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EC Tree
IUBMB Comments The enzyme, which appears to be limited to metazoa, acts on multiple nucleoside diphosphates as well as on D-ribose 5-diphosphate. Specificity depends on species and isoform.
The taxonomic range for the selected organisms is: Rattus norvegicus The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
tppase, nucleoside diphosphatase, ndpase, inosine diphosphatase, idpase, ntpdase5, ntpdase6, nucleoside triphosphate diphosphohydrolase-1, e-ntpdase1, sa1684,
more
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nucleoside triphosphate diphosphohydrolase
-
adenosine diphosphatase
-
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-
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adenosinepyrophosphatase
-
-
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ectonucleoside triphosphate diphosphohydrolase
-
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guanosine 5'-diphosphatase
-
-
-
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guanosine diphosphatase
-
-
-
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inosine 5'-diphosphatase
-
-
-
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inosine diphosphatase
-
-
-
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Lysosomal apyrase-like protein of 70 kDa
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-
-
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nucleoside 5'-diphosphatase
-
-
-
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Nucleoside diphosphatase
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-
-
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nucleoside diphosphate phosphatase
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nucleoside diphosphate phosphohydrolase
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nucleoside triphosphate diphosphohydrolase
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Proto-oncogene cph
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thiaminpyrophosphatase
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type B nucleoside diphosphatase
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type L nucleoside diphosphatase
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additional information
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the enzyme belongs to the ectonucleoside triphosphate diphosphohydrolase, E-NTPDase, family
ADPase
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NTPDase6
-
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-
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NTPDase8
-
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hydrolysis of phosphoric ester
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nucleoside-diphosphate phosphohydrolase
The enzyme, which appears to be limited to metazoa, acts on multiple nucleoside diphosphates as well as on D-ribose 5-diphosphate. Specificity depends on species and isoform.
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ADP + H2O
AMP + phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
ATP + 2 H2O
AMP + 2 phosphate
ATP + H2O
ADP + phosphate
-
-
-
-
?
CDP + H2O
CMP + phosphate
dTDP + H2O
dTMP + phosphate
GDP + H2O
GMP + phosphate
GTP + H2O
GDP + phosphate
weak activity
-
-
?
IDP + H2O
IMP + phosphate
TDP + H2O
TMP + phosphate
-
-
-
?
TPP + H2O
thiamine phosphate + phosphate
UDP + H2O
UMP + phosphate
UTP + H2O
UDP + phosphate
weak activity
-
-
?
additional information
?
-
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
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
sequential dephosphorylation of ATP to ADP and then AMP
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
?
CDP + H2O
CMP + phosphate
-
weak activity
-
?
CDP + H2O
CMP + phosphate
-
weak activity
-
?
CDP + H2O
CMP + phosphate
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weak activity
-
?
CDP + H2O
CMP + phosphate
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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
-
-
?
dTDP + H2O
dTMP + phosphate
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weak activity
-
?
dTDP + H2O
dTMP + phosphate
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14% of the activity with IDP, type L enzyme
-
?
GDP + H2O
GMP + phosphate
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-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
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95% of the activity with IDP, enzyme type B and enzyme type L
-
?
GDP + H2O
GMP + phosphate
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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
-
-
?
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
-
-
?
TPP + H2O
thiamine phosphate + phosphate
-
-
-
?
TPP + H2O
thiamine phosphate + phosphate
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is hydrolyzed twice as efficiently as nucleoside diphosphates
-
?
TPP + H2O
thiamine phosphate + phosphate
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64% of the activity with IDP, enzyme type B. 4% of the activity with IDP, enzyme type L
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?
UDP + H2O
UMP + phosphate
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-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
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?
UDP + H2O
UMP + phosphate
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-
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?
UDP + H2O
UMP + phosphate
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-
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?
UDP + H2O
UMP + phosphate
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59% of activity with IDP, enzyme type B. 88% of the activity with IDP, enzyme type L
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?
UDP + H2O
UMP + phosphate
hydrolyzes nucleoside 5'-diphosphates in the order: UDP, GDP, IDP, GDP
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-
?
additional information
?
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the enzyme may support glycosylation reactions related to quality control in the endoplasmic reticulum
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-
?
additional information
?
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no activity with ADP, nucleoside 5'-triphosphates are hydrolyzed to a minor extend, no hydrolysis of nucleoside 5'-monophosphates
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?
additional information
?
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NTPDase1 hydrolyzes ATP and ADP at a similar rate
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?
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ADP + H2O
AMP + phosphate
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-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
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-
-
?
ATP + H2O
ADP + phosphate
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-
-
-
?
GDP + H2O
GMP + phosphate
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type L enzyme chiefly works in the degradation of nucleoside diphosphates
-
-
?
additional information
?
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the enzyme may support glycosylation reactions related to quality control in the endoplasmic reticulum
-
-
?
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Cd2+
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Cd2+ can partially replace Mn2+, 16%, for TPPase activity. For GDPase activity Ca2+ can be partially replaced by Cd2+, 38%
Manganese
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metalloenzyme contains 0.9 mol zinc and 0.1 mol manganese per mol of 65000 Da subunit
Zinc
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metalloenzyme contains 0.9 mol zinc and 0.1 mol manganese per mol of 65000 Da subunit
additional information
insensitive to Mg2+
Ca2+
required
Ca2+
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can partially replace Mg2+ in activation
Ca2+
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increases hydrolysis of IDP
Ca2+
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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+
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activates
Co2+
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Co2+ can partially replace Mn2+, 20%, for TPPase activity. For GDPase activity Ca2+ can be partially replaced by Co2+, 55%
Mg2+
required
Mg2+
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increases hydrolysis of IDP
Mg2+
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in presence of Mn2+ the activity of the enzyme on the substrates is in decreasing order: GDP, IDP, TPP, UDP, CDP
Mg2+
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divalent cation required, maximum activity with Mg2+, half-maximal activity at 0.4 mM MgCl2
Mn2+
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Mn2+
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can partially replace Mg2+ in activation
Mn2+
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in presence of Mn2+ the activity of the enzyme on the substrates is in decreasing order: TPP, IDP, GDP, UDP, CDP, dTDP
Mn2+
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increases hydrolysis of IDP
Zn2+
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activates
Zn2+
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Zn2+ can partially replace Mn2+, 4%, for TPPase activity. For GDPase activity Ca2+ can be partially replaced by Zn2+, 23%
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1,10-phenanthroline
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2 mM, 66% inhibition
2,2'-bipyridyl
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2 mM, 64% inhibition
ADP
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1 mM, 27% inhibition of thiamin-diphosphatase activity, competitive
chlorpromazine
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1 mM, 15% inhibition
IMP
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slight competitive inhibition of thiamin-diphosphatase activity
NEM
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1 mM, 16% inhibition
Promethazine
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1 mM, 15% inhibition
pyridoxal 5'-phosphate
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1 mM, 43% inhibition of thiamin-diphosphatase activity, competitive
AMP
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slight competitive inhibition of thiamin-diphosphatase activity
AMP
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0.07 mM, , 50% inhibition, type B enzyme
ATP
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ATP
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slight competitive inhibition of thiamin-diphosphatase activity
ATP
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inhibits enzyme form A and B2 from mitochondria
diphosphate
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0.5 mM, 50% inhibition
diphosphate
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complete inhibition at 1 mM, 61% inhibition at 0.06 mM
EDTA
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EDTA
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0.1 mM, complete inhibition
F-
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100 mM KF, 33% inhibition
F-
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50 mM NaF, more than 80% inhibition
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pyridoxal 5'-phosphate
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activation due to Schiff base formation with epsilon-amino groups of Lys residues of the enzyme, Km: 0.0052 mM, no further stimulation of the reaction which is maximally activated by pyridoxal 5'-phosphate
ATP
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0.2 mM, 2fold increase of activity with IDP, 10fold increase of activity with TPP, type L enzyme
ATP
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activates, no stimulation of the reaction which is activated by pyridoxal 5'-phosphate
ATP
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enhances hydrolysis of GDP
ATP
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activates microsomal enzyme and enzyme form B1 from mitochondria
ATP
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0.2 mM ATP stimulates free enzyme 2.6fold when IDP is used as substrate, immobilized enzyme on CNBr-activated Sepharose is activated almost to the same degree, the immobilized enzyme on the 3-O-pyridoxal 5'-phosphate-Sepharose is less sensitive to ATP
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0.66
thiamine diphosphate
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in presence of Mn2+
0.4
GDP
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in presence of Mn2+
0.48
IDP
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native enzyme in presence of ATP
0.54
IDP
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in presence of Mn2+
2.94
IDP
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native enzyme in absesence of ATP
0.216
UDP
pH 7
1.06
UDP
-
in presence of Mn2+
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additional information
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-
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6
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hydrolysis of IDP and TPP, enzyme type B
6 - 9
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hydrolysis of GDP
7
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GDPase activity in presence of Mn2+ and Ca2+
8 - 8.5
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TTPase activity in presence of Ca2+
6.5
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hydrolysis of GDP in presence of Mg2+, TTPase activity in presence of Mg2+
6.5
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hydrolysis of IDP, enzyme type L
7.4
assay at
7.4
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hydrolysis of thiamin-diphosphate in presence of Mn2+
9
-
TPPase activity, enzyme type L
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6 - 8
pH 6.0: about 80% of maximal activity, pH 8.0: about 70% of maximal activity
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37
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assay at
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NTPDase1
UniProt
brenda
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-
brenda
expression of isozymes NTPDase1, -2, and -8 in distinct liver compartments in normal and fibrotic rat liver
brenda
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brenda
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brenda
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brenda
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oviductal and uterine, endothelium, NTPDase1 is located especially in the lamina propria mucosae and uterine blood vessel endothelium
brenda
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NTPDase3
brenda
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epithelium, NTPDase1
brenda
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NTPDase1 in epididymal, NTPDase3 in secretory
brenda
restricted to the canalicular membrane domain of hepatocytes
brenda
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ascites hepatoma AH-66 cells
brenda
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interstitial, NTPDase1
brenda
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NTPDase1
brenda
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-
brenda
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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
brenda
-
NTPDase1
brenda
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of tunica muscularis and blood vessels of the muscular layer of oviductal serosa, NTPDase1
brenda
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round, NTPDase6
brenda
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NTPDase1
brenda
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-
brenda
-
-
brenda
-
brenda
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enzyme type L and enzyme type B
brenda
-
-
brenda
expression of isozymes NTPDase1, -2, and -8 in distinct liver compartments in normal and fibrotic rat liver
brenda
additional information
enzyme tissue localization by in situ immunohistochemistry, overview
brenda
additional information
enzyme tissue localization by in situ immunohistochemistry, overview
brenda
additional information
-
tissue localization of isozymes, overview
brenda
additional information
enzyme tissue localization by in situ immunohistochemistry, overview
brenda
additional information
enzyme tissue localization by in situ immunohistochemistry, overview
brenda
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-
brenda
-
-
brenda
associated with
brenda
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Golgi-phase acrosome, NTPDase6
brenda
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at the lumen side of the membrane
-
brenda
-
-
-
brenda
-
-
brenda
associated with
-
brenda
additional information
-
subcellular localization of isozymes, overview
-
brenda
-
brenda
-
bound
brenda
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metabolism
plasma membrane-bound NTPDases, namely NTPDase1/CD39, NTPDase2/CD39L1, and NTPDase8, represent the major liver ectonucleotidase activities
metabolism
plasma membrane-bound NTPDases, namely NTPDase1/CD39, NTPDase2/CD39L1, and NTPDase8, represent the major liver ectonucleotidase activities
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ENTP1_RAT
511
2
57408
Swiss-Prot
-
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30000
-
4 * 30000, SDS-PAGE
45700
x * 45700, calculation from nucleotide sequence
52000
-
enzyme form A and B2, gel filtration
60000
-
enzyme form B, gel filtration
63000
-
2 * 63000, SDS-PAGE
65000
-
2 * 65000, SDS-PAGE
67000
-
2 * 67000, SDS-PAGE
75000
-
1 * 75000, SDS-PAGE
140000
-
gel filtration
140000
-
enzyme form B1, gel filtration
140000
-
type L enzyme, gel filtration
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?
x * 45700, calculation from nucleotide sequence
tetramer
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4 * 30000, SDS-PAGE
dimer
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2 * 63000, SDS-PAGE
dimer
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2 * 67000, SDS-PAGE
dimer
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2 * 65000, SDS-PAGE
monomer
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1 * 75000, SDS-PAGE
monomer
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1 * 45000, L-type enzyme, SDS-PAGE
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glycoprotein
-
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glycoprotein
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contains 9% carbohydrate
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additional information
-
NTPDase activities are increased in Entpd1-deficient mice
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5
-
10 min, about 40% loss of activity of the native enzyme, about 30% loss of activity of the enzyme after treatment with pyridoxal phosphate and reduction with NaBH4
210211
6
-
10 min, native enzyme and enzyme after treatment with pyridoxal phosphate and reduction with NaBH4, stable
210211
9
-
10 min, about 25% loss of activity of the native enzyme, about 5% loss of activity of the enzyme after treatment with pyridoxal phosphate and reduction with NaBH4
210211
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40
-
about 70% loss of activity after 30 min
45
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pH 7.4, 50 mM triethanolamine hydrochloride, about 80% loss of activity after 16 min, inactivation is decreased by 2 mM pyridoxal phosphate
55
-
5 min, about 50% loss of activity of the immobilized enzyme, complete loss of activity of the free enzyme
50
-
about 70% loss of activity after 2 min, about 85% loss of activity after 5 min
50
-
5 min, immobilized enzyme is stable, free enzyme loses about 90% of its activity
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high resiststance against lipid peroxidation
-
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-18°C, stable for several months
-
-70°C, stable for several weeks
-
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mitochondrial enzyme form A, B1 and B2
-
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expression of NTPDase1, NTPDase2, and NTPDase3 in COS-7 cells
-
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analysis
-
because of its resistance against lipid peroxidation nucleoside diphosphatase is a well-suited intrinsic parameter to estimate this effect of lipid peroxidation on the microsomal membrane
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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
De Groot, H.; Noll, T.; Toelle, T.
Loss of latent activity of liver microsomal membrane enzymes evoked by lipid peroxidation. Studies of nucleoside diphosphatase, glucose-6-phosphatase, and UDP glucuronyltransferase
Biochim. Biophys. Acta
815
91-96
1985
Rattus norvegicus
brenda
Sano, S.; Matsuda, Y.; Miyamoto, S.; Nakagawa, H.
Thiamine pyrophosphatase and nucleoside diphosphatase in rat brain
Biochem. Biophys. Res. Commun.
118
292-298
1984
Rattus norvegicus
brenda
Ohkubo, I.; Taniguchi, N.; Mitsuyama, T.; Tsukada, Y.; Makita, A.
Comparative studies on nucleoside diphosphatase of rat ascites hepatoma and rat liver: activity level, purification and properties
Int. J. Biochem.
14
1075-1081
1982
Rattus norvegicus
brenda
Yang, W.J.; Kim, K.W.; Lee, B.J.
Rat brain nucleoside diphosphatase: purification and properties of type L isoenzyme
Arch. Pharm. Res.
17
256-262
1994
Rattus norvegicus
-
brenda
Brandan, E.; Fleischer, B.
Orientation and role of nucleosidediphosphatase and 5'-nucleotidase in Golgi vesicles from rat liver
Biochemistry
21
4640-4645
1982
Rattus norvegicus
brenda
Ohkubo, I.; Ishibashi, T.; Taniguchi, N.; Makita, A.
Purification and characterization of nucleoside diphosphatase from rat-liver microsomes. Evidence for metalloenzyme and glycoprotein
Eur. J. Biochem.
112
111-118
1980
Rattus norvegicus
brenda
Kawakita, N.; Yamazaki, M.
Immobilization of nucleoside diphosphatase at its allosteric site using immobilized derivatives of pyridoxal 5 -phosphate
Arch. Biochem. Biophys.
204
326-330
1980
Rattus norvegicus
brenda
Kawakita, N.; Yamazaki, M.
Allosteric properties of nucleoside diphosphatase. Activation by pyridoxal 5'-phosphate and specific modification of effector binding sites
Biochem. J.
17
3546-3551
1978
Rattus norvegicus
brenda
Ishibashi, T.; Gasa, S.; Ohkubo, I.; Makita, A.
Affinity purification and some properties of nucleoside diphosphatase from rat liver cytosol
Biochim. Biophys. Acta
525
265-274
1978
Rattus norvegicus
brenda
Shirasaka, T.; Arima, T.; Fujii, S.
Studies on mitochondrial and microsomal nucleoside diphosphatases of rat liver
J. Biochem.
76
99-106
1974
Rattus norvegicus
brenda
Failer, B.U.; Braun, N.; Zimmermann, H.
Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase
J. Biol. Chem.
277
36978-36986
2002
Rattus norvegicus (Q8K4Y7)
brenda
Martin-Satue, M.; Lavoie, E.G.; Pelletier, J.; Fausther, M.; Csizmadia, E.; Guckelberger, O.; Robson, S.C.; Sevigny, J.
Localization of plasma membrane bound NTPDases in the murine reproductive tract
Histochem. Cell Biol.
131
615-628
2009
Mus musculus, Mus musculus C57BL/6, Rattus norvegicus
brenda
Fausther, M.; Lecka, J.; Soliman, E.; Kauffenstein, G.; Pelletier, J.; Sheung, N.; Dranoff, J.; Sevigny, J.
Coexpression of ecto-5'-nucleotidase/CD73 with specific NTPDases differentially regulates adenosine formation in the rat liver
Am. J. Physiol. Gastrointest. Liver Physiol.
302
447-459
2012
Rattus norvegicus (P97687), Rattus norvegicus (Q5DRK1), Rattus norvegicus Sprague-Dawley (P97687), Rattus norvegicus Sprague-Dawley (Q5DRK1)
brenda