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Information on EC 3.6.1.8 - ATP diphosphatase
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3.6.1.8 ATP diphosphataseIUBMB Comments
Also acts on ITP, GTP, CTP and UTP.
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The enzyme appears in viruses and cellular organisms
Synonyms
atp pyrophosphatase, atp pyrophosphohydrolase, pk-rec, atpdase 1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine triphosphate pyrophosphatase
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-
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ATP pyrophosphatase
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ATP pyrophosphohydrolase
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-
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ATPase
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ATPDase 1
pyrophosphatase, adenosine triphosphate
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = AMP + diphosphate
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-
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ATP diphosphohydrolase (diphosphate-forming)
Also acts on ITP, GTP, CTP and UTP.
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CAS REGISTRY NUMBER
COMMENTARY
37289-25-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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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-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Co2+
Mg2+
Mn2+
Sr2+
Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Osteoarthritis
A unique ectonucleotide pyrophosphohydrolase associated with porcine chondrocyte-derived vesicles.
Photophobia
A RecA/RAD51 homologue from a hyperthermophilic archaeon retains the major RecA domain only.
Tuberculosis
Mycobacterial MazG is a novel NTP pyrophosphohydrolase involved in oxidative stress response.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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
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
brenda
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
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (2142 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial purification
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heppel, L.A.; Hilmoe, R.J.
Mechanism of enzymatic hydrolysis of adenosinetriphosphate
J. Biol. Chem.
202
217-226
1953
Bos taurus, Crotalus adamanteus, Oryctolagus cuniculus, Rattus norvegicus
brenda
Kawamura, M.; Nagano, K.
A calcium ion-dependent ATP pyrophosphohydrolase in Physarum polycephalum
Biochim. Biophys. Acta
397
207-219
1975
Physarum polycephalum
brenda
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
brenda
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.
171
817-820
1978
Rattus norvegicus
brenda
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
brenda
Capito, K.; Hansen, S.E.; Hedeskov, C.J.; Thams, D.
Presence of ATP-pyrophosphohydrolase in mouse pancreatic islets
Diabetes
35
1096-1100
1986
Mus musculus
brenda
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.
95
699-704
1995
Sus scrofa
brenda
Martins, S.M.; Torres, C.R.; Ferreira, S.T.
Inhibition of the ecto-ATPdiphosphohydrolase of Schistosoma mansoni by thapsigargin
Biosci. Rep.
20
369-381
2000
Schistosoma mansoni
brenda
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.
25
719-726
1997
Thermococcus kodakarensis (P95547)
brenda
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)
brenda
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