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Information on EC 3.6.1.6 - nucleoside diphosphate phosphatase and Organism(s) Rattus norvegicus and UniProt Accession P97687

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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.
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This record set is specific for:
Rattus norvegicus
UNIPROT: P97687
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Word Map
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NTPDase1/CD39
-
nucleoside triphosphate diphosphohydrolase
-
adenosine diphosphatase
-
-
-
-
adenosinepyrophosphatase
-
-
-
-
ADPase
CDPase
-
-
-
-
ectonucleoside triphosphate diphosphohydrolase
-
-
ER-UDPase
-
-
-
-
GDPase
-
-
-
-
guanosine 5'-diphosphatase
-
-
-
-
guanosine diphosphatase
-
-
-
-
IDPase
-
-
-
-
inosine 5'-diphosphatase
-
-
-
-
inosine diphosphatase
-
-
-
-
Lysosomal apyrase-like protein of 70 kDa
-
-
-
-
NDPase
-
-
-
-
NTPDase1
-
-
NTPDase2
-
-
NTPDase3
-
-
NTPDase4
-
-
-
-
NTPDase5
-
-
-
-
NTPDase6
NTPDase8
nucleoside 5'-diphosphatase
-
-
-
-
Nucleoside diphosphatase
-
-
-
-
nucleoside diphosphate phosphatase
-
-
-
-
nucleoside diphosphate phosphohydrolase
-
-
-
-
nucleoside triphosphate diphosphohydrolase
-
Proto-oncogene cph
-
-
-
-
thiaminpyrophosphatase
-
-
-
-
TPPase
-
-
-
-
type B nucleoside diphosphatase
-
-
-
-
type L nucleoside diphosphatase
-
-
-
-
additional information
-
the enzyme belongs to the ectonucleoside triphosphate diphosphohydrolase, E-NTPDase, family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-69-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
dTDP + H2O
dTMP + phosphate
show the reaction diagram
GDP + H2O
GMP + phosphate
show the reaction diagram
GTP + H2O
GDP + phosphate
show the reaction diagram
weak activity
-
-
?
IDP + H2O
IMP + phosphate
show the reaction diagram
TDP + H2O
TMP + phosphate
show the reaction diagram
-
-
-
?
TPP + H2O
thiamine phosphate + phosphate
show the reaction diagram
UDP + H2O
UMP + phosphate
show the reaction diagram
UTP + H2O
UDP + phosphate
show the reaction diagram
weak activity
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
-
type L enzyme chiefly works in the degradation of nucleoside diphosphates
-
-
?
additional information
?
-
the enzyme may support glycosylation reactions related to quality control in the endoplasmic reticulum
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Ni2+
-
activates
Zinc
-
metalloenzyme contains 0.9 mol zinc and 0.1 mol manganese per mol of 65000 Da subunit
additional information
insensitive to Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
2 mM, 66% inhibition
2,2'-bipyridyl
-
2 mM, 64% inhibition
ADP
-
1 mM, 27% inhibition of thiamin-diphosphatase activity, competitive
chlorpromazine
-
1 mM, 15% inhibition
diphosphate
IMP
-
slight competitive inhibition of thiamin-diphosphatase activity
NEM
-
1 mM, 16% inhibition
Promethazine
-
1 mM, 15% inhibition
pyridoxal 5'-phosphate
-
1 mM, 43% inhibition of thiamin-diphosphatase activity, competitive
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4 - 4
GDP
0.48 - 3.5
IDP
0.66
thiamine diphosphate
-
in presence of Mn2+
0.216 - 10
UDP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
diphosphate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
hydrolysis of IDP and TPP, enzyme type B
6 - 9
-
hydrolysis of GDP
7
-
GDPase activity in presence of Mn2+ and Ca2+
7.6
-
assay at
8 - 8.5
-
TTPase activity in presence of Ca2+
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
pH 6.0: about 80% of maximal activity, pH 8.0: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38
-
free enzyme
50
-
immobilized enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
NTPDase1
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression of isozymes NTPDase1, -2, and -8 in distinct liver compartments in normal and fibrotic rat liver
Manually annotated by BRENDA team
-
oviductal and uterine, endothelium, NTPDase1 is located especially in the lamina propria mucosae and uterine blood vessel endothelium
Manually annotated by BRENDA team
-
epithelium, NTPDase1
Manually annotated by BRENDA team
-
NTPDase1 in epididymal, NTPDase3 in secretory
Manually annotated by BRENDA team
restricted to the canalicular membrane domain of hepatocytes
Manually annotated by BRENDA team
-
ascites hepatoma AH-66 cells
Manually annotated by BRENDA team
-
interstitial, NTPDase1
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
of tunica muscularis and blood vessels of the muscular layer of oviductal serosa, NTPDase1
Manually annotated by BRENDA team
-
round, NTPDase6
Manually annotated by BRENDA team
-
NTPDase1
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
Golgi-phase acrosome, NTPDase6
Manually annotated by BRENDA team
-
at the lumen side of the membrane
-
Manually annotated by BRENDA team
additional information
-
subcellular localization of isozymes, overview
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ENTP1_RAT
511
2
57408
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
-
gel filtration
130000
-
gel filtration
140000
30000
-
4 * 30000, SDS-PAGE
45000
-
gel filtration
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 45700, calculation from nucleotide sequence
dimer
monomer
tetramer
-
4 * 30000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
NTPDase activities are increased in Entpd1-deficient mice
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
about 70% loss of activity after 30 min
45
-
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
high resiststance against lipid peroxidation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, stable for several months
-
-70°C, stable for several weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity purification
-
mitochondrial enzyme form A, B1 and B2
-
type L isoenzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of NTPDase1, NTPDase2, and NTPDase3 in COS-7 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Shirasaka, T.; Arima, T.; Fujii, S.
Studies on mitochondrial and microsomal nucleoside diphosphatases of rat liver
J. Biochem.
76
99-106
1974
Rattus norvegicus
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team