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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
atp pyrophosphatase, atp pyrophosphohydrolase, pk-rec, atpdase 1,
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adenosine triphosphate pyrophosphatase
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ATP pyrophosphatase
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ATP pyrophosphohydrolase
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ATPdiphosphohydrolase
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pyrophosphatase, adenosine triphosphate
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ATPDase 1
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ATP + H2O = AMP + diphosphate
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phosphorous acid anhydride hydrolysis
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ATP diphosphohydrolase (diphosphate-forming)
Also acts on ITP, GTP, CTP and UTP.
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ATP + H2O
AMP + diphosphate
beta, gamma-imido ATP + H2O
AMP + imido diphosphate
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beta,gamma-methylene ATP + H2O
AMP + methylene diphosphate
CTP + H2O
CMP + diphosphate
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dATP + H2O
dAMP + diphosphate
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GTP + H2O
GMP + diphosphate
ITP + H2O
IMP + diphosphate
ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
the enzyme shows DNase activity on both single- and double-stranded DNAs along with the ATPase activity. ATPase activity is independent of both single-stranded and double-stranded DNAs
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beta,gamma-methylene ATP + H2O
AMP + methylene diphosphate
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beta,gamma-methylene ATP + H2O
AMP + methylene diphosphate
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GTP + H2O
GMP + diphosphate
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GTP + H2O
GMP + diphosphate
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ITP + H2O
IMP + diphosphate
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ITP + H2O
IMP + diphosphate
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ATP + H2O
AMP + diphosphate
CTP + H2O
CMP + diphosphate
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GTP + H2O
GMP + diphosphate
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ITP + H2O
IMP + diphosphate
ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
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ATP + H2O
AMP + diphosphate
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ITP + H2O
IMP + diphosphate
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ITP + H2O
IMP + diphosphate
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Ba2+
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no effect
Ba2+
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weak inhibition in absence of Mg2+
Ca2+
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no effect
Ca2+
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required for activity
Ca2+
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required for activity
Ca2+
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required for activity
Co2+
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activating
Mg2+
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no effect
Mn2+
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no effect
Sr2+
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no effect
Sr2+
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partial substitution for Ca2+
Sr2+
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weak inhibition in absence of Mg2+
Zn2+
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activating
Zn2+
preferable divalent cation for ATPase activity
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15-desoxybludein
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0.065 mg/ml, 11% inhibition
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Caffeine
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25% inhibition at 3 mM
cAMP
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20% inhibition at 3 mM
eremantolide C
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0.065 mg/ml, 17% inhibition
glaucolide A
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0.065 mg/ml, 11% inhibition
glaucolide B
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0.065 mg/ml, 16% inhibition
GMP
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competitive inhibition with Ki: 0.001 mM
goyazensolide
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0.065 mg/ml, 10% inhibition
isogoyazensolide
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0.065 mg/ml, 11% inhibition
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licnofolide
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0.065 mg/ml, 22% inhibition
licoflavone B
isolated from Glycyrrhiza inflata, possesses high in vitro schistosomicidal activity against adult worms of Schistosoma mansoni. Licoflavone B causes massive damage in the worm's tegument and inhibits egg laying, without affecting mammalian Vero cells. The tegument of Schistosoma mansoni is crucial for the parasite survival and its host immune defense. Licoflavone B is highly effective in inhibiting Schistosoma mansoni ATP diphosphohydrolase, docking studies with licoflavone B and SmATPase 1 revealing a spontaneous process. The docking study predicts different interactions between licoflavone B and ATPDase 1, corroborating with the in vitro inhibitory activity. Licoflavone B also shows inhibitory activity against ATPase in Schistosoma mansoni
thapsigargicin
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0.065 mg/ml, 57% inhibition
thapsigargin
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inhibits ATP hydrolysis, 70% inhibition at 0.065 mg/ml, mixed type inhibition, little or not affected by changes in free Ca2+ or Mg2+ concentrations, hydrolysis of ADP is not inhibited
additional information
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no inhibition by 0.065 mg/ml 15-desoxygoyazensolide
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additional information
in vitro schistosomicidal activity of the crude extract of Glycyrrhiza inflata roots containing echinatin, licoflavone A and licoflavone B
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additional information
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in vitro schistosomicidal activity of the crude extract of Glycyrrhiza inflata roots containing echinatin, licoflavone A and licoflavone B
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3-isobutyl-1-methylxanthine
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activation in preincubation
glucose
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activation in preincubation
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0.0022
GTP
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with 0.1 mM free Ca2+, pH 8
0.00032
ATP
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with 0.1 mM free Ca2+, pH 8
0.0173
ATP
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37°C, pH 7.4
0.076
ATP
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in presence of ZnCl2 and CaCl2
0.18
ATP
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in presence of 2 mM ZnCl2
0.2
ATP
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without added metal ions
0.83
ATP
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vesicle associated enzyme at pH 7.3
1.28
ATP
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vesicle associated enzyme at pH 9.9
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0.001
GMP
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competitive inhibition
0.02
thapsigargin
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37°C, pH 7.4, inhibition of ATP hydrolysis
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0.0315
licoflavone B
Schistosoma mansoni
pH and temperature not specified in the publication
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0.03 - 0.04
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with ATP as substrate
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6 - 10
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20% activity at pH 6, 50% activity at pH 10
7.4 - 8.8
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much higher activity at pH 8.8
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snake
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acellular slime mold
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strain Belo Horizonte, Brazil
UniProt
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SwissProt
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strain Belo Horizonte, Brazil
UniProt
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additional information
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18 tissues examined
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additional information
ATP diphosphohydrolases are ecto-enzymes localized on the external tegumental surface of Schistosoma mansoni. Worms are maintained in Biomphalaria glabrata snails as intermediate hosts and Mesocricetus auratus hamsters as definitive host
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additional information
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ATP diphosphohydrolases are ecto-enzymes localized on the external tegumental surface of Schistosoma mansoni. Worms are maintained in Biomphalaria glabrata snails as intermediate hosts and Mesocricetus auratus hamsters as definitive host
brenda
additional information
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ATP diphosphohydrolases are ecto-enzymes localized on the external tegumental surface of Schistosoma mansoni. Worms are maintained in Biomphalaria glabrata snails as intermediate hosts and Mesocricetus auratus hamsters as definitive host
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two different localisations found
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human erythrocyte membrane
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human erythrocyte membrane
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Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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127000
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SDS-PAGE, sedimentable enzyme
28000
2 * 28000, SDS-PAGE
61000
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SDS-PAGE, soluble enzyme
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dimer
2 * 28000, SDS-PAGE
tetramer
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4 * 56000, SDS-PAGE and gel filtration
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60
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30 min at 60°C causes no loss of activity
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partial purification
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expression in Escherichia coli
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Heppel, L.A.; Hilmoe, R.J.
Mechanism of enzymatic hydrolysis of adenosinetriphosphate
J. Biol. Chem.
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217-226
1953
Bos taurus, Crotalus adamanteus, Oryctolagus cuniculus, Rattus norvegicus
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Kawamura, M.; Nagano, K.
A calcium ion-dependent ATP pyrophosphohydrolase in Physarum polycephalum
Biochim. Biophys. Acta
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207-219
1975
Physarum polycephalum
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Kawamura, M.; Tonotsuka, N.; Nagano, K.
Change in ATP-pyrophosphohydrolase activity during spherule formation of Physarum polycephalum
Biochim. Biophys. Acta
421
195-202
1976
Physarum polycephalum
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Flodgaard, H.; Torp-Pedersen, C.
A calcium ion-dependent adenosine triphosphate pyrophosphohydrolase in plasma membrane from rat liver. Demonstration that the adenosine triphosphate analogues adenosine 5-[betagamma-imido]triphosphate and adenosine 5-[betagamma-methylene]-triphosphate are substrates for the enzyme
Biochem. J.
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817-820
1978
Rattus norvegicus
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Torp-Pedersen, C.; Flodgaard, H.; Saermark, T.
Studies on a Ca2+-dependent nucleoside triphosphate pyrophosphohydrolase in rat liver plasma membranes
Biochim. Biophys. Acta
571
94-104
1979
Rattus norvegicus
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Capito, K.; Hansen, S.E.; Hedeskov, C.J.; Thams, D.
Presence of ATP-pyrophosphohydrolase in mouse pancreatic islets
Diabetes
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1096-1100
1986
Mus musculus
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Masuda, I.; Hamada, J.; Haas, A.L.; Ryan, L.M.; McCarthy, D.J.
A unique ectonucleotide pyrophosphohyrolase associated with porcine chondrocyte-derived vesicels
J. Clin. Invest.
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699-704
1995
Sus scrofa
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Martins, S.M.; Torres, C.R.; Ferreira, S.T.
Inhibition of the ecto-ATPdiphosphohydrolase of Schistosoma mansoni by thapsigargin
Biosci. Rep.
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369-381
2000
Schistosoma mansoni
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Rashid, N.; Morikawa, M.; Nagahisa, K.; Kanaya, S.; Imanaka, T.
Characterization of a RecA/RAD51 homologue from the hyperthermophilic archaeon Pyrococcus sp. KOD1
Nucleic Acids Res.
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719-726
1997
Thermococcus kodakarensis (P95547)
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Aleixo de Carvalho, L.S.; Geraldo, R.B.; de Moraes, J.; Silva Pinto, P.L.; de Faria Pinto, P.; Pereira, O.d.o.s. .S.; Da Silva Filho, A.A.
Schistosomicidal activity and docking of Schistosoma mansoni ATPDase 1 with licoflavone B isolated from Glycyrrhiza inflata (Fabaceae)
Exp. Parasitol.
159
207-214
2015
Schistosoma mansoni (Q7YTA4), Schistosoma mansoni, Schistosoma mansoni BH (Q7YTA4)
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