase synthesis at lower concentrations of superoxide. Differential response to oxidative stress by different Candida species, overview
metabolism
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the organism shows a basic mechanism to cope with oxidative stress, suggesting that the pathogen might activate mechanisms for UDPase synthesis at lower concentrations of superoxide. Differential response to oxidative stress by different Candida species, overview
metabolism
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the organism shows a basic mechanism to cope with oxidative stress, suggesting that the pathogen might activate mechanisms for UDPase synthesis at lower concentrations of superoxide. Differential response to oxidative stress by different Candida species, overview
metabolism
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the organism shows a basic mechanism to cope with oxidative stress, suggesting that the pathogen might activate mechanisms for UDPase synthesis at lower concentrations of superoxide. Differential response to oxidative stress by different Candida species, overview
metabolism
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plasma membrane-bound NTPDases, namely NTPDase1/CD39, NTPDase2/CD39L1, and NTPDase8, represent the major liver ectonucleotidase activities
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physiological function
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NTPDase1 is the dominant ectonucleotidase responsible for the hydrolysis of ATP and ADP at the surface of mouse primary macrophages. NTPDase1 regulates P2X7-dependent responses in peritoneal macrophages
physiological function
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functional roles of NTPDase3 in association with NTPDase2 and ecto-5'-nucleotidase, in epithelial functions such as secretion and in enteric neurotransmission
physiological function
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important role for the Glycine max ecto-apyrase GS52 in rhizobial root hair infection and root nodule formation
physiological function
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NTPDase1 controls endothelial P2Y receptor-dependent relaxation, regulating both agonist level and P2 receptor reactivity. NTPDase1 differentially influences UTP and ATP responses in vivo
physiological function
the enzyme is critical for glycosaminoglycan biosynthesis in cartilage and endochondral ossification
physiological function
both AtAPY1 and AtAPY2 have been shown to play numerous physiological roles in pollen development, vegetative growth and stomata opening/closure. AtAPY1 and AtAPY2 function as plant endo-apyrases and are necessary for lumenal glycosylation. The Arabidopsis apyrases family members have possible roles in regulating endomembrane NDP/NMP (nucleoside monophosphate) homoeostasis. AtAPY 1 and AtAPY2 are able to function as internal Golgi lumenal NDPases
physiological function
RNA sequence analysis reveals thatSA1684 is required for the expression of the virulence regulatory genes agr, sarZ, and sarX, as well as metabolic genes involved in glycolysis and fermentation pathways. These findings suggest that the nucleoside diphosphatase SA1684 links metabolic pathways and virulence gene expression and plays an important role in Staphylococcus aureus virulence in silkworms. Introduction of wild-type SA1684 to the SA1684-deletion mutant restores the hemolysin production, nuclease production, and the colony-spreading activity. Enzyme SA1684 is required for hemolysin production, nuclease production, and colony spreading
physiological function
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the terminal processing of proteins and lipids occurs in the Golgi apparatus and involves the transport of sugar nucleotides into the Golgi lumen by specific carriers and the accumulation of nucleoside diphosphates (NDPs) as a result of oligosaccharide-protein glycosyltransferase activity. NDPs are converted into the corresponding nucleoside monophosphates (NMPs) by nucleoside diphosphatases (NDPases), thus relieving inhibition of sugar transferases. NMPs are then exchanged for equimolecular amounts of cytosolic sugar nucleotides by antiport transport systems. NDPases, commonly GDPase and UDPase, thus play a critical role in glycoprotein maturation and may influence fungal pathogenesis, morphogenesis, and cell wall properties
physiological function
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the terminal processing of proteins and lipids occurs in the Golgi apparatus and involves the transport of sugar nucleotides into the Golgi lumen by specific carriers and the accumulation of nucleoside diphosphates (NDPs) as a result of oligosaccharide-protein glycosyltransferase activity. NDPs are converted into the corresponding nucleoside monophosphates (NMPs) by nucleoside diphosphatases (NDPases), thus relieving inhibition of sugar transferases. NMPs are then exchanged for equimolecular amounts of cytosolic sugar nucleotides by antiport transport systems. NDPases, commonly GDPase and UDPase, thus play a critical role in glycoprotein maturation and may influence fungal pathogenesis, morphogenesis, and cell wall properties
physiological function
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the terminal processing of proteins and lipids occurs in the Golgi apparatus and involves the transport of sugar nucleotides into the Golgi lumen by specific carriers and the accumulation of nucleoside diphosphates (NDPs) as a result of oligosaccharide-protein glycosyltransferase activity. NDPs are converted into the corresponding nucleoside monophosphates (NMPs) by nucleoside diphosphatases (NDPases), thus relieving inhibition of sugar transferases. NMPs are then exchanged for equimolecular amounts of cytosolic sugar nucleotides by antiport transport systems. NDPases, commonly GDPase and UDPase, thus play a critical role in glycoprotein maturation and may influence fungal pathogenesis, morphogenesis, and cell wall properties
physiological function
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the terminal processing of proteins and lipids occurs in the Golgi apparatus and involves the transport of sugar nucleotides into the Golgi lumen by specific carriers and the accumulation of nucleoside diphosphates (NDPs) as a result of oligosaccharide-protein glycosyltransferase activity. NDPs are converted into the corresponding nucleoside monophosphates (NMPs) by nucleoside diphosphatases (NDPases), thus relieving inhibition of sugar transferases. NMPs are then exchanged for equimolecular amounts of cytosolic sugar nucleotides by antiport transport systems. NDPases, commonly GDPase and UDPase, thus play a critical role in glycoprotein maturation and may influence fungal pathogenesis, morphogenesis, and cell wall properties
physiological function
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RNA sequence analysis reveals thatSA1684 is required for the expression of the virulence regulatory genes agr, sarZ, and sarX, as well as metabolic genes involved in glycolysis and fermentation pathways. These findings suggest that the nucleoside diphosphatase SA1684 links metabolic pathways and virulence gene expression and plays an important role in Staphylococcus aureus virulence in silkworms. Introduction of wild-type SA1684 to the SA1684-deletion mutant restores the hemolysin production, nuclease production, and the colony-spreading activity. Enzyme SA1684 is required for hemolysin production, nuclease production, and colony spreading
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physiological function
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functional roles of NTPDase3 in association with NTPDase2 and ecto-5'-nucleotidase, in epithelial functions such as secretion and in enteric neurotransmission
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physiological function
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NTPDase1 controls endothelial P2Y receptor-dependent relaxation, regulating both agonist level and P2 receptor reactivity. NTPDase1 differentially influences UTP and ATP responses in vivo
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additional information
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uracil nucleotides induce a strong contractile response in Entpd1-/- denuded aortic rings, ATP and ADP do not display constrictor effect at concentrations below 0.03 mM
additional information
structure comparison of homologous structures of TTHA1091 protein (PDB ID 1VGG) and PAE2307 protein (PDB ID 1WVQ, from Pyrobaculum aerophilum strain ATCC 51768), overview. The model structure also suggests that the beta-phosphate group of ADP (and CDP) can be located near His80
additional information
structure comparison of homologous structures of TTHA1091 protein (PDB ID 1VGG, from Thermus thermophilus strain HB8) and PAE2307 protein (PDB ID 1WVQ), overview. The model structure also suggests that the beta-phosphate group of ADP (and CDP) can be located near His80
additional information
the amino acid residues Tyr88, Asp106, and Asp123/Glu124 of SA1684 protein are required for NDP hydrolysis and Staphylococcus aureus virulence
additional information
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the amino acid residues Tyr88, Asp106, and Asp123/Glu124 of SA1684 protein are required for NDP hydrolysis and Staphylococcus aureus virulence
additional information
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structure comparison of homologous structures of TTHA1091 protein (PDB ID 1VGG, from Thermus thermophilus strain HB8) and PAE2307 protein (PDB ID 1WVQ), overview. The model structure also suggests that the beta-phosphate group of ADP (and CDP) can be located near His80
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additional information
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the amino acid residues Tyr88, Asp106, and Asp123/Glu124 of SA1684 protein are required for NDP hydrolysis and Staphylococcus aureus virulence
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additional information
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structure comparison of homologous structures of TTHA1091 protein (PDB ID 1VGG, from Thermus thermophilus strain HB8) and PAE2307 protein (PDB ID 1WVQ), overview. The model structure also suggests that the beta-phosphate group of ADP (and CDP) can be located near His80
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additional information
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structure comparison of homologous structures of TTHA1091 protein (PDB ID 1VGG) and PAE2307 protein (PDB ID 1WVQ, from Pyrobaculum aerophilum strain ATCC 51768), overview. The model structure also suggests that the beta-phosphate group of ADP (and CDP) can be located near His80
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additional information
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structure comparison of homologous structures of TTHA1091 protein (PDB ID 1VGG, from Thermus thermophilus strain HB8) and PAE2307 protein (PDB ID 1WVQ), overview. The model structure also suggests that the beta-phosphate group of ADP (and CDP) can be located near His80
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additional information
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structure comparison of homologous structures of TTHA1091 protein (PDB ID 1VGG, from Thermus thermophilus strain HB8) and PAE2307 protein (PDB ID 1WVQ), overview. The model structure also suggests that the beta-phosphate group of ADP (and CDP) can be located near His80
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additional information
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structure comparison of homologous structures of TTHA1091 protein (PDB ID 1VGG, from Thermus thermophilus strain HB8) and PAE2307 protein (PDB ID 1WVQ), overview. The model structure also suggests that the beta-phosphate group of ADP (and CDP) can be located near His80
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additional information
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structure comparison of homologous structures of TTHA1091 protein (PDB ID 1VGG) and PAE2307 protein (PDB ID 1WVQ, from Pyrobaculum aerophilum strain ATCC 51768), overview. The model structure also suggests that the beta-phosphate group of ADP (and CDP) can be located near His80
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additional information
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uracil nucleotides induce a strong contractile response in Entpd1-/- denuded aortic rings, ATP and ADP do not display constrictor effect at concentrations below 0.03 mM
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D209A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
E182A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
Q216A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
S214A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
C139S
mutant enzyme lacking the single free sulfhydryl is more stable than the wild-type enzyme under refolding conditions, 10-15°C, 2-3 days. The mutant enzyme is less susceptible to oxidative inactivation than the wild-type enzyme
D106A
site-directed mutagenesis, the mutant shows highly reduced nucleoside diphosphatase activity
D123A/E124A
site-directed mutagenesis, the mutant shows highly reduced nucleoside diphosphatase activity
Y88A
site-directed mutagenesis, the mutant shows highly reduced nucleoside diphosphatase activity
D106A
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site-directed mutagenesis, the mutant shows highly reduced nucleoside diphosphatase activity
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D123A/E124A
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site-directed mutagenesis, the mutant shows highly reduced nucleoside diphosphatase activity
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Y88A
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site-directed mutagenesis, the mutant shows highly reduced nucleoside diphosphatase activity
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E493G
the mutant of isoform NTPDase1 shows conversion of ATP/ADP specificity compared to the wild type enzyme
R492G
the mutant of isoform NTPDase1 shows conversion of ATP/ADP specificity compared to the wild type enzyme
R492G/E493G
the mutant of isoform NTPDase1 shows conversion of ATP/ADP specificity compared to the wild type enzyme
additional information
when clade I Arabidopsis apyrases are expressed in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant, both AtAPY1 and AtAPY2 are able to complement the growth phenotype compared to the yeast mutant harbouring the empty vector
additional information
when clade I Arabidopsis apyrases are expressed in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant, both AtAPY1 and AtAPY2 are able to complement the growth phenotype compared to the yeast mutant harbouring the empty vector
additional information
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NTPDase activities are increased in Entpd1-deficient mice
additional information
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generation of E-NTPDase1 knock-out mice
additional information
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generation of E-NTPDase1 knock-out mice
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additional information
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NTPDase activities are increased in Entpd1-deficient mice
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additional information
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NTPDase activities are increased in Entpd1-deficient mice
additional information
introduction of the wild-type SA1684 gene restores the hemolysin production of the SA1684-deletion mutant, whereas none of the alanine-substituted SA1684 mutant genes restores the hemolysin production. Construction of a DELTASA1684 deletion mutant, which exhibits drastically decreased virulence in a silkworm (Bombyx mori) infection model, in which the LD50 against silkworm larvae is more than 10times that of the parent strain. The SA1684-deletion mutant also exhibits decreased exotoxin production and colony-spreading ability. Introduction of wild-type SA1684 to the SA1684-deletion mutant restores the hemolysin production, nuclease production, and the colony-spreading activity
additional information
-
introduction of the wild-type SA1684 gene restores the hemolysin production of the SA1684-deletion mutant, whereas none of the alanine-substituted SA1684 mutant genes restores the hemolysin production. Construction of a DELTASA1684 deletion mutant, which exhibits drastically decreased virulence in a silkworm (Bombyx mori) infection model, in which the LD50 against silkworm larvae is more than 10times that of the parent strain. The SA1684-deletion mutant also exhibits decreased exotoxin production and colony-spreading ability. Introduction of wild-type SA1684 to the SA1684-deletion mutant restores the hemolysin production, nuclease production, and the colony-spreading activity
additional information
-
introduction of the wild-type SA1684 gene restores the hemolysin production of the SA1684-deletion mutant, whereas none of the alanine-substituted SA1684 mutant genes restores the hemolysin production. Construction of a DELTASA1684 deletion mutant, which exhibits drastically decreased virulence in a silkworm (Bombyx mori) infection model, in which the LD50 against silkworm larvae is more than 10times that of the parent strain. The SA1684-deletion mutant also exhibits decreased exotoxin production and colony-spreading ability. Introduction of wild-type SA1684 to the SA1684-deletion mutant restores the hemolysin production, nuclease production, and the colony-spreading activity
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Sano, S.; Matsuda, Y.; Nakagawa, H.
Type B nucleoside-diphosphatase of rat brain. Purification and properties of an enzyme with high thiamin pyrophosphatase activity
Eur. J. Biochem.
171
231-236
1988
Rattus norvegicus
brenda
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Rattus norvegicus
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Oryctolagus cuniculus
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Rattus norvegicus
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Ivanenkov, V.V.; Murphy-Piedmonte, D.M.; Kirley, T.L.
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Homo sapiens (O75354), Homo sapiens
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Rattus norvegicus (Q8K4Y7)
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Uccelletti, D.; OCallaghan, C.; Berninsone, P.; Zemtseva, I.; Abeijon, C.; Hirschberg, C.B.
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Mus musculus, Mus musculus C57BL/6
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brenda
Kauffenstein, G.; Fuerstenau, C.R.; DOrleans-Juste, P.; Sevigny, J.
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Mus musculus, Mus musculus 129 SVJ x C57 BL/6
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Tanaka, K.; Nguyen, C.T.; Libault, M.; Cheng, J.; Stacey, G.
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Glycine max
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Lopez-Esparza, A.; Alvarez-Vargas, A.; Mora-Montes, H.M.; Hernandez-Cervantes, A.; Del Carmen Cano-Canchola, M.; Flores-Carreon, A.
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Krug, U.; Totzauer, R.; Zebisch, M.; Straeter, N.
The ATP/ADP substrate specificity switch between Toxoplasma gondii NTPDase1 and NTPDase3 is caused by an altered mode of binding of the substrate base
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Toxoplasma gondii (Q27895)
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Paganini, C.; Monti, L.; Costantini, R.; Besio, R.; Lecci, S.; Biggiogera, M.; Tian, K.; Schwartz, J.M.; Huber, C.; Cormier-Daire, V.; Gibson, B.G.; Pirog, K.A.; Forlino, A.; Rossi, A.
Calcium activated nucleotidase 1 (CANT1) is critical for glycosaminoglycan biosynthesis in cartilage and endochondral ossification
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Mus musculus (Q8VCF1)
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Chiu, T.Y.; Lao, J.; Manalansan, B.; Loque, D.; Roux, S.J.; Heazlewood, J.L.
Biochemical characterization of Arabidopsis APYRASE family reveals their roles in regulating endomembrane NDP/NMP homoeostasis
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Arabidopsis thaliana (Q9SPM5), Arabidopsis thaliana (Q9SQG2)
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Tomoike, F.; Tsunetou, A.; Kim, K.; Nakagawa, N.; Kuramitsu, S.; Masui, R.
A putative adenosine kinase family protein possesses adenosine diphosphatase activity
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Thermus thermophilus (Q5SJC3), Pyrobaculum aerophilum (Q8ZVF7), Pyrobaculum aerophilum DSM 7523 (Q8ZVF7), Pyrobaculum aerophilum IM2 (Q8ZVF7), Thermus thermophilus DSM 579 (Q5SJC3), Pyrobaculum aerophilum NBRC 100827 (Q8ZVF7), Pyrobaculum aerophilum ATCC 51768 (Q8ZVF7), Pyrobaculum aerophilum JCM 9630 (Q8ZVF7), Thermus thermophilus ATCC 27634 (Q5SJC3)
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Delgado-Carmona, J.D.; Ramirez-Quijas, M.D.; Vega-Gonzalez, A.; Lopez-Romero, E.; Cuellar-Cruz, M.
Changes in GDPase/UDPase enzymatic activity in response to oxidative stress in four Candida species
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Candida albicans, Candida parapsilosis, Pichia kudriavzevii, [Candida] glabrata
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Imae, K.; Saito, Y.; Kizaki, H.; Ryuno, H.; Mao, H.; Miyashita, A.; Suzuki, Y.; Sekimizu, K.; Kaito, C.
Novel nucleoside diphosphatase contributes to Staphylococcus aureus virulence
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Staphylococcus aureus (Q7A4T2), Staphylococcus aureus, Staphylococcus aureus N315 (Q7A4T2)
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