Information on EC 3.6.1.5 - apyrase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
3.6.1.5
-
RECOMMENDED NAME
GeneOntology No.
apyrase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a nucleoside 5'-diphosphate + H2O = a nucleoside 5'-phosphate + phosphate
show the reaction diagram
(1b)
-
-
-
a nucleoside 5'-triphosphate + 2 H2O = a nucleoside 5'-phosphate + 2 phosphate
show the reaction diagram
overall reaction
-
-
-
a nucleoside 5'-triphosphate + H2O = a nucleoside 5'-diphosphate + phosphate
show the reaction diagram
(1a)
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
conversions
-
-
NIL
-
-
Purine metabolism
-
-
Pyrimidine metabolism
-
-
UTP and CTP dephosphorylation II
-
-
SYSTEMATIC NAME
IUBMB Comments
nucleoside triphosphate phosphohydrolase (nucleoside monophosphoate-forming)
Apyrases are active against both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyse NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates. They differ from ATPases, which specifically hydrolyse ATP, by hydrolysing both ATP and ADP. The eukaryotic enzymes requires Ca2+, but Mg2+ can substitute. Most of the ecto-ATPases that occur on the cell surface and hydrolyse extracellular nucleotides belong to this enzyme family.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5'-nucleotidase
A7LH73, A7LH74
-
adenosine diphosphatase
-
-
-
-
ADPase
-
-
-
-
Apy 1
Q06K73
isoform
Apy 2
Q06K77
isoform
APY-1
-
-
APY1
-
isoform
APY2
-
isoform
APY2-type apyrase
G1UFQ9
-
Apyrase
-
-
Apyrase
-
-
Apyrase
Q6QHT8
-
ATP diphosphohydrolase
E0D877
-
ATP diphosphohydrolase
-
-
ATP diphosphohydrolase
Q9FEA6
-
ATP diphosphohydrolase
A1BXT9
-
ATP diphosphohyrolase
-
-
ATP-diphosphatase
-
-
-
-
ATP-diphosphohydrolase
-
-
-
-
ATP-diphosphohydrolase
-
-
ATP-diphosphohydrolase 2
A1BXT9
-
ATPase
O93295
-
ATPase
O35795
-
ATPase
P97687, Q5DRK1
-
ATPase
Rattus norvegicus Sprague-Dawley
O35795, P97687, Q5DRK1
-
-
ATPase 2
A1BXT9
-
ATPDase
-
-
-
-
ATPDase2
A1BXT9
-
Ca2+-activated nucleoside diphosphatase
Q5CXD0
-
CApy
Q5CXD0
gene name
CD39
-
-
CD39
-
-
CD39
Rattus norvegicus Sprague-Dawley
P97687
-
-
CD39 antigen
-
-
-
-
CD39-like ATP diphosphohydrolase
A1BXT9
-
CD39L1
O35795
-
CD39L1
Rattus norvegicus Sprague-Dawley
O35795
-
-
E-NTPDase
-
-
E-NTPDase
P55772
-
E-NTPDase 3
-
-
ecto-5'-nucleotidase
-
-
ecto-5'-nucleotidase
A7LH73, A7LH74
-
ecto-apyrase
-
-
ecto-apyrase
-
-
ecto-apyrase
Q9FVC2
-
ecto-apyrase
-
-
ecto-ATP diphosphohydrolase
-
-
ecto-ATP diphosphohydrolase
Candida parapsilosis CCT3834
-
-
-
ecto-ATP diphosphohydrolase
Q5CXD0
-
ecto-ATP-diphosphohydrolase
-
-
ecto-ATPase
-
-
ecto-ATPase
Candida parapsilosis CCT3834
-
-
-
ecto-ATPDase
Q6QHT8
-
ecto-NTPDase
Q6QHT8
-
Ecto-NTPDase1
Q6QHT8
-
ecto-nucleoside triphosphate diphosphohydrolase
-
-
ecto-nucleoside triphosphate diphosphohydrolase
-
-
ecto-nucleoside triphosphate diphosphohydrolase
-
-
ecto-nucleoside triphosphate-diphosphohydrolase
-
-
ecto-nucleoside-triphosphate-diphosphohydrolase
Q6QHT8
-
ectoapyrase
-
-
ectoapyrase
-
-
ectoapyrase
-
-
ectonucleoside triphosphate diphosphohydrolase
-
-
ectonucleoside triphosphate diphosphohydrolase
P55772
-
Golgi nucleoside diphosphatase
-
-
-
-
GS50
-
-
GS52
-
-
GS52
-
-
GS52
Q9FVC2
-
HB6
-
-
-
-
LALP1
Q9NQZ7
-
LALP1
Q3TCT4
-
MpAPY2
G1UFQ9
-
NTPase
-
-
NTPDase 1
P97687
-
NTPDase 2
Q9Y5L3
-
NTPDase 3
-
-
NTPDase 5
-
-
NTPDase 6
-
-
NTPDase 8
O93295
-
NTPDase1
-
-
-
-
NTPDase1
-
-
NTPDase1
P55772
-
NTPDase1
P97687
-
NTPDase1
Rattus norvegicus Sprague-Dawley
P97687
-
-
NTPDase1
-
-
NTPDase1/CD39
P97687
-
NTPDase1/CD39
Rattus norvegicus Sprague-Dawley
P97687
-
-
NTPDase2
Q9Y5L3
-
NTPDase2
O35795
-
NTPDase2
Rattus norvegicus Sprague-Dawley
O35795
-
-
NTPDase2/CD39L1
O35795
-
NTPDase2/CD39L1
Rattus norvegicus Sprague-Dawley
O35795
-
-
NTPDase3
-
-
-
-
NTPDase8
O93295
-
NTPDase8
Q5DRK1
-
NTPDase8
Rattus norvegicus Sprague-Dawley
Q5DRK1
-
-
nucleoside triphosphatase
-
-
nucleoside triphosphate diphosphohydrolase
Q9FVC2
-
nucleoside triphosphate diphosphohydrolase
Q9Y5L3
-
nucleoside triphosphate diphosphohydrolase
O35795
-
nucleoside triphosphate diphosphohydrolase
P97687, Q5DRK1
-
nucleoside triphosphate diphosphohydrolase
Rattus norvegicus Sprague-Dawley
O35795, P97687, Q5DRK1
-
-
nucleoside triphosphate diphosphohydrolase
-
-
nucleoside triphosphate diphosphohydrolase 1
P97687
-
nucleoside triphosphate diphosphohydrolase 8
O93295
-
nucleoside triphosphate diphosphohydrolase-1, NDPDase 1
-
-
nucleoside triphosphate diphosphohydrolase-3
Q8BFW6
-
nucleoside triphosphate-diphosphohydrolase
-
-
potato-specific apyrase
-
-
Lymphoid cell activation antigen
-
-
-
-
additional information
-
Lpg1905 is a prokaryotic member of the CD39/NTPDase1 family of enzymes
additional information
A7LH73, A7LH74
the apyrase belongs to the 5'-nucleotidase family
additional information
A1BXT9
the enzyme belongs to the apyrase family
additional information
-
apyrase belongs to the actin superfamily of proteins and is a member of the NTPDase family
CAS REGISTRY NUMBER
COMMENTARY
9000-95-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
; recombinant enzyme
-
-
Manually annotated by BRENDA team
isozymes APY1 and APY2
-
-
Manually annotated by BRENDA team
Candida parapsilosis CCT3834
-
-
-
Manually annotated by BRENDA team
chick-pea
-
-
Manually annotated by BRENDA team
enzymes NT5E-1 and NT5E-2 encoded by genes CG4827 and CG30104
-
-
Manually annotated by BRENDA team
expression in Lotus japonicus
-
-
Manually annotated by BRENDA team
cv. Williams 82, GS50 and GS52 genes
-
-
Manually annotated by BRENDA team
wild soybean
UniProt
Manually annotated by BRENDA team
variant TM-1
-
-
Manually annotated by BRENDA team
-
Swissprot
Manually annotated by BRENDA team
hLALP70 and the splice variant hLALP70v
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
barley
-
-
Manually annotated by BRENDA team
-
Swissprot
Manually annotated by BRENDA team
-
Swissprot
Manually annotated by BRENDA team
genes Entpd1, 2, 3, 5, 6, and Entpd8
-
-
Manually annotated by BRENDA team
Swiss strain, male
SwissProt
Manually annotated by BRENDA team
mouse
-
-
Manually annotated by BRENDA team
Orchopeas howardi
-
-
-
Manually annotated by BRENDA team
isozyme I; collected from the Upington region in the Western Cape, South Africa by sifting of sand, isozyme I
UniProt
Manually annotated by BRENDA team
isozyme II; collected from the Upington region in the Western Cape, South Africa by sifting of sand, isozyme II
UniProt
Manually annotated by BRENDA team
Oropsylla bacchi
-
-
-
Manually annotated by BRENDA team
isotypes P0, P1, P2, P3, P4
-
-
Manually annotated by BRENDA team
variant Alaska
UniProt
Manually annotated by BRENDA team
NTPDase1
UniProt
Manually annotated by BRENDA team
NTPDase2
UniProt
Manually annotated by BRENDA team
NTPDase8
UniProt
Manually annotated by BRENDA team
recombinant enzyme expressed in Xenopus laevis oocyte
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
NTPDase1
UniProt
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
NTPDase2
UniProt
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
NTPDase8
UniProt
Manually annotated by BRENDA team
ATP-diphosphohydrolase 2; BH strain, gene ATPDase2
SwissProt
Manually annotated by BRENDA team
BH strain, gene ATPDase1
-
-
Manually annotated by BRENDA team
recombinant enzyme expressed in Pichia pastoris
-
-
Manually annotated by BRENDA team
varieties Pimpernel and Desiree
-
-
Manually annotated by BRENDA team
variety Desiree, low ATPase/ADPase ratio; variety Pimpernel, high ATPase/ADPase ratio
-
-
Manually annotated by BRENDA team
strain RIA 57
-
-
Manually annotated by BRENDA team
Streptomyces aureofaciens RIA
strain RIA 57
-
-
Manually annotated by BRENDA team
enzyme belongs to E-type ATPase/NTPDase family; enzyme called NTPDase1; pig
Uniprot
Manually annotated by BRENDA team
enzyme belongs to E-type ATPase/NTPDase family; pig
-
-
Manually annotated by BRENDA team
cysticerci
-
-
Manually annotated by BRENDA team
five N-glycosylated isoforms of 88, 82, 79,68, and 67 kDa molecular masses
-
-
Manually annotated by BRENDA team
precursor molecule, 79 kDa isoform
SwissProt
Manually annotated by BRENDA team
Triticosecale Wittmack
triticale
-
-
Manually annotated by BRENDA team
wild-type strains Y, CL, and Be-62, and hybrid strain and CL Brener
Swissprot
Manually annotated by BRENDA team
expression during all developmental stages tested
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
CG5276 belongs to another family of calcium-activated nucleotidases. CG5276 may represent an apyrase related to calcium-activated nucleotidases
evolution
-
GS52 is a member of the NTPDase/apyrase family
evolution
Q5CXD0
the capy gene is most likely an ancestral feature that has been lost from most apicomplexan genomes except Cryptosporidium, Neospora and Toxoplasma
evolution
-
the enzyme is a member of the E-NTPDase family
evolution
P97687
the enzyme is a member of the eukaryotic NTPDase family
malfunction
-
a soluble truncated mutant NTPDase8, lacking the extracellular domain, shows 85% reduced activity compared to the full-length membrane-bound enzyme. Also activity of the soluble chicken NTPDase8 decreases with time in a temperature-dependent manner as a result of inactivation by ATP, ADP, and phosphate, in contrast to the wild-type full-length enzyme
malfunction
-
suppression of apyrase expression affects the regulation of stomatal aperture
malfunction
Q9FVC2
the inactivated, functionally disrupted enzyme is not active in stimulating nodulation
metabolism
-
plasma membrane-bound NTPDases, namely NTPDase1/CD39, NTPDase2/CD39L1, and NTPDase8, represent the major liver ectonucleotidase activities
physiological function
Q9FEA6
apyrase plays a role in growth and development of tissues, for example, lateral roots
physiological function
-
ectoapyrase and extracellular nucleotides play a significant role in regulating cotton fiber growth
physiological function
-
the recombinant protein inhibits ADP- and collagen-induced platelet aggregation. Thus, this salivary protein plays an important role in the blood-feeding process in Phlebotomus duboscqi
physiological function
Q5CXD0
antibodies directed against CApy block Cryptosporidium parvum sporozoite invasion of HCT-8 cells
physiological function
E0D877
apyrases can inhibit platelet activation by depletion of adenosine diphosphate
physiological function
Q9FVC2
ecto-apyrase is an extracellular nucleoside triphosphate diphosphohydrolase that modulates the nucleotide concentration in the extracellular matrix. Ecto-apyrase controls the concentration of extracellular nucleotides. GS52 activity stimulates root nodulation, the inactivated enzyme is not effective
physiological function
-
ecto-nucleoside triphosphate diphosphohydrolases, E-NTPDases, regulate the concentration of extracellular nucleotides, signaling molecules that play a role in the pathogenesis of hepatic fibrosis. Up-regulation of Entpd3 mRNA expression modulates the extracellular concentration of nucleotides/nucleosides and affect P2-receptor signaling differently in quiescent-like cells and may play a role in the regulation of hepatic stellate cell functions
physiological function
-
expression of the two apyrase isozymes in Arabidopsis thaliana, APY1 and APY2, is strongly correlated with cell growth and secretory activity. Ectoapyrases and extracellular nucleotides play key roles in regulating stomatal functions, overview
physiological function
-
important role for the Glycine max ecto-apyrase GS52 in rhizobial root hair infection and root nodule formation
physiological function
P97687
nucleoside triphosphate diphosphohydrolases are a physiologically important class of membrane-bound ectonucleotidases responsible for the regulation of extracellular levels of nucleotides
physiological function
-
unlike NT5E-1, NT5E-2 seems to play a specific role in male reproduction since it is expressed more strongly in males than in females and is expressed specifically in testis
metabolism
Rattus norvegicus Sprague-Dawley
-
plasma membrane-bound NTPDases, namely NTPDase1/CD39, NTPDase2/CD39L1, and NTPDase8, represent the major liver ectonucleotidase activities
-
additional information
P97687
influence of transmembrane helix dynamics on activity is achieved by coupling to a domain motion. Active site structure of NTPDase1, overview, closure movement in NTPDases
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,N6-etheno-ADP + H2O
1,N6-etheno-AMP + phosphate
show the reaction diagram
-
-
-
-
?
1,N6-etheno-ATP + H2O
1,N6-etheno-AMP + phosphate
show the reaction diagram
-
-
-
-
?
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate + H2O
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate + H2O
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
3'(2')-O-(methylanthranoyl)adenosine 5'-diphosphate + H2O
3'(2')-O-(methylanthranoyl)adenosine 5'-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
3'(2')-O-(methylanthranoyl)adenosine 5'-triphosphate + H2O
3'(2')-O-(methylanthranoyl)adenosine 5'-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl thymidine 5'-phosphate + H2O
4-nitrophenol + TMP
show the reaction diagram
-
-
-
-
?
4-nitrophenylphosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
low activity
-
-
?
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
23% of activity compared to ATP
-
-
?
8-oxo-dGTP + 2 H2O
8-oxo-dGMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
adenosine (5')-tetraphospho-(5')-adenosine + H2O
?
show the reaction diagram
-
-
-
-
?
adenosine 5'-tetraphosphate + H2O
adenosine 5'-monophosphate + phosphate
show the reaction diagram
-
-
-
-
?
ADP + 2 H2O
adenosine + 2 phosphate
show the reaction diagram
-
-
-
-
?
ADP + 2 H2O
adenosine + 2 phosphate
show the reaction diagram
-
-
-
-
?
ADP + 2 H2O
adenosine + 2 phosphate
show the reaction diagram
Q6QHT8
-
-
-
?
ADP + 2 H2O
adenosine + 2 phosphate
show the reaction diagram
-
-
-
-
?
ADP + 2 H2O
adenosine + 2 phosphate
show the reaction diagram
Candida parapsilosis, Candida parapsilosis CCT3834
-
82.2% activity compared to ATP
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
Q8BFW6
-
-
-
-
ADP + H2O
AMP + phosphate
show the reaction diagram
Q8K0L2
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
-
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
A1BXT9
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
G1UFQ9
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
Triticosecale Wittmack
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
Oropsylla bacchi, Orchopeas howardi, Xenopsylla cheopis
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
Q6QHT8
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
Q8BFW6
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
Q06K73, Q06K77
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
P97687, Q5DRK1
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
P97687
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
Q5CXD0
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
as CaADP- only
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
87% relative activity compared to ATP
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
maximum activity at 7 mM, about 90% relative activity of ATP
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
104% of activity compared to ATP
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
119% of activity compared to ATP
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
67% of activity compared to ATP
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
71% of activity compared to ATP
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
ATP and ADP are hydrolyzed equivalently
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
37.7% of the activity with ATP
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
97% of the activity with ATP
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
Q70GK8
activity in decreasing order: ADP, IDP, CDP, GDP
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
hydrolysis of extracellular ADP
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
ADPase activity of GS52 is consistently more than 1.5fold higher than the ATPase activity
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
Rattus norvegicus Sprague-Dawley
P97687, Q5DRK1
-
-
-
?
ADP-ribose + H2O
?
show the reaction diagram
-
-
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
-
low activity, hydrolysis of extracellular AMP, low activity
-
-
?
AMPCPP + H2O
?
show the reaction diagram
P97687
low activity
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Q8BFW6
-
-
-
-
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Q8K0L2
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
-
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
ir
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
G1UFQ9
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Triticosecale Wittmack
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
ir
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Oropsylla bacchi, Orchopeas howardi, Xenopsylla cheopis
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Q6QHT8
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Q8BFW6
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Q9NQZ7
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Q3TCT4
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Q9Y5L3
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
O93295
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Q06K73, Q06K77
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Q9FEA6
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
P97687, Q5DRK1
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
P97687
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
E0D877
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
best substrate
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
as CaATP2- only
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
maximum activity at 8 mM
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
100% relative activity
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
better substrate then ADP
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
100% activity
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
inhibition of platelet aggregation in the placenta
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
salvage of purine nucleobases in primary urine
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
regulation of extracellular ATP-level
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
inhibition of platelet aggregation
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Orchopeas howardi, Xenopsylla cheopis
-
inhibition of platelet aggregation
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
ATP and ADP are hydrolyzed equivalently
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Q70GK8
activity in decreasing order: ATP, CTP, GTP, UTP, ITP
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
dissipation of ATP by CD39 reduces P2X7 receptor stimulation and thereby suppresses baseline leukocyte alphaMbeta2-integrin expression. As alphaMbeta2-integrin blockade reverses the postischemic, inflammatory phenotype of Cd39-/- mice. Phosphohydrolytic activity on the leukocyte surface suppresses cell-cell interactions that would otherwise promote thrombosis or inflammation
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
ATP-diphosphohydrolase releases ADP during the catalytic cycle, mechanism of ATP hydrolysis, overview
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
slight preference for ATP as substrate
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
best substrate in hepatic stellate cells
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
ADPase activity of GS52 is consistently more than 1.5fold higher than the ATPase activity
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
P97687, Q5DRK1
sequential dephosphorylation of ATP to ADP and then AMP
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Rattus norvegicus Sprague-Dawley
P97687, Q5DRK1
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Rattus norvegicus Sprague-Dawley
P97687, Q5DRK1
sequential dephosphorylation of ATP to ADP and then AMP
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Candida parapsilosis CCT3834
-
100% activity
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
A1BXT9
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
-
ATP + H2O
ADP + phosphate
show the reaction diagram
P55772
-
-
-
-
ATP + H2O
ADP + phosphate
show the reaction diagram
P97687
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
hydrolysis of extracellular ATP
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
O35795
ATP incubated with NTPDase2 is readily converted into ADP, but very poorly into AMP
-
-
?
ATP + H2O
AMP + 2 phosphate
show the reaction diagram
Q5CXD0
-
-
-
?
ATP + H2O
AMP + 2 phosphate
show the reaction diagram
-
CG5276 functions as apyrase converting extracellular ATP to ADP and AMP
-
-
?
ATP + H2O
AMP + phosphate + H+
show the reaction diagram
-
-
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
-
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
-
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
-
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
-
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
-
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
-
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
-
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
-
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
-
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
-
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
lowest relative activity with 61%
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
high enzyme activity by hLALP70v
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
42% of activity compared to ATP
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
Q70GK8
activity in decreasing order: ADP, IDP, CDP, GDP
-
-
?
CDP-choline + H2O
?
show the reaction diagram
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
-
-
-
-
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
-
-
-
ir
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
better substrate then ATP
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
highest enzyme activity by hLALP70v
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
60% of activity compared to ATP
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
87% of activity compared to ATP
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
Q9NQZ7
UTP, GTP and CTP are preferred substrates
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
Q70GK8
activity in decreasing order: ATP, CTP, GTP, UTP, ITP
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
15.9% activity compared to ATP
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
-
-
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
-
17.4% of the activity with ATP
-
-
?
CTP + H2O
CMP + phosphate + H+
show the reaction diagram
-
-
-
-
?
dATP + 2 H2O
dAMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
dATP + H2O
dAMP + phosphate
show the reaction diagram
-
-
-
-
?
dATP + H2O
dAMP + phosphate + H+
show the reaction diagram
-
-
-
-
?
dCTP + 2 H2O
dCMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
dCTP + H2O
dCMP + phosphate + H+
show the reaction diagram
-
-
-
-
?
dGTP + 2 H2O
dGMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
dGTP + H2O
dGMP + phosphate + H+
show the reaction diagram
-
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
low activity
-
-
?
dTTP + H2O
dTMP + phosphate
show the reaction diagram
-
-
-
-
?
dTTP + H2O
dTMP + phosphate + H+
show the reaction diagram
-
-
-
-
?
dUTP + H2O
dUMP + phosphate + H+
show the reaction diagram
-
-
-
-
?
FAD + H2O
?
show the reaction diagram
-
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
-
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
-
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
-
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
-
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
-
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
-
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
-
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
-
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
-
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
-
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
Q6QHT8
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
-
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
P97687
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
Q5CXD0
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
-
best substrate
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
-
61% of activity compared to ATP
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
Q70GK8
activity in decreasing order: ADP, IDP, CDP, GDP
-
-
?
GDP + H2O
GDP + phosphate
show the reaction diagram
-
35% of the activity with ATP
-
-
?
GDP-mannose + H2O
?
show the reaction diagram
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
-
-
-
ir
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
P97687
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
best substrate
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
Q6QHT8
best substrate
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
comparative hydrolysis to ATP
-
-
-
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
better substrate than UTP
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
hLALP70v
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
37% of the activity with ATP
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
23% of activity compared to ATP
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
91% of activity compared to ATP
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
Q9NQZ7
UTP, GTP and CTP are preferred substrates
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
51.4% of the activity with ATP
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
Q70GK8
activity in decreasing order: ATP, CTP, GTP, UTP, ITP
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
Candida parapsilosis, Candida parapsilosis CCT3834
-
20.7% activity compared to ATP
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GMP + phosphate + H+
show the reaction diagram
-
-
-
-
?
IDP + H2O
IMP + phosphate
show the reaction diagram
-
-
-
-
?
IDP + H2O
IMP + phosphate
show the reaction diagram
-
-
-
-
?
IDP + H2O
IMP + phosphate
show the reaction diagram
-
-
-
-
?
IDP + H2O
IMP + phosphate
show the reaction diagram
-
-
-
-
?
IDP + H2O
IMP + phosphate
show the reaction diagram
-
-
-
-
?
IDP + H2O
IMP + phosphate
show the reaction diagram
-
-
-
-
?
IDP + H2O
IMP + phosphate
show the reaction diagram
P97687
-
-
-
?
IDP + H2O
IMP + phosphate
show the reaction diagram
-
comparative hydrolysis to ADP
-
-
-
IDP + H2O
IMP + phosphate
show the reaction diagram
Q70GK8
activity in decreasing order: ADP, IDP, CDP, GDP
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
show the reaction diagram
P97687
-
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
show the reaction diagram
-
109% of activity compared to ATP
-
-
?
ITP + H2O
IDP + phosphate
show the reaction diagram
P97687
-
-
-
?
ITP + H2O
IDP + phosphate
show the reaction diagram
-
best substrate
-
-
?
ITP + H2O
IMP + phosphate
show the reaction diagram
-
-
-
-
?
ITP + H2O
IMP + phosphate
show the reaction diagram
-
-
-
-
?
ITP + H2O
IMP + phosphate
show the reaction diagram
-
-
-
-
?
ITP + H2O
IMP + phosphate
show the reaction diagram
-
-
-
-
?
ITP + H2O
IMP + phosphate
show the reaction diagram
-
-
-
-
?
ITP + H2O
IMP + phosphate
show the reaction diagram
-
-
-
-
?
ITP + H2O
IMP + phosphate
show the reaction diagram
-
-
-
-
?
ITP + H2O
IMP + phosphate
show the reaction diagram
-
-
-
-
ir
ITP + H2O
IMP + phosphate
show the reaction diagram
-
comparative hydrolysis to ATP
-
-
?
ITP + H2O
IMP + phosphate
show the reaction diagram
-
78% of activity compared to ATP
-
-
?
ITP + H2O
IMP + phosphate
show the reaction diagram
-
84.8% of the activity with ATP
-
-
?
ITP + H2O
IMP + phosphate
show the reaction diagram
Q70GK8
activity in decreasing order: ATP, CTP, GTP, UTP, ITP
-
-
?
NADH + H2O
?
show the reaction diagram
-
-
-
-
?
oligophosphates + H2O
?
show the reaction diagram
-
n = 3, 15, 40, 60
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
show the reaction diagram
-
-
-
-
?
TDP + H2O
TMP + phosphate
show the reaction diagram
-
-
-
-
?
TDP + H2O
TMP + phosphate
show the reaction diagram
-
-
-
-
?
TDP + H2O
TMP + phosphate
show the reaction diagram
P97687
-
-
-
?
TDP + H2O
TMP + phosphate
show the reaction diagram
-
44% of activity compared to ATP
-
-
?
tetraamine(imidodiphosphato)cobalt + H2O
?
show the reaction diagram
-
-
-
-
?
thiamine diphosphate + 2 H2O
thiamine + 2 phosphate
show the reaction diagram
-
-
-
-
?
thio-dATP + H2O
thio-dAMP + phosphate
show the reaction diagram
-
-
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
show the reaction diagram
-
high enzyme activity by hLALP70
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
show the reaction diagram
-
better substrate then CTP
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
show the reaction diagram
-
82% of activity compared to ATP
-
-
?
TTP + H2O
TDP + phosphate
show the reaction diagram
-
low activity
-
-
?
UDP + 2 H2O
uridine + 2 phosphate
show the reaction diagram
-
-
-
-
?
UDP + 2 H2O
uridine + 2 phosphate
show the reaction diagram
-
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
Q8BFW6
-
-
-
-
UDP + H2O
UMP + phosphate
show the reaction diagram
Q8K0L2
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
-
UDP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
-
UDP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
Q6QHT8
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
Q8BFW6
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
P97687
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
Q5CXD0
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
hLALP70v
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
18% of the activity with ATP
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
104% of activity compared to ATP
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
31% of activity compared to ATP
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
56% of activity compared to ATP
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
best substrate in myofibroblasts
-
-
?
UDP-glucose + H2O
?
show the reaction diagram
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
show the reaction diagram
P97687
-
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
-
-
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
P97687
-
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
Q8BFW6
-
-
-
-
UTP + H2O
UMP + phosphate
show the reaction diagram
Q8K0L2
-
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
-
UTP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
-
UTP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
ir
UTP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
Q6QHT8
-
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
Q8BFW6
-
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
best substrate
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
better substrate then TTP
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
highest enzyme activity by hLALP70
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
40% of the activity with ATP
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
150% of activity compared to ATP
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
25% of activity compared to ATP
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
94% of activity compared to ATP
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
Q9NQZ7
UTP, GTP and CTP are preferred substrates
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
25.2% of the activity with ATP
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
Q70GK8
activity in decreasing order: ATP, CTP, GTP, UTP, ITP
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
Candida parapsilosis, Candida parapsilosis CCT3834
-
43.3% activity compared to ATP
-
-
?
UTP + H2O
UMP + phosphate + H+
show the reaction diagram
-
-
-
-
?
ITP + H2O
IMP + phosphate
show the reaction diagram
Candida parapsilosis, Candida parapsilosis CCT3834
-
70.7% activity compared to ATP
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
-
additional information
?
-
-
no hydrolysis of GMP, UMP
-
-
-
additional information
?
-
-
neglible hydrolysis of AMP
-
-
-
additional information
?
-
-
neglible hydrolysis of AMP
-
-
-
additional information
?
-
-
neglible hydrolysis of AMP
-
-
-
additional information
?
-
Q9MYU4
neglible hydrolysis of AMP
-
-
-
additional information
?
-
-
neglible hydrolysis of AMP
-
-
-
additional information
?
-
-
neglible hydrolysis of AMP
-
-
-
additional information
?
-
-
neglible hydrolysis of AMP
-
-
-
additional information
?
-
-
neglible hydrolysis of AMP
-
-
-
additional information
?
-
-
neglible hydrolysis of AMP
-
-
-
additional information
?
-
-
neglible hydrolysis of AMP
-
-
-
additional information
?
-
-
neglible hydrolysis of AMP
-
-
-
additional information
?
-
-
neglible hydrolysis of AMP
-
-
-
additional information
?
-
-
neglible hydrolysis of AMP
-
-
-
additional information
?
-
-
neglible hydrolysis of AMP
-
-
-
additional information
?
-
Oropsylla bacchi, Orchopeas howardi, Xenopsylla cheopis
-
neglible hydrolysis of AMP
-
-
-
additional information
?
-
Q8BFW6
no substrate: AMP
-
-
-
additional information
?
-
-
enzyme abrogates platelet aggregation and recruitment in intact vessels
-
-
-
additional information
?
-
-
enzyme terminates P2 receptor-mediated signal transmission
-
-
-
additional information
?
-
-
both ATP and ADP hydrolysis occur at the same active site of enzyme
-
-
-
additional information
?
-
-
no substrate: CTP, CDP, GTP, GDP
-
-
-
additional information
?
-
-
relative efficacy for substrate in decreasing order: CTP, ADP, UTP, TTP, GTP, ATP
-
-
-
additional information
?
-
-
enzyme inhibits ADP-, collagen-, and thrombin-induced human platelet aggregation in dose-dependent manner
-
-
-
additional information
?
-
Q70GK8
enzyme inhibits ADP-induced human platelet aggregation
-
-
-
additional information
?
-
-
enzyme is involved in regulating ATP signaling associated primarily with auditory neurotransmission
-
-
-
additional information
?
-
-
introduction of large groups in the ribose does not produce steric hindrance in substrate binding, but causes a reduction in kcat-value
-
-
-
additional information
?
-
Q70GK8
no substrate: nucleoside 5-monophosphates, glycerol phosphate, glycose 6-phosphate, UDP-galactose
-
-
-
additional information
?
-
-
only one enzymatic site is responsible for hydrolysis of both ATP and ADP
-
-
-
additional information
?
-
-
apyrase, an ecto-enzyme with ADPase and ATPase activities, rapidly metabolizes ADP and ATP released from platelets and endothelial cells, thereby reducing platelet activation and recruitment. The recombinant apyrase inhibits ADP-, collagen- and thrombin-induced human platelet aggregation, overview
-
-
-
additional information
?
-
A1BXT9
ATPDase2 plays a non-redundant role in the parasite-host interplay
-
-
-
additional information
?
-
-
the enzyme acts in a multienzyme complex transforming ATP into adenosine without accumulation of intermediates
-
-
-
additional information
?
-
-
the enzyme plays a role in the salvage of purines from the extracellular medium in the organism
-
-
-
additional information
?
-
-
apyrases are non-energy-coupled nucleotide phosphohydrolases that hydrolyze nucleoside triphosphates and nucleoside diphosphates to nucleoside monophosphates and orthophosphates, critical role for the GS52 ecto-apyrase during nodulation
-
-
-
additional information
?
-
-
apyrases hydrolyze nucleoside triphosphates and diphosphates
-
-
-
additional information
?
-
-
CD39 can regulate platelet activation from either the endothelial or leukocyte compartment. CD39 on monocytes and neutrophils regulates their own sequestration into ischemic cerebral tissue, by catabolizing nucleotides released by injured cells, thereby inhibiting their chemotaxis, adhesion, and transmigration. Leukocyte ectoapyrases modulate the ambient vascular nucleotide milieu. Dissipation of ATP by CD39 reduces P2X7 receptor stimulation and thereby suppresses baseline leukocyte alphaMbeta2-integrin expression. As alphaMbeta2-integrin blockade reverses the postischemic, inflammatory phenotype of Cd39-/- mice
-
-
-
additional information
?
-
Q6QHT8
Ecto-NTPDase1 is required in the infection process of trypanosomes into mammalian cells, overview. Ecto-NTPDase act as facilitators of infection and virulence in vitro and in vivo
-
-
-
additional information
?
-
-
Lpg1905 is essentially required for intracellular replication of Legionella pneumophila in eukaryotic cells leading to the Legionnaires disease, a severe and potentially fatal form of pneumonia
-
-
-
additional information
?
-
A7LH73, A7LH74
salivary apyrases are nucleotide-metabolising enzymes that blood-feeding parasites utilise for modulation of extracellular nucleotides to prevent platelet activation and aggregation
-
-
-
additional information
?
-
-
APY-1 has also NDPase activity
-
-
-
additional information
?
-
-
identification of the amino acids interacting with the nucleoside triphosphate substrate and probably involved in the catalyzed hydrolysis. The mixed two-step catalytic mechanism of hydrolysis involves Thr127 and Thr55 as potential nucleophilic factors responsible for the cleavage of the Pgamma and Pbeta anhydride bonds, respectively. Their is assisted by Glu170 and Glu78 residues, respectively, detailed overview
-
-
-
additional information
?
-
-
the enzyme hydrolyzes purine and pyrimidine nucleoside 5'-di- and 5'-triphosphates, substrate specificity and competition, overview
-
-
-
additional information
?
-
-
the enzyme shows the ability to hydrolyze nucleoside tri- and diphosphates, but has limited activity against CTP, CDP, UTP, and UDP
-
-
-
additional information
?
-
Q06K73, Q06K77
the enzyme does not hydrolyze AMP, GDP, CDP or UDP
-
-
-
additional information
?
-
E0D877
apyrases hydrolyze the phosphodiester bonds of nucleoside tri- and diphosphates to orthophosphate and mononucleodides
-
-
-
additional information
?
-
-
substrate specificity in myofibroblasts and quiescent-like hepatic stellate cells, overview
-
-
-
additional information
?
-
P97687
establishment of a kinetic isothermal titration calorimetry assay. Substrate recognition by NTPDase1, overview
-
-
-
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 substratebinding pocket of the enzyme. No hydrolytic activity with AMP
-
-
-
additional information
?
-
G1UFQ9
the purified MP67 shows extremely high substrate specificity toward ADP in the presence of Ca2+, the recombinant MpAPY2 hydrolyzes ATP and ADP to the same extent
-
-
-
additional information
?
-
-
the recombinant MpAPY2 hydrolyzes ATP and ADP to the same extent
-
-
-
additional information
?
-
Q5CXD0
UDP and GDP, rather than ADP or ATP, are the preferred substrates of CApy
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + 2 H2O
adenosine + 2 phosphate
show the reaction diagram
-
-
-
-
?
ADP + 2 H2O
adenosine + 2 phosphate
show the reaction diagram
Q6QHT8
-
-
-
?
ADP + 2 H2O
adenosine + 2 phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
A1BXT9
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
G1UFQ9
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
Triticosecale Wittmack
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
Oropsylla bacchi, Orchopeas howardi, Xenopsylla cheopis
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
P97687, Q5DRK1
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
Q5CXD0
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
hydrolysis of extracellular ADP
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
Rattus norvegicus Sprague-Dawley
P97687, Q5DRK1
-
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
-
hydrolysis of extracellular AMP, low activity
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
-
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
ir
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
G1UFQ9
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Triticosecale Wittmack
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
ir
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Oropsylla bacchi
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Q6QHT8
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Q9Y5L3
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
O93295
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Q9FEA6
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
P97687, Q5DRK1
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
E0D877
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
inhibition of platelet aggregation in the placenta
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
salvage of purine nucleobases in primary urine
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
regulation of extracellular ATP-level
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
inhibition of platelet aggregation
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Orchopeas howardi, Xenopsylla cheopis
-
inhibition of platelet aggregation
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
dissipation of ATP by CD39 reduces P2X7 receptor stimulation and thereby suppresses baseline leukocyte alphaMbeta2-integrin expression. As alphaMbeta2-integrin blockade reverses the postischemic, inflammatory phenotype of Cd39-/- mice. Phosphohydrolytic activity on the leukocyte surface suppresses cell-cell interactions that would otherwise promote thrombosis or inflammation
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
-
best substrate in hepatic stellate cells
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
Rattus norvegicus Sprague-Dawley
P97687, Q5DRK1
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
A1BXT9
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
-
-
ATP + H2O
ADP + phosphate
show the reaction diagram
P55772
-
-
-
-
ATP + H2O
ADP + phosphate
show the reaction diagram
-
hydrolysis of extracellular ATP
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
O35795
ATP incubated with NTPDase2 is readily converted into ADP, but very poorly into AMP
-
-
?
ATP + H2O
AMP + 2 phosphate
show the reaction diagram
Q5CXD0
-
-
-
?
ATP + H2O
AMP + 2 phosphate
show the reaction diagram
-
CG5276 functions as apyrase converting extracellular ATP to ADP and AMP
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
Rattus norvegicus Sprague-Dawley
O35795
ATP incubated with NTPDase2 is readily converted into ADP, but very poorly into AMP
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
-
-
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
-
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
-
-
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
Q5CXD0
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
UDP + 2 H2O
uridine + 2 phosphate
show the reaction diagram
-
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
Q5CXD0
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
best substrate in myofibroblasts
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
UTP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme abrogates platelet aggregation and recruitment in intact vessels
-
-
-
additional information
?
-
-
enzyme terminates P2 receptor-mediated signal transmission
-
-
-
additional information
?
-
-
enzyme inhibits ADP-, collagen-, and thrombin-induced human platelet aggregation in dose-dependent manner
-
-
-
additional information
?
-
Q70GK8
enzyme inhibits ADP-induced human platelet aggregation
-
-
-
additional information
?
-
-
enzyme is involved in regulating ATP signaling associated primarily with auditory neurotransmission
-
-
-
additional information
?
-
-
apyrase, an ecto-enzyme with ADPase and ATPase activities, rapidly metabolizes ADP and ATP released from platelets and endothelial cells, thereby reducing platelet activation and recruitment. The recombinant apyrase inhibits ADP-, collagen- and thrombin-induced human platelet aggregation, overview
-
-
-
additional information
?
-
A1BXT9
ATPDase2 plays a non-redundant role in the parasite-host interplay
-
-
-
additional information
?
-
-
the enzyme acts in a multienzyme complex transforming ATP into adenosine without accumulation of intermediates
-
-
-
additional information
?
-
-
the enzyme plays a role in the salvage of purines from the extracellular medium in the organism
-
-
-
additional information
?
-
-
apyrases are non-energy-coupled nucleotide phosphohydrolases that hydrolyze nucleoside triphosphates and nucleoside diphosphates to nucleoside monophosphates and orthophosphates, critical role for the GS52 ecto-apyrase during nodulation
-
-
-
additional information
?
-
-
apyrases hydrolyze nucleoside triphosphates and diphosphates
-
-
-
additional information
?
-
-
CD39 can regulate platelet activation from either the endothelial or leukocyte compartment. CD39 on monocytes and neutrophils regulates their own sequestration into ischemic cerebral tissue, by catabolizing nucleotides released by injured cells, thereby inhibiting their chemotaxis, adhesion, and transmigration. Leukocyte ectoapyrases modulate the ambient vascular nucleotide milieu. Dissipation of ATP by CD39 reduces P2X7 receptor stimulation and thereby suppresses baseline leukocyte alphaMbeta2-integrin expression. As alphaMbeta2-integrin blockade reverses the postischemic, inflammatory phenotype of Cd39-/- mice
-
-
-
additional information
?
-
Q6QHT8
Ecto-NTPDase1 is required in the infection process of trypanosomes into mammalian cells, overview. Ecto-NTPDase act as facilitators of infection and virulence in vitro and in vivo
-
-
-
additional information
?
-
-
Lpg1905 is essentially required for intracellular replication of Legionella pneumophila in eukaryotic cells leading to the Legionnaires disease, a severe and potentially fatal form of pneumonia
-
-
-
additional information
?
-
A7LH73, A7LH74
salivary apyrases are nucleotide-metabolising enzymes that blood-feeding parasites utilise for modulation of extracellular nucleotides to prevent platelet activation and aggregation
-
-
-
additional information
?
-
E0D877
apyrases hydrolyze the phosphodiester bonds of nucleoside tri- and diphosphates to orthophosphate and mononucleodides
-
-
-
additional information
?
-
-
substrate specificity in myofibroblasts and quiescent-like hepatic stellate cells, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
either Mg2+ or Ca2+ required for activity
Ca2+
-
either Mg2+ or Ca2+ required for activity
Ca2+
-
required for activity
Ca2+
-
either Mg2+ or Ca2+ required for activity
Ca2+
-
either Mg2+ or Ca2+ required for activity; hLALP70 prefers Ca2+ to Mg2+; hLALP70v either Md2+ or Ca2+ dependent
Ca2+
-
Ca2+ preferred to Mg2+; either Mg2+ or Ca2+ required for activity
Ca2+
-
Ca2+ preferred to Mg2+
Ca2+
-
either Mg2+ or Ca2+ required for activity
Ca2+
-
Ca2+ preferred to Mg2+
Ca2+
-
required for activity
Ca2+
-
only ADP hydrolysed in the presence of Ca2+
Ca2+
-
either Mg2+ or Ca2+ required for activity
Ca2+
-
Ca2+ preferred to Mg2+; maximum activity at 0.5 mM
Ca2+
-
required for activity
Ca2+
-
either Mg2+ or Ca2+ required for activity
Ca2+
-
either Mg2+ or Ca2+ required for activity
Ca2+
Orchopeas howardi, Oropsylla bacchi, Xenopsylla cheopis
-
function enhanced, not essential
Ca2+
Q8BFW6
or Mg2+, required, Ca2+ is preferred
Ca2+
Q8K0L2
absolute requirement for divalent cation, Ca2+ fulfilling requirement best
Ca2+
-
or Mg2+, required, Km-value 0.377 mM
Ca2+
-
about 30% of the activity with Mg2+, at 5 mM and pH 7.4
Ca2+
-
required
Ca2+
Q9NQZ7
absolute requirement
Ca2+
Q3TCT4
absolute requirement
Ca2+
-
activation
Ca2+
-
best activating kation
Ca2+
Q9Y5L3
activates, required
Ca2+
-
activates
Ca2+
-
activates
Ca2+
-
activates
Ca2+
Q06K73, Q06K77
strictly dependent on Ca2+; strictly dependent on Ca2+
Ca2+
P97687, Q5DRK1
required; required
Ca2+
O35795
required
Ca2+
-
required
Ca2+
E0D877
required
Ca2+
-
the most effective activating divalent cation
Ca2+
Q5CXD0
required
Cl-
P97687
the active-site clefts of NTPDase1 contain three chloride ions, one of which is bound to the second phosphate-binding loop, apyrase conserved region 4, ACR4
Co2+
-
lower activation than Ca2+, Mg2+, Mn2+
Co2+
-
at 1 mM, 73% of ATPase activity compared to Ca2+
Co2+
Q70GK8
required, may be substituted by Mg2+, Mg2+
Co2+
-
activates
Co2+
-
stimulates ecto-ATPase activity
Cu2+
-
activates
Mg2+
-
required for activity
Mg2+
-
either Mg2+ or Ca2+ required for activity
Mg2+
-
either Mg2+ or Ca2+ required for activity
Mg2+
-
either Mg2+ or Ca2+ required for activity; hLALP70v either Mg2+ or Ca2+ required for activity
Mg2+
-
either Mg2+ or Ca2+ required for activity
Mg2+
-
cannot be activated by Mg2+
Mg2+
-
either Mg2+ or Ca2+ required for activity
Mg2+
-
either Mg2+ or Ca2+ required for activity
Mg2+
-
either Mg2+ or Ca2+ required for activity
Mg2+
-
Mg2+ preferred to Mn2+
Mg2+
-
either Mg2+ or Ca2+ required for activity; maximum activity at 6 and 9 mM with ADP and ATP respectively
Mg2+
-
either Mg2+ or Ca2+ required for activity
Mg2+
Orchopeas howardi, Oropsylla bacchi, Xenopsylla cheopis
-
function enhanced, not essential
Mg2+
Q8BFW6
or Ca2+, required, Ca2+ is preferred
Mg2+
Q8K0L2
absolute requirement for divalent cation, Ca2+ fulfilling requirement best
Mg2+
-
or Ca2+, required, Km-value 0.595 mM
Mg2+
-
best activation
Mg2+
-
most effective as activating cation, but not absolutely required
Mg2+
-
at 1 mM, 61% of ATPase activity compared to Ca2+
Mg2+
-
up to 3fold activation
Mg2+
Q70GK8
required, may be substituted by Mn2+, Co2+
Mg2+
-
activates, most effect divalent cation, activity profile, overview
Mg2+
-
required, activates
Mg2+
Q9Y5L3
activates, required
Mg2+
-
activates, best metal ion
Mg2+
-
activates
Mg2+
-
dependent on, inhibitory at 11 mM
Mg2+
-
activates
Mg2+
-
ecto-ATPase activity is increased in the presence of 5 mM Mg2+
Mg2+
P97687, Q5DRK1
required; required
Mg2+
O35795
required
Mg2+
-
required
Mg2+
Q5CXD0
required
MgCl2
-
5 mM, stimulation up to 20fold, best activating kation
Mn2+
-
lower activation than Ca2+ and Mg2+
Mn2+
-
cannot be activated by Mn2+
Mn2+
-
lower activation than Ca2+ and Mg2+
Mn2+
-
preferred to Zn2+
Mn2+
-
lower activation than Ca2+, Mg2+
Mn2+
-
activation
Mn2+
-
at 1 mM, 65% of ATPase activity compared to Ca2+
Mn2+
Q70GK8
required, may be substituted by Mg2+, Co2+
Mn2+
-
activates, most effect divalent cation
Mn2+
-
activates
Mn2+
-
activates
Mn2+
-
stimulates ecto-ATPase activity
Mn2+
-
15% residual activity compared with Mg2+
Zn2+
-
lower activation than Ca2+ ,Mg2+ and Mn2+
Zn2+
-
cannot be activated by Zn2+
Zn2+
-
preferred to Co2+
Zn2+
-
lower activation than Ca2+, Mg2+
Zn2+
-
-
Zn2+
-
at 1 mM, 70% of ATPase activity compared to Ca2+
Zn2+
-
activates
Zn2+
-
activates
ZnCl2
-
5 mM, stimulation
MnCl2
-
5 mM, stimulation up to 10fold
additional information
-
no effect: Na+ at 100 mM or K+ at 4 mM
additional information
-
enzyme activity is absolutely dependent on divalent metal ions, Mg2+ exhibits the maximal activating effect among the studied cations. Other metal cations like Mn2+, Co2+, Ca2+, Cu2+, and Zn2+ are less efficient, and Ba2+ is not able to activate the enzyme
additional information
-
Lpg1905 is dependent on divalent metal cations
additional information
Q06K73, Q06K77
not dependent on Mg2+; not dependent on Mg2+
additional information
P97687
complex structures with decavanadate and heptamolybdate show that both polyoxometallates bind electrostatically to a loop that is involved in binding of the nucleobase
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-hydroxy-naphthalene-3,6-disulfonic acid
-
-
4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid
-
0.5 mM reduces enzyme activity in yeast living cells by 83.1%
4,4'-diisothiocyanostilbene 2,2'-disulfonate
-
DIDS, an impermeable inhibitor
4,4'-diisothiocyanostilbene-2,2'-disulfonic acid
-
-
4-nitrophenyl phosphate
-
15% inhibition at 5 mM
5'-AMP
-
11% inhibition at 5 mM
5'-p-fluorosulfonyl benzoyl adenosine
-
85-90% inhibition at 2 mM, pseudo first-order inhibition kinetics
5'-p-fluorosulfonylbenzoyladenosine
-
50% inhibition at 2 mM
5'-p-fluorosulfonylbenzoyladenosine
-
-
5,5'-diisothiocyanato-2,2'-(ethene-1,2-diyl)dibenzenesulfonic acid
-
0.1 mM, 40% residual activity
6-N,N-diethyl-beta,gamma-dibromomethylene-D-adenosine-5'-triphosphate
Q6QHT8
i.e. ARL 67156, a selective inhibitor of Ecto-ATPase, shows 30% inhibition of Ecto-ATPDase activities and 50% inhibition of trypomastigotes infectivity in vivo at 0.5 mM and 0.3 mM, respectively
adenosine
-
decrease in activity may be due to downregulation of enzyme expression
adenosine 5'-[beta,gamma-imido]triphosphate
-
-
adenylyl methylenediphosphate
-
-
ADP
-
competitive inhibition
ADP
-
hydrolysis of CaATP2- and CaADP- decreased by 50% at 0.48 mM free ADP
ADP
-
competitive
ADP
-
50% inhibition at 5 mM
ADP
-
75% inhibition at 0.5 mM
ADP
-
free substrate inhibition
ammonium heptamolybdate
P97687
AHM, (NH4)6[Mo7O24]
AMP
-
-
AMP
-
complete inhibition at 0.5 mM
AMP
P97687
-
ARL 67156
-
i.e. 6-N,N'-diethyl-D-beta-gamma-dibromomethylene-ATP, inhibits the ecto-ATPase activity in a dose-dependent manner (about 60% residual activity at 0.5 mM in the presence of 50 mM ATP and about 40% residual activity at 0.5 mM in the presence of 0.5 mM ATP)
Asparaginase
-
-
-
ATP
-
hydrolysis of CaATP2- and CaADP- decreased by 50% at 0.3 mM free ATP
ATP
-
68% inhibition at 0.5 mM
ATP
-
free substrate inhibition
azide
-
at 10 mM and pH 7.4, 21% inhibition of ATP hydrolysis, 85% inhibition of ADP hydrolysis
Ba2+
-
-
Ca2+
-
inhibitory at 11 mM
CDP
-
59% inhibition at 0.5 mM
CDP
-
free substrate inhibition
CDTA
-
-
Cibacron blue
-
-
citrate
-
20% inhibition at 0.5 mM
CMP
-
complete inhibition at 0.5 mM
CTP
-
free substrate inhibition
Cu2+
-
-
detergent NP-40
Q9Y5L3
at low concentration inhibition of the membrane-bound enzyme, not of the soluble enzyme
dicylcohexylcarbodiimid
-
DCCD, slightly inhibited
Dinitrophenol
-
-
diphosphate
-
at 10 mM and pH 7.4, 51% inhibition of ATP hydrolysis, 97% inhibition of ADP hydrolysis
dipyridamole
-
10% inhibition at 0.01 mM
EDTA
-
activity restored by adding Ca2+ or Mg2+
EDTA
-
activity not restored with 5 mM Ca2+ or Mg2+ for periods up to 24h
EDTA
-
about 40% inhibition at 5 mM
EDTA
-
analyzed in presence and absence of, control reaction
EDTA
P55772
analyzed in presence and absence of, control reaction
EDTA
Q06K73, Q06K77
;
EDTA
-
complete inhibition at 1 M
EGTA
-
-
erythrosine B
-
-
erythrosine B
G1UFQ9
does not affect the ATPase activity but inhibits ADPase activity of MP67 to a minor extent
Ethacrynic acid
-
-
Evans blue
-
complete inhibition at 0.1 mM
fluoride
-
at 10 mM and pH 7.4, 2% inhibition of ATP hydrolysis, 91% inhibition of ADP hydrolysis
Furosemide
-
20% inhibition at 1 mM
gadolinium
Q6QHT8
GdCl3, an Ecto-ATPDase inhibitor, shows 30% inhibition of Ecto-ATPDase activities and 60% inhibition of trypomastigotes infectivity in vivo at 0.3 mM and 0.5 mM, respectively
GDP
-
81% inhibition at 0.5 mM
GDP
-
free substrate inhibition
Glutaminase
-
-
-
GMP
-
complete inhibition at 0.5 mM
GTP
-
70% inhibition at 0.5 mM
GTP
-
free substrate inhibition
HgCl
-
-
IDP
-
59% inhibition at 0.5 mM
IMP
-
95% inhibition at 0.5 mM
iodoacetic acid
-
-
ITP
-
42% inhibition at 0.5 mM
Mg2+
-
-
Mg2+
-
dependent on, inhibitory at 11 mM
N3-
-
-
N3-
-
-
NaF
Q70GK8
1 mM, inhibition
NaN3
Q9MYU4
inhibition from 30-70% depending on tissue, inhibition of ADP hydrolysis slightly more pronounced
NaN3
-
above 10 mM
NaN3
-
60% inhibition
NaN3
-
above 5 mM
NaN3
-
10 mM
NaN3
-
58% inhibition at 10 mM
orthovanadate
-
-
orthovanadate
-
0.1 mM, 45% inhibition of ATPase activity
orthovanadate
-
hydrolysis of ADP
p-Chloromercuriphenylsulfonic acid
-
1 mM, 56% of inhibition
p-hydroxymercuribenzoate
-
1 mM, 35% of inhibition
polytungstate salt POM-1
P97687
Na6[H2W12O40]
-
POM-1
-
i.e. Na6[H2W12O40], a polyoxometalate
-
POM-6
-
i.e. (NH4)18[NaSb9W21O86], a polyoxometalate
-
Propionate
-
61% inhibition at 0.5 mM
pyridoxal-phosphate-6-azophenyl-2',4'-disulfonate
-
i.e.PPADS
Sodium azide
-
-
Sodium azide
-
-
Sodium azide
-
not inhibitory at 5 mM, up to 37% inhibition at 20 mM
Sodium azide
-
not inhibitory at 1 mM, 25% inhibition of ATPase activity at 20 mM
Sodium azide
-
-
Sodium azide
-
hydrolysis of both ATP and ADP
Sodium azide
-
58% inhibition of the ATPase activity at 5 mM
Sodium fluoride
-
20 mM, 50% residual ATPase activity, 56% residual ADPase activity
Sodium fluoride
G1UFQ9
inhibits the ADPase activity rather than the ATPase activity of MP67
sodium orthovanadate
-
53% inhibition of the ATPase activity at 5 mM
sodium orthovanadate
G1UFQ9
has a strong inhibitory effect on ATPase activity and a weaker effect on ADPase activity of MP67
Sodium vanadate
P97687
Na3VO4
succinate
-
55% inhibition at 0.5 mM
suramin
-
-
suramin
-
0.1 mM, 10% residual activity
suramin
-
-
suramin
-
0.25 mM, 19% inhibition of ATPase activity
suramin
-
0.3 mM, 44% residual ATPase activity, 63% residual ADPase activity
suramin
-
a P2 purinoreceptor antagonist, 50% inhibition at 0.05-0.5 mM
suramin
Q6QHT8
an Ecto-ATPDase inhibitor, shows 60% inhibition of Ecto-ATPDase activities and 75% inhibition of trypomastigotes infectivity in vivo at 0.1 mM and 0.5 mM, respectively
suramin
-
0.5 mM suramin reduces enzyme activity in yeast living cells by 81.8%
Trifluoperazine
-
0.2 mM, 31% residual ATPase activity, 61% residual ADPase activity
triflupromazine
-
-
UDP
-
68% inhibition at 0.5 mM
UMP
-
92% inhibition at 0.5 mM
UMP
P97687
-
UTP
-
inhibitory at 0.6 mM and above, 34% inhibition at 0.5 mM
vanadate
Q6QHT8
1 mM, about 65% inhibition
vanadate
-
at 10 mM and pH 7.4, 7% inhibition of ATP hydrolysis, 54% inhibition of ADP hydrolysis
vanadate
Q70GK8
1 mM, inhibition
vanadate
-
15% inhibition at 1 mM
XTP
-
60% inhibition at 0.5 mM
Mn2+
-
at higher concentrations
additional information
-
not being altered by P-type, F-type or V-type NTPase inhibitors
-
additional information
-
no inhibition by NaN3
-
additional information
-
no inhibition by azide; no inhibition by orthovanadate; no inhibition by ouabain
-
additional information
-
no inhibition by orthovanadate; no inhibition by ouabain; no inhibition by P1,P5-di(adenosine-5'-)pentanphospate
-
additional information
-
no inhibition by lanthanum; no inhibition by levamisole; no inhibition by N-ethylmaleimide; no inhibition by oligomycin; no inhibition by orthovanadate; no inhibition by P1,P5-di(adenosine-5'-)pentanphospate
-
additional information
-
no inhibition by ouabain
-
additional information
-
-
-
additional information
-
no inhibition by ouabain
-
additional information
-
no inhibition by oligomycin; no inhibition by ouabain
-
additional information
-
no inhibition by oligomycin; no inhibition by orthovanadate; no inhibition by ouabain
-
additional information
-
no inhibition by NaN3; no inhibition by ouabain; no inhibition by p-NPP, beta-GP
-
additional information
-
no inhibition by Ap5A; no inhibition by ouabain
-
additional information
-
no inhibition by lanthanum; no inhibition by NEM; no inhibition by oligomycin; no inhibition by orthovanadate; no inhibition by ouabain
-
additional information
-
no inhibition by Ap5A; no inhibition by ouabain; no inhibition by tetramisole
-
additional information
Q6QHT8
not inhibitory: sodium azide, bafilomycin A, ammonium molybdate, DMSO
-
additional information
-
not inhibitory: oligomycin, ouabain, bafilomycin A, theophylline, thapsigarin, ethacrynic acid, P1,P5-(adenosine-5)pentyphosphate, omeprazole
-
additional information
-
not inhibitory: sodium orthovanadate, sodium fluoride, ammonium molybdate, oligomycin, sodium azide, bafilomycin A, ouabain, levamizole
-
additional information
-
not inhibitory: Concanavalin A, suramin
-
additional information
-
not inhibitory: ouabain, N-ethylmaleimide, orthovanadate, levamisole, P1,P5-di(adenosine 5)pentaphosphate
-
additional information
-
not inhibitory: N-ethylmaleimide, iodoacetamide, iodoacetic acid
-
additional information
-
not inhibitory: ouabain, N-ethylmaleimide, lanthanum, oligomycin, levamisole, cAMP
-
additional information
-
not inhibitory: vanadate, ouabain, thapsigargin, dicyclohexylcarbodiimide, oligomycin, bafilomycin A, levamisole, ammonium molybdate
-
additional information
-
not inhibitory: P1,P5-di(adenosine-5)pentaphosphate, ouabain, levamisole, oligomycin, N-ethylmaleimide, sodium azide
-
additional information
-
not inhibitory: oligomycin, sodium azide, bafilomycin A1, ouabain, furosemide, vanadate, molybdate, sodium fluoride, tartrate, levamizole
-
additional information
-
not inhibitory: Triton X-100
-
additional information
-
not inhibitory: N,N'-dicyclohexylcarbodiimide, azide, oligomycin, N'-ethylmaleimide, p-chloromercuribenzoate, orthovanadate, or ouabain
-
additional information
-
no inhibition by oligomycin, ouabain, and molybdate
-
additional information
-
the chicken enzyme does not show substrate inhibition
-
additional information
Q9Y5L3
the enzyme shows substrate inhibition
-
additional information
Q6QHT8
inhibition of Ecto-ATPDase by ant-Ecto-NTPDase-anti-serum, inhibition of Ecto-ATPDase activities and of trypomastigotes infectivity in vivo
-
additional information
-
discrimination between total ATPase activity and ecto-ATPase activity by using vanadate, oligomycin and N-ethylmaleimide as inhibitors of ATPases of type P, F and V to focus on ecto-ATPase activity
-
additional information
P55772
discrimination between total ATPase activity and ecto-ATPase activity by using vanadate, oligomycin and N-ethylmaleimide as inhibitors of ATPases of type P, F and V to focus on ecto-ATPase activity
-
additional information
-
ecto-ATPase activity is insensitive to 10 mM inorganic phosphate. Ammonium molybdate, 5'-AMP, 4-nitrophenyl phosphate, beta-glycerphosphate, sodium fluoride, sodium tartrate, levamizole, ouabain, oligomycin, and sodium azide have no effect on the Mg2+-stimulated ecto-ATPase
-
additional information
-
ATPase activity is not inhibited by DCCD
-
additional information
-
chicken NTPDase8 is not susceptible to substrate inactivation or agents that cause membrane perturbation, but its soluble mutant, lacking C- and N-termini, is susceptible to inhibition. This inhibition of the mutant can be abolished by mutant enzyme-crosslinking on membranes with glutaraldehyde, the ATPase activities of glutaraldehyde-treated chicken NTPDase8 ECD preincubated with ATP, ADP, and phosphate are respectively 95%, 80%, and 89% of the control
-
additional information
P97687
inhibition mechanism of polyoxometallates, overview
-
additional information
G1UFQ9
recombinant MpAPY2 shows no significant effect in the presence of vanadate
-
additional information
Q9FVC2
the activity of the GS52 enzyme is not significantly affected by Nod factor addition
-
additional information
Q5CXD0
antibodies directed against CApy block Cryptosporidium parvum sporozoite invasion of HCT-8 cells
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
-
activates to 148% at 0.5 mM
acetyl-CoA
-
activates to 148% at 0.5 mM
bafilomycin
-
13% activation at 0.001 mM
-
D-fructose-1,6-diphosphate
-
activates to 155% at 0.5 mM
L-glutamate
-
activation of ATP hydrolysis, no activation of ADP hydrolysis
lipophorin
-
-
-
MgCl2
-
stimulation in intact parasite
NP-40
-
0.1%, about 3fold activation
Ouabain
-
13% activation at 1 mM
oubain
-
138% relative ATPase activity at 1 mM oubain
Tartrate
-
14% activation at 10 mM
tri-iodothyronine
-
increase in enzyme activity and enzyme mRNA in isolated myocytes
MnCl2
-
stimulation in intact parasite, may substitute for MgCl2
additional information
-
not stimulatory: CaCl2, SrCl2, ZnCl2
-
additional information
-
ecto-apyrase is induced very early in response to inoculation with the symbiotic bacterium Bradyrhizobium japonicum
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.073
1,N6-etheno-ADP
-
30C, pH 6.0, presence of Ca2+
0.114
1,N6-etheno-ADP
-
30C, pH 6.0, presence of Ca2+
0.024
1,N6-Etheno-ATP
-
30C, pH 6.0, presence of Ca2+
0.031
1,N6-Etheno-ATP
-
30C, pH 6.0, presence of Ca2+
0.009
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate
-
30C, pH 6.0, presence of Ca2+
0.019
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate
-
30C, pH 6.0, presence of Ca2+
0.008
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate
-
30C, pH 6.0, presence of Ca2+
0.018
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate
-
30C, pH 6.0, presence of Ca2+
0.014
3'(2')-O-(methylanthranoyl)adenosine 5'-diphosphate
-
30C, pH 6.0, presence of Ca2+
0.017
3'(2')-O-(methylanthranoyl)adenosine 5'-diphosphate
-
30C, pH 6.0, presence of Ca2+
0.012
3'(2')-O-(methylanthranoyl)adenosine 5'-triphosphate
-
30C, pH 6.0, presence of Ca2+
0.018
3'(2')-O-(methylanthranoyl)adenosine 5'-triphosphate
-
30C, pH 6.0, presence of Ca2+
0.43
8-oxo-dGTP
-
pH 8.5, 37C
0.0025
ADP
P97687
recombinant mutant EDC K257M, pH 7.4, 25C; recombinant mutant EDC Y314F, pH 7.4, 25C
0.0047
ADP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
0.0051
ADP
P97687
recombinant mutant EDC Y409F, pH 7.4, 25C
0.0056
ADP
-
-
0.0059
ADP
P97687
recombinant mutant EDC DELTA MIL, pH 7.4, 25C
0.0074
ADP
-
-
0.0125
ADP
-
; pH 7.5, 37C
0.019
ADP
Q8BFW6
-
0.02
ADP
-
-
0.029
ADP
-
-
0.031
ADP
-
CaADP-
0.041
ADP
Q8K0L2
pH 7.4, 37C
0.041
ADP
G1UFQ9
pH 7.5, 25C; pH 7.5, 25C
0.042
ADP
-
free ADP
0.05
ADP
-
pH 7.2, 37C
0.07
ADP
-
variety Desiree, 20C
0.095
ADP
-
pH 7.6, 37C
0.1
ADP
-
variety Desiree, 30C
0.1
ADP
-
-
0.107
ADP
-
pH 8.0, 37C
0.13
ADP
-
variety Desiree, 40C
0.14
ADP
-
variety Pimpernel, 20C
0.15
ADP
-
pH 7.5, 37C, presence of Mg2+
0.163
ADP
-
pH 7.4, 37C
0.167
ADP
-
pH 7.4, 37C, presence of Ca2+
0.196
ADP
-
pH 7.5, 37C, presence of Ca2+
0.222
ADP
-
pH 7.4, 37C
0.25
ADP
-
variety Pimpernel, 30C
0.27
ADP
-
variety Pimpernel, 40C
0.291
ADP
-
-
0.309
ADP
-
pH and temperature not specified in the publication
0.5
ADP
-
-
0.72
ADP
-
pH 6.4, 37C
1
ADP
-
pH 7.4, 37C, recombinant enzyme
5.3
ADP
-
pH 7.4, 37C
0.117
AMP
-
pH 7.4, 37C
0.1712
AMPCPP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
0.0031
ATP
-
-
0.0073
ATP
-
-
0.011
ATP
Q8BFW6
-
0.013
ATP
Q8K0L2
pH 7.4, 37C
0.015
ATP
-
; pH 7.5, 37C
0.02
ATP
-
-
0.023
ATP
-
-
0.024
ATP
-
CaATP2-
0.025
ATP
-
free ATP
0.049
ATP
-
pH 7.2, 37C
0.062
ATP
-
-
0.0776
ATP
-
pH 8.0, 37C
0.083
ATP
-
pH 7.5, 37C, presence of Mg2+
0.085
ATP
-
pH 7.5, 37C, presence of Ca2+
0.097
ATP
-
pH 7.6, 37C
0.1
ATP
-
-
0.13
ATP
-
pH 6.4, 37C
0.141
ATP
-
pH 7.4, 37C, presence of Ca2+
0.169
ATP
G1UFQ9
pH 7.5, 25C; pH 7.5, 25C
0.2
ATP
-
-
0.224
ATP
-
pH 7.4, 37C
0.229
ATP
-
-
0.234
ATP
-
pH 7.4, 37C
0.4
ATP
-
pH 7.4, 37C, recombinant enzyme
0.424
ATP
-
pH and temperature not specified in the publication
0.51
ATP
-
pH 7.4, 37C
0.6
ATP
-
at 30C in 50 mM HEPES, pH 7.2
0.61
ATP
-
pH 7.2, 30C
0.777
CDP
-
pH 7.5, 37C, presence of Mg2+
0.148
CTP
-
pH 7.5, 37C, presence of Mg2+
0.018
dATP
-
30C, pH 6.0, presence of Ca2+
0.031
dATP
-
30C, pH 6.0, presence of Ca2+
0.89
dATP
-
pH 8.5, 37C
0.029
dCTP
-
30C, pH 6.0, presence of Ca2+
0.032
dCTP
-
30C, pH 6.0, presence of Ca2+
0.028
dGTP
-
30C, pH 6.0, presence of Ca2+
0.133
dGTP
-
30C, pH 6.0, presence of Ca2+
0.16
dGTP
-
pH 8.5, 37C
0.027
dTTP
-
30C, pH 6.0, presence of Ca2+
0.093
dTTP
-
30C, pH 6.0, presence of Ca2+
0.0114
GDP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
0.0131
GDP
P97687
in presence of 0.1 mM UMP, recombinant wild-type enzyme, pH 7.4, 25C
0.0488
GDP
P97687
in presence of 0.1 mM AMP, recombinant wild-type enzyme, pH 7.4, 25C
0.149
GDP
P97687
in presence of 0.1 mM AHM, recombinant wild-type enzyme, pH 7.4, 25C
0.357
GDP
-
pH 7.5, 37C, presence of Mg2+
0.009
GTP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
0.164
GTP
-
pH 7.5, 37C, presence of Mg2+
0.0105
IDP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
0.622
IDP
-
pH 7.5, 37C, presence of Mg2+
0.0108
ITP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
0.7495
TDP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
0.021
thio-dATP
-
30C, pH 6.0, presence of Ca2+
0.048
thio-dATP
-
30C, pH 6.0, presence of Ca2+
0.0113
UDP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
0.0175
UDP
P97687
recombinant mutant EDC DELTA MIL, pH 7.4, 25C
0.027
UDP
Q8BFW6
-
0.171
UDP
Q8K0L2
pH 7.4, 37C
0.555
UDP
-
pH 7.5, 37C, presence of Mg2+
0.01
UTP
Q8BFW6
-
0.01
UTP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
0.0129
UTP
P97687
recombinant mutant EDC DELTA MIL, pH 7.4, 25C
0.047
UTP
Q8K0L2
pH 7.4, 37C
0.207
UTP
-
pH 7.5, 37C, presence of Mg2+
0.259
ITP
-
pH 7.5, 37C, presence of Mg2+
additional information
additional information
-
kinetics with different substrates, overview
-
additional information
additional information
-
the enzyme shows Michaelis-Menten kinetics with all substrates except for UTP
-
additional information
additional information
-
substrate specificity and Michaelis-Menten kinetics, overview
-
additional information
additional information
P97687
kinetics, overview
-
additional information
additional information
G1UFQ9
Michaelis-Menten kinetics; Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
86
1,N6-etheno-ADP
-
30C, pH 6.0, presence of Ca2+
1384
1,N6-etheno-ADP
-
30C, pH 6.0, presence of Ca2+
682
1,N6-Etheno-ATP
-
30C, pH 6.0, presence of Ca2+
1642
1,N6-Etheno-ATP
-
30C, pH 6.0, presence of Ca2+
70
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate
-
30C, pH 6.0, presence of Ca2+
328
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate
-
30C, pH 6.0, presence of Ca2+
191
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate
-
30C, pH 6.0, presence of Ca2+
982
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate
-
30C, pH 6.0, presence of Ca2+
23
3'(2')-O-(methylanthranoyl)adenosine 5'-diphosphate
-
30C, pH 6.0, presence of Ca2+
828
3'(2')-O-(methylanthranoyl)adenosine 5'-diphosphate
-
30C, pH 6.0, presence of Ca2+
800
3'(2')-O-(methylanthranoyl)adenosine 5'-triphosphate
-
30C, pH 6.0, presence of Ca2+
965
3'(2')-O-(methylanthranoyl)adenosine 5'-triphosphate
-
30C, pH 6.0, presence of Ca2+
0.96
8-oxo-dGTP
-
pH 8.5, 37C
31.1
ADP
P97687
recombinant mutant EDC Y409F, pH 7.4, 25C
50.4
ADP
P97687
recombinant mutant EDC K257M, pH 7.4, 25C
77.3
ADP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
86.1
ADP
P97687
recombinant mutant EDC Y314F, pH 7.4, 25C
86.9
ADP
P97687
recombinant mutant EDC DELTA MIL, pH 7.4, 25C
40.5
AMPCPP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
860
ATP
-
pH 7.6, 37C
1.5
dATP
-
pH 8.5, 37C
636
dATP
-
30C, pH 6.0, presence of Ca2+
2222
dATP
-
30C, pH 6.0, presence of Ca2+
490
dCTP
-
30C, pH 6.0, presence of Ca2+
2174
dCTP
-
30C, pH 6.0, presence of Ca2+
0.74
dGTP
-
pH 8.5, 37C
573
dGTP
-
30C, pH 6.0, presence of Ca2+
3019
dGTP
-
30C, pH 6.0, presence of Ca2+
455
dTTP
-
30C, pH 6.0, presence of Ca2+
2841
dTTP
-
30C, pH 6.0, presence of Ca2+
82.6
GDP
P97687
in presence of 0.1 mM AMP, recombinant wild-type enzyme, pH 7.4, 25C
83.2
GDP
P97687
in presence of 0.1 mM UMP, recombinant wild-type enzyme, pH 7.4, 25C; recombinant wild-type enzyme, pH 7.4, 25C
103.7
GDP
P97687
in presence of 0.1 mM AHM, recombinant wild-type enzyme, pH 7.4, 25C
80.9
GTP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
79.9
IDP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
105.3
ITP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
80.2
TDP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
595
thio-dATP
-
30C, pH 6.0, presence of Ca2+
1101
thio-dATP
-
30C, pH 6.0, presence of Ca2+
80.9
UDP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
93
UDP
P97687
recombinant mutant EDC DELTA MIL, pH 7.4, 25C
103.4
UTP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
121.2
UTP
P97687
recombinant mutant EDC DELTA MIL, pH 7.4, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.4
8-oxo-dGTP
-
pH 8.5, 37C
2299
3.02
ADP
-
pH and temperature not specified in the publication
13
6100
ADP
P97687
recombinant mutant EDC Y409F, pH 7.4, 25C
13
14700
ADP
P97687
recombinant mutant EDC DELTA MIL, pH 7.4, 25C
13
16400
ADP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
13
20200
ADP
P97687
recombinant mutant EDC K257M, pH 7.4, 25C
13
26900
ADP
P97687
recombinant mutant EDC Y314F, pH 7.4, 25C
13
230
AMPCPP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
25099
1.28
ATP
-
pH and temperature not specified in the publication
4
1.6
dATP
-
pH 8.5, 37C
140
4.6
dGTP
-
pH 8.5, 37C
219
700
GDP
P97687
in presence of 0.1 mM AHM, recombinant wild-type enzyme, pH 7.4, 25C
53
1700
GDP
P97687
in presence of 0.1 mM AMP, recombinant wild-type enzyme, pH 7.4, 25C
53
6400
GDP
P97687
in presence of 0.1 mM UMP, recombinant wild-type enzyme, pH 7.4, 25C
53
7300
GDP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
53
9000
GTP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
37
7600
IDP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
444
9800
ITP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
229
110
TDP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
694
5300
UDP
P97687
recombinant mutant EDC DELTA MIL, pH 7.4, 25C
26
7200
UDP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
26
9400
UTP
P97687
recombinant mutant EDC DELTA MIL, pH 7.4, 25C
65
10300
UTP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
65
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.07
1-hydroxy-naphthalene-3,6-disulfonic acid
-
pH 7.6, 37C, substrate ADP
0.103
1-hydroxy-naphthalene-3,6-disulfonic acid
-
pH 7.6, 37C, substrate ATP
0.73
5'-p-fluorosulfonyl benzoyl adenosine
-
pH 8.5, 30C
2
5'-p-fluorosulfonylbenzoyladenosine
-
-
0.00859
ammonium heptamolybdate
P97687
recombinant wild-type enzyme, pH 7.4, 25C
0.0268
AMP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
0.267
POM-1
-
pH 7.4, 37C, recombinant enzyme
-
0.067
POM-6
-
pH 7.4, 37C, recombinant enzyme
-
5
Sodium azide
-
pH 7.6, 37C, substrate ADP
12
Sodium azide
-
pH 7.6, 37C, substrate ATP
1.7
suramin
-
pH 7.6, 37C, substrate ADP
1.8
suramin
-
pH 7.6, 37C, substrate ATP
0.3345
UMP
P97687
recombinant wild-type enzyme, pH 7.4, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.004
-
ADP, presence of Ca2+
0.007
-
ATP, presence of Ca2+
0.01
-
ATP, ADP homogenate of tissue
0.03
-
ATP, homogenate of tissue
0.0366
-
venom, substrate ATP
0.0598
-
venom, substrate ADP
0.07
-
ATP, media, fraction
0.08
-
-
0.08
-
ATP, microsome
0.08
-
ADP, intima, fraction; ATP, media, fraction
0.09
-
erythrocytes
0.1
-
-
0.1
-
ATP, homogenate of tissue
0.1
-
ADP, microsome
0.1
-
ATP, intima, fraction
0.15
-
ADP, homogenate of tissue
0.17
-
recombinant chimeric mutant hu-ck ACR1,5
0.17
Q9Y5L3
recombinant chimeric mutant hu-ck ACR1,5
0.175
-
substrate AMP, pH 7.4, 37C
0.1872
-
venom, substrate AMP
0.23
-
ATP, cytoplasm
0.238
Q6QHT8
ADPase activity, purified recombinant His-tagged enzyme
0.24
-
ADP, cytoplasm
0.24
Triticosecale Wittmack
-
ADP, homogenate of tissue
0.25
-
ADP, cytoplasm
0.27
-
ADP, 1.5 mM Ca2+, sarcolemmal fraction
0.28
Triticosecale Wittmack
-
ATP, homogenate of tissue
0.3
-
ATP, cytoplasm
0.33
-
ADP, homogenate of tissue
0.36
-
ATP, cytoplasm
0.4
-
ATP, ADP homogenate of tissue and microsome
0.4
Q6QHT8
ATPase activity, purified recombinant His-tagged enzyme
0.43
-
ATP, homogenate of tissue
0.47
-
liver
0.48
-
ATP, microsome
0.5
-
ATP, microsome, tuber
0.52
Triticosecale Wittmack
-
ADP, cytoplasm
0.6
-
ADP, cytoplasm
0.6
-
ADP, microsome
0.6
Triticosecale Wittmack
-
ATP, cytoplasm
0.7
-
ADP, microsome, tuber; ATP, homogenate of tuber
0.8
-
ADP, tissue
0.8
-
ATP, homogenate of tuber
0.854
-
partially purified enzyme
0.9
-
ADP, cytoplasm
0.9
-
ADP, homogenate of tissue
0.94
-
ADP, microsome
0.941
-
substrate ADP, pH 7.4, 37C
1
-
ATP, cytoplasm; ATP, homogenate of tissue
1
-
ATP, homogenate of tissue
1.1
-
ADP, homogenate of tissue
1.1
-
ATP, cytoplasm
1.2
-
ATP, 1.5 mM Ca2+, sarcolemmal fraction
1.2
-
ADP, cytoplasm
1.3
-
ADP, microsome
1.3
-
ATP, homogenate of tissue
1.3
-
pH 7.6, 37C, presence of 1.5 mM Cu2+
1.4
-
ATP, ADP, microsomes; ATP, cytoplasm
1.4
-
ADP, cytoplasm
1.5
-
ADP, cytoplasm
1.5
-
ATP, cytoplasm
1.806
-
venom, substrate 4-nitrophenyl thymidine 5'-phosphate
1.9
-
ADP, microsome
2.1
-
ATP, microsome
2.275
-
substrate ATP, pH 7.4, 37C
2.33
Q9Y5L3
purified recombinant wild-type enzyme
2.4
-
ATP
2.5
-
ATP, microsome
2.7
Triticosecale Wittmack
-
ADP, microsome
3
-
ATP, cytoplasm, tuber
3.6
Triticosecale Wittmack
-
ATP, microsome
4.1
-
pH 7.6, 37C, presence of 1.5 mM Ba2+
4.2
-
ADP, cytoplasm, tuber
7
-
ADP, microsome
7.3
-
ADP
8.4
-
-
10.8
-
pH 7.6, 37C, presence of 5 mM EDTA
12.7
-
ATP, microsome
12.8
G1UFQ9
substrate ATP, purified enzyme, pH 7.5, 25C; substrate ATP, purified MP67, pH 7.5, 25C
13
-
ADP
15.2
-
ATP
19.4
-
pH 7.6, 37C, presence of 1.5 mM Zn2+
25.6
-
pH 7.6, 37C
43.8
-
ADP
48.2
-
ATP
69.2
-
ADP
69.4
-
pH 7.6, 37C, presence of 1.5 mM Ca2+
84.2
-
pH 7.6, 37C, presence of 1.5 mM Mn2+
94.7
-
pH 7.6, 37C, presence of 1.5 mM Mg2+
639
-
purifed native enzyme from brain
1020
Q9Y5L3
purified recombinant extracellular domain, pH 7.5, in presence of Ca2+
1140
G1UFQ9
substrate ADP, purified enzyme, pH 7.5, 25C; substrate ADP, purified MP67, pH 7.5, 25C
1200
Q70GK8
hydrolysis of ADP, 37C, pH 8.0
1242
-
pH 7.4, 37C
1500
Q70GK8
hydrolysis of ATP, 37C, pH 8.0
additional information
-
Mg2+-stimulated activity in intact parasite is 5.24 nmol Pi per h and 10000000 cells
additional information
-
-
additional information
-
tissue-specific activity, overview
additional information
-
catalytic efficiency
additional information
-
immunocytochemical localization in retinal layers, compartmentalized regulation of extracellular nucleotide/nucleoside concentration in the retinal layers, potential role for extracellular nucleotide mediated-signaling in the retina of vertebrates
additional information
P55772
immunocytochemical localization in retinal layers, compartmentalized regulation of extracellular nucleotide/nucleoside concentration in the retinal layers, potential role for extracellular nucleotide mediated-signaling in the retina of vertebrates
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
Q8BFW6
and 7.4, ATPase activity
6
-
substrate ADP
6.4
Q8K0L2
hydrolysis of ADP
6.8 - 8
-
-
6.8
-
non-specific phosphatase assay at, substrate 4-nitrophenylphosphate
7 - 8
Orchopeas howardi, Oropsylla bacchi, Xenopsylla cheopis
-
-
7
A7LH73, A7LH74
assay at; assay at
7.2
Q6QHT8
assay at
7.4
Q8BFW6
and 5.0, ATPase activity
7.4
P97687, Q5DRK1
assay at; assay at
7.4
-
assay at
7.4
Q5CXD0
assay at
7.5
-
assay at
7.5
-
assay at
7.5
Q9Y5L3
assay at
7.5
-
the pH optimum of MgATPase of the wild-type full-length chicken NTPDase8 is in the neutral pH range while the pH optimum of the mutant MgADPase activity is more acidic at about pH 6.0
7.5
E0D877
assay at
7.5
G1UFQ9
assay at; assay at
7.6
-
-
8 - 9
-
-
8
Q8BFW6
ADPase activity
8
-
substrate ATP
8
Q70GK8
both hydrolysis of ATP and ADP
8.8
-
phosphodiesterase assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 9
-
the Mg2+-stimulated ATPase activity increases with the pH. At pH 9.0, the values of ATP hydrolysis are around 7fold higher than those obtained at pH 3.0
4 - 10.5
-
-
4.6 - 8.4
-
50% activity at pH 4.6 and 8.4
5 - 9
-
significant hydrolysis of both ATP and ADP at pH 6.5-pH 8.0, negligible hydrolysis of ATP or ADP substrates occurs at pH 9.0 or at pH 6.0 or lower
5.5 - 8
Q8K0L2
hydrolysis of ATP
6 - 6.5
-
substrate ADP
6 - 8.5
-
about 40% activity at pH 6, 100% activity at pH 7.5, about 55% activity at pH 8.5
6 - 9.5
-
50% activity at pH 6, no activity at pH 9.5
6.5 - 9.5
Orchopeas howardi, Oropsylla bacchi, Xenopsylla cheopis
-
-
7 - 8
-
-
7.5 - 8.5
-
substrate ATP
additional information
-
the MgATPase/MgADPase ratio of the full-length chicken NTPDase8 varies widely with pH, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23
Q5CXD0
assay at
25
-
assay at
25
A7LH73, A7LH74
assay at; assay at
25
P97687
assay at
25
G1UFQ9
assay at; assay at
30
-
assay at
30
-
assay at
37
-
assay at
37
Q9MYU4
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
Q70GK8
both hydrolysis of ATP and ADP
37
-
assay at
37
-
assay at
37
Q9Y5L3
native full-length enzyme
37
-
assay at
37
Q6QHT8
assay at
37
P97687, Q5DRK1
assay at; assay at
37
O35795
assay at
37
-
assay at
37
-
assay at
37
E0D877
assay at
62
Q9Y5L3
above, enzyme, recombinant soluble His-tagged secreted NTPDase2 extracellular domain
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 60
Q9Y5L3
native full-length enzyme
15 - 60
-
activity range, the activity of the full-length enzyme increases with temperature up to 60C, whereas the ATPase activity of the mutant truncated NTPDase8 ECD decreases at temperatures higher than 25C even when assayed for 1 min
30 - 62
Q9Y5L3
and above, recombinant soluble His-tagged secreted NTPDase2 extracellular domain
37 - 75
-
37-45C optimum, 75C no activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9 - 5.4
-
isoelectric focusing
4.9
-
isoelectric focusing
5.23
Q5CXD0
sequence calculation
6
Q8BFW6
calculated from amino acid sequence
6
Q8K0L2
calculated from amino acid sequence
6
-
isotype P0, isoelectric focusing; isotype P1, isoelectric focusing; isotype P2, isoelectric focusing
7.1
-
isotype P3, isoelectric focusing; isotype P4, isoelectric focusing
7.4
Q06K73, Q06K77
isoform Apy 1, calculated from amino acid sequence
9
Q06K73, Q06K77
isoform Apy 2, calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
12fold increase in activity compared to promastigote
Manually annotated by BRENDA team
-
smooth muscle cells
Manually annotated by BRENDA team
-
intima and media layers
Manually annotated by BRENDA team
Q9MYU4
aortic endothelial cells
Manually annotated by BRENDA team
-
expression of GS50
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
-
immunoreactive enzyme detected exclusively in neurons, primarily in axon-like structures and presynaptic elements. No enzyme in noradrenaline cells or terminals. Enzyme immunopositive cells mostly also express hypocretin-1/orexin-A
Manually annotated by BRENDA team
-
substantial portion of ATP-hydrolyzing activity depends on enzyme, enzyme is coexpressed with ecto-ATPase
Manually annotated by BRENDA team
-
increase in enzymic activity from birth to day 30, decrease afterwards, highest enzymic activity at day 30, highest affinity for enzyme at day 365, relative abundance of enzyme is highest at day 15 of ontogeny
Manually annotated by BRENDA team
-
marked enzyme immunoreactivity in primary afferent neurones of the spiral ganglion and synaptic regions of the inner and outer hair cells
Manually annotated by BRENDA team
-
seedling cotyledons
Manually annotated by BRENDA team
-
two enzyme isoforms with different net charge but identical molecular weight. In soluble egg antigen, presence of isoform with lower net charge. Localization on external surface of miracidium and in von Lichtenbergs envelope
Manually annotated by BRENDA team
-
enzyme is widely distributed in the embryo, from late neurulae through to late tailbud stages
Manually annotated by BRENDA team
Q9FEA6
plumule, hook, and elongating regions of the epicotyl and in the region between cotyledons and epicotyls
Manually annotated by BRENDA team
O35795
portal fibroblasts
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
portal fibroblasts
-
Manually annotated by BRENDA team
-
expression of GS50
Manually annotated by BRENDA team
-
absent from Mller glia
Manually annotated by BRENDA team
-
hepatic stellate cell line. Both phenotypes of GRX cell line express NTPDase 3 and 5, but only activated cells express NTPDase 6, quantitative real-time PCR expression analysis of Entpd genes, overview
Manually annotated by BRENDA team
-
ventricle, detected by immunoblotting in smooth muscle cells and endothelial cells
Manually annotated by BRENDA team
-
ventricle, sarcolemma
Manually annotated by BRENDA team
-
cardiac vasulature, endothelium, endocardium and to a lesser extent in vascular smooth muscle
Manually annotated by BRENDA team
P97687, Q5DRK1
restricted to the canalicular membrane domain of hepatocytes
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
restricted to the canalicular membrane domain of hepatocytes
-
Manually annotated by BRENDA team
-
cultured neurons, soma of pyramidal and bipolar neurons
Manually annotated by BRENDA team
-
substantial portion of ATP-hydrolyzing activity depends on enzyme, enzyme is coexpressed with ecto-ATPase
Manually annotated by BRENDA team
-
NTPDases 1 and 2 differentially localized in
Manually annotated by BRENDA team
P55772
diffuse labelling of
Manually annotated by BRENDA team
A1BXT9
ATPDase1 is located at the external surface of the parasite
Manually annotated by BRENDA team
-
surface and membrane, the active site of the ATP-diphosphohydrolase is oriented to the external surface of the tegument
Manually annotated by BRENDA team
-
cortex, detected by immunoblotting in blood vessel walls of glomerular and peritubular capillaries
Manually annotated by BRENDA team
-
ATPDase/cd39 detected by immunoblotting in vascular endothelium and smooth muscles (blood vessel walls)
Manually annotated by BRENDA team
-
mRNA found in this tissue
Manually annotated by BRENDA team
-
ATPDase detected by immunoblotting in luminal side of the ductular epithelium
Manually annotated by BRENDA team
-
low enzyme activity
Manually annotated by BRENDA team
-
expression of GS50
Manually annotated by BRENDA team
-
ATPDase/cd39 detected by immunoblotting in vascular endothelium and smooth muscles (blood vessel walls), ATPDase detected by immunoblotting in bile canaliculi of hepatocytes
Manually annotated by BRENDA team
-
bile canaliculi
Manually annotated by BRENDA team
-
high enzyme activity
Manually annotated by BRENDA team
-
expression of isozymes NTPDase1, -2, and -8 in distinct liver compartments in normal and fibrotic rat liver
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
expression of isozymes NTPDase1, -2, and -8 in distinct liver compartments in normal and fibrotic rat liver
-
Manually annotated by BRENDA team
-
mRNA found in this tissue
Manually annotated by BRENDA team
-
detected by immunoblotting in trachea, alveolar cells, airway and vascular smooth muscle cells, submucous glanda, chondrocytes, leucocytes, endothelial cells, mesothelial cells
Manually annotated by BRENDA team
Q9FEA6
mainly localized in the cytoplasm and around nuclei in the apical meristem
Manually annotated by BRENDA team
Streptomyces aureofaciens RIA, Streptomyces aureofaciens RIA57
-
-
-
Manually annotated by BRENDA team
-
ventricular neonatal myocyte
Manually annotated by BRENDA team
P55772
activity on surface of
Manually annotated by BRENDA team
-
synaptosome from brain cortex
Manually annotated by BRENDA team
-
alkaline phosphatase depleted
Manually annotated by BRENDA team
P55772
sharp thin band in, mainly restricted to horizontal cell processes in
Manually annotated by BRENDA team
-
photoreceptor segments, NTPDases 1 and 2 differentially localized in
Manually annotated by BRENDA team
-
mRNA found in this tissue
Manually annotated by BRENDA team
-
young, expression of GS50
Manually annotated by BRENDA team
-
surface and flagellar pocket
Manually annotated by BRENDA team
-
12fold increase in activity compared to amastigote
Manually annotated by BRENDA team
P55772
expression in, also in intraretinal blood vessels of, no expression in Mller glia, highly in optic fiber bundles
Manually annotated by BRENDA team
-
expression of GS50 and GS52
Manually annotated by BRENDA team
-
expression of GS50 and GS52
Manually annotated by BRENDA team
Q9FEA6
mainly localized in the cytoplasm and around nuclei in the root tip
Manually annotated by BRENDA team
Q70GK8
storage of enzyme in lumen of salivary gland D1 pairs, about one half of enzyme is consumed during feeding, upregulation of enzyme mRNA level after feeding
Manually annotated by BRENDA team
Oropsylla bacchi, Orchopeas howardi, Xenopsylla cheopis
-
-
Manually annotated by BRENDA team
-
cell culture from submandibular salivary gland
Manually annotated by BRENDA team
-
enzyme synthesis
Manually annotated by BRENDA team
-
salivary gland-specific apyrase, developmental- and tissue-specific enzyme expression
Manually annotated by BRENDA team
-
green, expression of GS50
Manually annotated by BRENDA team
-
mRNA found in this tissue
Manually annotated by BRENDA team
-
low enzyme activity
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
Q5CXD0
polar localization of Capy, possible co-localization with the apical complex of the parasite
Manually annotated by BRENDA team
-
cytoskeleton
Manually annotated by BRENDA team
-
expression of GS50 and GS52
Manually annotated by BRENDA team
-
specific expression of NT5E-2
Manually annotated by BRENDA team
Q6QHT8
sequential sub-cultivation in mammalian cells, at third to fourth passages most of the cell-derived trypomastigotes cannot penetrate mammalian cells and have differentiated into amastigote-like parasites that exhibit 3-4fold lower levels of Ecto-NTPDase activities
Manually annotated by BRENDA team
-
smooth muscle cells
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
P97687
CD39 and NTPDase1 are the dominant NTPDases
Manually annotated by BRENDA team
O35795
cells in the vascular external layer
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
cells in the vascular external layer
-
Manually annotated by BRENDA team
additional information
Q6QHT8
external surface of all forms of parasite
Manually annotated by BRENDA team
additional information
-
apyrase is an ecto-enzyme
Manually annotated by BRENDA team
additional information
A1BXT9
ATPDase1 is found in adult worm tegument basal and apical membranes, immunohistochemic localization anaylsis, ATPDase2 is found in adult worm tegument basal and apical membranes, and in the tegument syncytium, immunohistochemic localization anaylsis
Manually annotated by BRENDA team
additional information
-
ATPDase2 is found in adult worm tegument basal and apical membranes, and in the tegument syncytium, immunohistochemic localization anaylsis
Manually annotated by BRENDA team
additional information
-
GS50 and GS52 expression levels in different tissues, overview
Manually annotated by BRENDA team
additional information
-
enzyme tissue localization by in situ immunohistochemistry, overview
Manually annotated by BRENDA team
additional information
Q5CXD0
isolated CApy interacts with the host cell
Manually annotated by BRENDA team
additional information
G1UFQ9
MP67 is ubiquitously distributed in various tissues, most abundantly in leaves
Manually annotated by BRENDA team
additional information
-
NTPs may be hydrolyzed mainly by NTPDase 3 in GRX cells and the increase in the NTPs hydrolysis observed in lipocytes is probably related to the up-regulation of Entpd3 mRNA expression
Manually annotated by BRENDA team
additional information
Rattus norvegicus Sprague-Dawley
-
enzyme tissue localization by in situ immunohistochemistry, overview
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q9Y5L3
the enzyme contains two transmembrane domains and five apyrase conserved regions, ACRs. ACR1 is located near the N-terminal transmembrane domain, whereas ACR5 is located near the C-terminal transmembrane domain
Manually annotated by BRENDA team
-
NTPDase8 is a cell surface ectonucleotidase with a large extracellular domain containing the active site and is anchored to the membrane by two transmembrane domains at the N- and C-termini
Manually annotated by BRENDA team
-
and some secretion, enzyme expressed in HEK 293 cell
Manually annotated by BRENDA team
-
mainly localized to endoplasmic reticulum, plus some secretion, enzyme expressed in HEK 293 cell
-
Manually annotated by BRENDA team
A1BXT9
ATPDase2 is secreted by the worm to the culture medium
-
Manually annotated by BRENDA team
Q9FVC2
the catalytic domain of the GS52 ectoapyrase is extracellular and therefore, must act to hydrolyze extracellular nucleotides
-
Manually annotated by BRENDA team
Q9NQZ7
associated with membrane
Manually annotated by BRENDA team
Q3TCT4
associated with membrane
Manually annotated by BRENDA team
-
membrane-bound
Manually annotated by BRENDA team
-
ectonucleotidase/ectoenzyme
Manually annotated by BRENDA team
-
ectonucleotidase/ectoenzyme
Manually annotated by BRENDA team
-
ectonucleotidase/ectoenzyme
Manually annotated by BRENDA team
-
ectonucleotidase/ectoenzyme
Manually annotated by BRENDA team
-
synaptic plasma membrane
Manually annotated by BRENDA team
A1BXT9
ATPDase2 contains a single N-terminal transmembrane domain
Manually annotated by BRENDA team
Q9Y5L3
the enzyme contains two transmembrane domains and five apyrase conserved regions, ACRs. ACR1 is located near the N-terminal transmembrane domain, whereas ACR5 is located near the C-terminal transmembrane domain
Manually annotated by BRENDA team
-
NTPDase8 is a cell surface ectonucleotidase with a large extracellular domain containing the active site and is anchored to the membrane by two transmembrane domains at the N- and C-termini
Manually annotated by BRENDA team
-
located at the surface of the plasma membrane
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
-
associated to microvesicles
-
Manually annotated by BRENDA team
Secale cereale, Triticosecale Wittmack
-
-
-
Manually annotated by BRENDA team
additional information
Q9FEA6
not detected in vacuoles and cell walls
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35200
Q06K73, Q06K77
mature isoform Apy 2, calculated from amino acid sequence
712658
35800
Q06K73, Q06K77
mature isoform Apy 1, calculated from amino acid sequence
712658
40000
-
gel filtration
210145
40000
-
SDS-PAGE
210154
43000
-
there are two bands detected at 48000 and 43000 Da, SDS-PAGE
713185
44000
-
gel filtration
210153
48000
-
there are two bands detected at 48000 and 43000 Da, SDS-PAGE
713185
49000
-
gel filtration
210140
49000
-
SDS-PAGE
210152
49000
Q9FEA6
gel filtration
713333
50000
-
SDS-PAGE
210141
50000
Q06K73, Q06K77
recombinant Apy 2 thioredoxin-His-tagged fusion protein, SDS-PAGE
712658
51000
-
SDS-PAGE
210169
56000
-
-
210157
57000
-
gel filtration
210153
57760
Q9MYU4
calculated from amino-acid composition
210150
58600
-
gel filtration
696153
60000 - 70000
-
immunoblotting
210161
60500
-
radiation-inactivation, ADPase
210165
62700
-
radiation-inactivation, ATPase
210165
64000
-
SDS-PAGE
210160, 210165
65000
-
SDS-PAGE
210144
67000
-
SDS-PAGE
210155
67000
-
SDS-PAGE
210160
70000 - 80000
-
SDS-PAGE, immunoblotting
210151
71000
-
-
210147
75000
-
highly glycosylated protein, N-linked oligosaccarides, immunoaffinity techniques, SDS-PAGE
210149
78000
-
highly glycosylated, nominal weight of 57 kDa
210148
78000
-
immunoaffinity techniques, SDS-PAGE, ATPDase/cd39
210149
78000
-
nominal weight of 54 kDa, 6-12 NH2-linked oligosaccharide chains, SDS-PAGE, N-glycosidase F treatment
210156
78000
-
-
210159
83000
-
gel filtration
210133
140000
-
crosslinking experiments with glutaraldehyde plus SDS-PAGE, or blue native PAGE
655457
205000
-
analystical ultracentrifugation
667532
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 80000, SDS-PAGE
?
-
x * 78000, SDS-PAGE
?
-
x * 72000, SDS-PAGE
?
G1UFQ9
x * 52000, SDS-PAGE, x * 67000, SDS-PAGE
?
-
x * 67000, SDS-PAGE
?
-
x * 85000, SDS-PAGE
?
-
x * 68000, SDS-PAGE
?
Q8K0L2
x * 54650, deduced from gene sequence
?
Q6QHT8
x * 58000, SDS-PAGE, x * 69000, deduced from gene sequence
?
Q8BFW6
x * 58950, deduced from gene sequence
?
-
x * 65000-90000, glycosilated protein, x * 48000, deglycosilated protein, SDS-PAGE
?
Q3TCT4
x * 70000, deduced from gene sequence
?
Q70GK8
x * 79000, glycosylated form, SDS-PAGE, x * 59800, unglycosylated mature form, calculated, x * 88000, 82000, 79000, 68000, or 67000, SDS-PAGE
?
-
x * 88000, 82000, 79000, 68000, or 67000, SDS-PAGE
?
Q9Y5L3
x * 62000, recombinant soluble His-tagged secreted NTPDase2 extracellular domain, SDS-PAGE
?
A7LH73, A7LH74
x * 67000, recombinant, secreted isozyme I, SDS-PAGE
?
Q5CXD0
x * 36932, sequence calculation, x * 50000, about, recombinant enzyme, SDS-PAGE
?
-
x * 50000, about, isozymes APY1 and APY2, SDS-PAGE
dimer
-
2 * 70000-80000, SDS-PAGE
dimer
-
crosslinking experiments
dimer
-
or trimer, of isoforms with molecular masses of 88000, 82000, 79000, 68000, or 67000 Da
monomer
-
1 * 50000, SDS-PAGE
monomer
-
1* 51000
trimer
-
or dimer, of isoforms with molecular masses of 88000, 82000, 79000, 68000, or 67000 Da
monomer
-
1 * 60200, SDS-PAGE
additional information
-
detection of bands of 95000, 80000, 60000 Da by antibody
additional information
A7LH73, A7LH74
comparisons of predicted isozyme tertiary structure, N-terminal Edman sequence analysis and mass spectrometry, overview
additional information
A7LH73, A7LH74
comparisons of predicted isozyme tertiary structures, N-terminal Edman sequence analysis and mass spectrometry, overview
additional information
-
identification of ACR regions in residues 40-454 possibly involved in metal binding, sequence comparison, and structure analysis and modeling, overview
additional information
P80595
structure comparison and molecular modelling
additional information
A1BXT9
structure comparison and molecular modelling, evolutionary structural relationships, overview
additional information
P80595
structure comparison and molecular modelling, evolutionary structural relationships, overview
additional information
-
the enzyme contains five apyrase conserved regions
additional information
-
GS52 apyrase structure modeling of apo-form and tertiary complex with the nonhydrolyzable ATP analogue AMPPNP and cofactor Ca2+, overview
additional information
-
NTPDase8 is a cell surface ectonucleotidase with a large extracellular domain containing the active site and is anchored to the membrane by two transmembrane domains at the N- and C-termini
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
-
glycoprotein
-
6-12 NH2-linked oligosaccharide chains
glycoprotein
Q5CXD0
CApy in its mature form is posttranslationally glycosylated in an N-linked fashion
glycoprotein
-
-
glycoprotein
-
interaction with concanavalin-A
glycoprotein
G1UFQ9
MP67 is glycosylated
glycoprotein
Q8K0L2
amino acid sequence shows eight putative N-glycosilation sites
proteolytic modification
-
predicted site of cleavage for the mature protein of the 50-nucleotidase isoforms, mass spectrometry
glycoprotein
-
treatment with endoH or PNGase F results in a protein of 56000 Da
glycoprotein
-
hyperglycosylation, mass of glycosylated protein is 65000-90000, mass of deglycosylated protein is 48000 Da
glycoprotein
-
highly glycosylated, nominal weight of 57 kDa
glycoprotein
-
N-linked oligosaccarides
glycoprotein
Q70GK8
N-glycosylated protein, purification gives five N-glycosylated proteins of 88, 82, 79, 68, and 67 kDa molecular masses
proteolytic modification
Q70GK8
sequence contains a 23 amino acid signal peptide
glycoprotein
-
purification gives five N-glycosylated proteins of 88, 82, 79, 68, and 67 kDa molecular masses
additional information
-
enzyme oligomers are stabilized by intermolecular disulfide bonds
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type enzyme, free or in complex with decavanadate or heptamolybdate, X-ray diffraction structure determination and analysis at 1.7-2.5 A resolution, modeling
P97687
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
-
irreversible thermal inactivation
689891
75
-
10 min, 60% activity remain
210137
89
-
20 min, no loss of activity
678480
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivated by Tween 20
-
unstable to detergent Triton X-100
-
unstable to detergent Triton X-100
-
the detergents Triton X-100, deoxycholate, CHAPS, Nonidet, N-octoglucoside, C12E8 inactivate the enzyme, digitonin is not harmful
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
perchloric acid
-
enzyme remains active
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, octylglucoside, stable
-
4C, purified recombinant extracellular domain, stable for several weeks
Q9Y5L3
0-4C, 25 mM Tris.HCl, pH 7.4, 7 days, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from insect Sf9 cells by anion exchange chromatography to homogeneity, large scale preparation
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography, denaturing by urea and renaturing using glutathione and dialysis
E0D877
native enzyme 4915fold from brain by ammonium sulfate fractionation, hydrophobic interaction chromatography, gel filtration, anion exchange and hydroxyapatite chromatography, again gel filtration, and adsorption chromatography
-
two ATPDase isoforms
-
recombinant rCApy C-terminally fused to a His6/S-tag solubilized from inclusion bodies after expression in Escherichia coli strain BL21(DE3), by nickel and glutathione affinity chromatography
Q5CXD0
recombinant His-tagged wild-type and mutant NTPDase8s from HEK293 cell plasma membranes by ammonium sulfate fractionation and nickel affinity column chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli
-
recombinant GS52 from Escherichia coli and tabacco
Q9FVC2
partially
-
recombinant His-tagged soluble NTPDase2 extracellular domain from HEK-293 cells by ammonium sulfate fractionation, ultrafiltration, nickel affinity chromatography, and gel filtration
Q9Y5L3
reconstitution of enzyme in lipid vesicles is associated with a decrease in KM value of nearly an order of magnitude over the detergent-solubilized form, with a concomitant increase in both ADPase and ATPase catalytic efficiencies
-
recombinant His6-tagged Lpg1905 from Escherichia coli BL21(DE3) C41 strain by nickel affinity chromatography
-
native enzyme to homogeneity by ammonium sulfate fractionation, anion exchange chromatography, and concanavalin A affinity chromatography, recombinant enzyme from Escherichia coli
G1UFQ9
native enzyme from salivary gland by anion exchange chromatography, ultrafiltration, and cation exchange chromatography; native enzyme from salivary gland by anion exchange chromatography, ultrafiltration, and cation exchange chromatography
A7LH73, A7LH74
His SpinTrap column chromatography; His SpinTrap column chromatography
Q06K73, Q06K77
native enzyme partially by apoplast preparation
-
recombinant enzyme expressed in Pichia pastoris
-
purified from liver
-
salivary enzyme, purification gives five N-glycosylated proteins of 88, 82, 79, 68, and 67 kDa molecular masses; salivary enzyme, purification gives five N-glycosylated proteins of 88, 82, 79, 68, and 67 kDa molecular masses
Q70GK8
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Q6QHT8
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Spodoptera frugiperda Sf9 cells using the baculovirus infection system
-
expression of His-tagged enzyme in Escherichia coli
E0D877
DNA and amino acid sequence determination and analysis of the salivary gland-specific apyrase, genotyping and promoter analysis, developmental- and tissue-specific gene expression in three Anopheles gambiae transgenic lines, overview
-
isozymes APY1 and APY2, expression analysis, APY1 and APY2 promoter activity is high under conditions that induced stomata opening
-
Bacillus subtilis gene ytkD cloned and expressed in Escherichia coli
-
expression in COS-7 cells
-
gene capy, single copy gene, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of CApy C-terminally fused to a His6/S-tag in Escherichia coli strain BL21(D3)
Q5CXD0
cloning of His-tagged wild-type and mutant NTPDase8s in Escherichia coli strain DH5alpha and stable expression in HEK293 cell plasma membranes
-
expression of mutant hu-ck ACR1,5 chimeric enzymes in HEK-293 cells
-
quantitative real-time RT-PCR expression analysis, recombinant expression of HA-tagged wild-type and mutant enzymes in transgenic soybean roots via Agrobacterium rhizogenes-mediated hairy root transformation, expression of His-tagged wild-type and mutant enzymes in Escherichia coli
-
expression of GS52 in Escherichia coli and in tabacco
Q9FVC2
GS50 and GS52 expression analysis, overexpression of the ecto-apyrase in Lotus japonicus increasing the level of rhizobial infection and enhanced nodulation
-
-
Q9NQZ7
CD39, expression in COS-7 cells
-
expression of mutant hu-ck ACR1,5 chimeric enzymes in HEK-293 cells, stable expression of soluble His-tagged secreted NTPDase2 extracellular domain in HEK-293 cells
Q9Y5L3
gene LALP70 cloned into the mammalian expression vector pCl-Neo, expression on the surface of COS-7 cells
-
expression of a His6-tagged Lpg1905 using plasmid pRSET:lpg1905 in Escherichia coli BL21(DE3) C41 strain
-
MP67 DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Escherichia coli mainly in inclusion bodies; MpAPY2 DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Escherichia coli
G1UFQ9
genes Entpd1, 2, 3, 5, 6, and Entpd8
-
DNA and amino acid sequence determination and analysis of isozyme II, phylogenetic analysis; DNA and amino acid sequence determination and analysis of isozyme I, phylogenetic analysis, expression of isozyme I as secreted protein in Pichia pastoris strain GS115
A7LH73, A7LH74
expressed as a thioredoxin-His-tagged fusion protein in Escherichia coli BL21 cells; expressed as a thioredoxin-His-tagged fusion protein in Escherichia coli BL21 cells
Q06K73, Q06K77
expression in cells of chinese hamster ovaries
-
recombinant expression of the mutant NTPDase1 ECD DELTAMIL in Escherichia coli in soluble form and refolding to the active state
P97687
gene encoding ATPDase2, DNA and amino acid sequence determination and analysis, sequence comparison
A1BXT9
phylogenetic analysis
A1BXT9
phylogenetic analysis
P80595
expression in COS-7 cells
Q9MYU4
expression of the C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Q6QHT8
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APY expression in guard cell protoplasts rises quickly when these cells are moved from darkness into light
-
expression of the GS52 gene is induced upon Bradyrhizobium japonicum inoculation
Q9FVC2
APY1 and APY2 are up-regulated when cotton fibers enter their rapid growth phase
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D209A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
E182A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
Q216A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
C10S
-
112% of wild-type ATPase activity, 105% of wild-type ADPase activity, residue responsible for dimer formation
C10S/C501S
-
148% of wild-type ATPase activity, 133% of wild-type ADPase activity
C10S/C501S/C509S
-
79% of wild-type ATPase activity, 77% of wild-type ADPase activity
C10S/C509S
-
103% of wild-type ATPase activity, 99% of wild-type ADPase activity
C501S
-
130% of wild-type ATPase activity, 130% of wild-type ADPase activity, site of modification by p-chloromercuriphenylsulfonic acid
C501S/C509S
-
138% of wild-type ATPase activity, 134% of wild-type ADPase activity
N168A
-
site-directed mutagenesis, the mutant shows reduced activity due to decreased affinity for the nucleotide substrates, with a relatively increased Km 1.3fold for ATP hydrolysis and 3fold for ADP hydrolysis for the mutant enzyme, the mutant partially restores the ability of an enzyme-deficient Legionella pneumophila lpg1905 mutant strain to replicate in THP-1 macrophages
Q193A
-
site-directed mutagenesis, inactive mutant
R122A
-
site-directed mutagenesis, inactive mutant
Y409F
P97687
site-directed mutagenesis
additional information
-
construction of a hu-ck ACR1,5 chimera in which the extracellular domain of human NTPDase2 is anchored to the membrane by the two transmembrane domains of the chicken NTPDase8. The hu-ck ACR1,5 chimera is the first chimeric NTPDase reported that shows a resistance to membrane perturbation and substrate inactivation. The strength of interaction of the respective transmembrane domain pairs of the human NTPDase2 and chicken NTPDase8 determine their different responses to membrane perturbation and substrate. The chimeric mutants all show highly reduced ATPase activities, overview. Catalysis at the active site in the extracellular domain of the hu-ck ACR1,5 chimera is no longer negatively affected by membrane perturbation in the lipid bilayer by detergent and temperature
additional information
-
generation of a soluble truncated mutant NTPDase8 by removal of amino acids 1-28 (containing TMD1) and 464-493 (containing TMD2), the mutant shows 85% reduced activity compared to the full-length membrane-bound enzyme. Generation of chimeric mutant Ck-hu TMD1, encoding a protein in which the N-terminus (aa 1-28) of the chicken NTPDase8 is substituted with the corresponding region (aa 1-29) of the human NTPDase2, which includes its TMD1, and of chimeric mutant Ck-hu TMD2, encoding a protein in which the C-terminus (aa 465-493) of the chicken NTPDase8 is substituted with the corresponding region (aa 461-495) of the human NTPDase2, which includes its TMD2
S214A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
additional information
-
RNA interference to silence GS52 expression in Glycine max roots using Agrobacterium rhizogenes-mediated root transformation. Transcript levels of GS52 are significantly reduced in GS52 silenced roots, and these roots exhibit reduced numbers of mature nodules. Development of the nodule primordium and subsequent nodule maturation is significantly suppressed in GS52 silenced roots. Application of exogenous adenosine diphosphate to silenced GS52 roots restores nodule development, phenotype, overview
C509S
-
148% of wild-type ATPase activity, 155% of wild-type ADPase activity
additional information
Q9Y5L3
construction of a hu-ck ACR1,5 chimera in which the extracellular domain is anchored to the membrane by the two transmembrane domains of the chicken NTPDase8. The hu-ck ACR1,5 chimera is the first chimeric NTPDase reported that shows a resistance to membrane perturbation and substrate inactivation. The strengths of interaction of the respective transmembrane domain pairs of the human NTPDase2 and chicken NTPDase8 determine their different responses to membrane perturbation and substrate. The chimeric mutants all show highly reduced ATPase activities, overview. Catalysis at the active site in the extracellular domain of the hu-ck ACR1,5 chimera is no longer negatively affected by membrane perturbation in the lipid bilayer by detergent and temperature
additional information
-
inactivation of apy-1 function by RNAi increased GFP expression fourfold with respect to control, which reflects an hsp-4 upregulation, indicating that loss of apy-1 may effectively cause endoplasmic reticulum stress
E159A
-
site-directed mutagenesis, inactive mutant
additional information
-
following intratracheal inoculation of A/J mice, none of the Lpg1905 mutants is able to restore virulence to an lpg1905 mutant during lung infection
W384A
-
site-directed mutagenesis, inactive mutant
additional information
-
Cd39-/- mice phenotype with increased levels of macrophages and neutrophils, cerebral ischemia effects, overview. 50% increase in the number of alphaMbeta2-integrin high-expressing monocytes in Cd39-/- mice compared with wild-type controls. Although an acute rescue from CD39 deficiency can be obtained through administration of an apyrase or solCD39 analog, a permanent rescue can be obtained via bone marrow reconstitution with CD39-bearing cells
K257M
P97687
site-directed mutagenesis
additional information
-
construction of chimeric proteins from enzyme and ectoATPase. ectoATPase prefers ATP as substrate over ADP and releases mainly ADP. Chimeras contain N-terminal sequences of enzyme of increasing length fused to ectoATPase and vice versa. Protein structure rather than conserved regions may be of major relevance for determining differences in the catalytic properties
additional information
P97687
replacement of the extracellular domain of Rattus norvegicus NTPDase1, i.e. amino acid sequence 190TQEQSWLNFISDSQKQA206, with the shorter hydrophilic loop found in Homo sapiens NTPDase6, 240KTPGGS245. This NTPDase1 ECD DELTAMIL mutant variant is a soluble NTPDase1 that lacks a putative membrane interaction loop identified between the two lobes of the catalytic domain
Y413F
P97687
site-directed mutagenesis
additional information
-
mutational analysis of residues involved in catalysis, overview
additional information
-
silencing of the apyrase with RNAi constructs under the control of the constitutive 35S promoter leads to a strong decrease in apyrase activity to below 10% of the wild-type level. This decreased activity leads to phenotypic changes in the transgenic lines, including a general retardation in growth, an increase in tuber number per plant, and differences in tuber morphology. Silencing of apyrase under the control of a tuber-specific promoter B33 leads to similar changes in tuber morphology, but not to direct effects of apyrase inhibition on tuber metabolism, phenotypes, overview
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant rCApy from inclusion bodies after expression in Escherichia coli strain BL21(DE3), resuspended in 20 mM sodium phosphate, pH 7.4, 500 mM NaCl, 6 M guanidine hydrochloride
Q5CXD0
using 8 M urea, 50 mM Tris-HCl (pH 8.0), 1 mM EDTA and 1 mM dithiothreitol; using 8 M urea, 50 mM Tris-HCl (pH 8.0), 1 mM EDTA and 1 mM dithiothreitol
Q06K73, Q06K77
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
enzyme inhibits ADP- collagen- and thrombin-induced human platelet aggregation in dose-dependent manner, use as a therapeutic agent for inhibition of platelet-mediated thrombosis
pharmacology
-
the enzyme may serve as a therapeutic agent for inhibition of platelet-mediated thrombosis
agriculture
-
expression of enzyme in in Lotus japonicus results in enhanced nodulation that correlates with expression level
medicine
-
enzyme in lipid vesicles effectively inhibits platelet aggregation when activated by ADP, collagen, or thrombin, and also promotes platelet disaggregation. Treatment with enzyme lipid vesicles preserves platelet counts after thromboplastin injection
medicine
-
its unique enzymatic activity makes the salivary apyrase an attractive candidate as a therapeutic agent for the treatment of thrombotic pathologies
medicine
A1BXT9
significant IgG antibody reactivity was observed in sera from patients with American cutaneous leishmaniasis and schistosomiasis using Schistoma mansoni adult worm or egg as antigen, development of drug targets or molecular markers
medicine
P80595
significant IgG antibody reactivity was observed in sera from patients with American cutaneous leishmaniasis and schistosomiasis using potato apyrase as antigen, development of drug targets or molecular markers
drug development
Q6QHT8
Ecto-NTPDase1 is a target candidate in chemotherapy of Chagas disease