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Information on EC 3.6.1.5 - apyrase and Organism(s) Sus scrofa and UniProt Accession Q9MYU4

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EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.5 apyrase
IUBMB Comments
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.
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Sus scrofa
UNIPROT: Q9MYU4
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The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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a nucleoside 5'-triphosphate
+
2
H2O
=
a nucleoside 5'-phosphate
+
2
phosphate
+
2
=
+
2
Synonyms
apyrase, ecto-atpase, adpase, ntpdase3, atp diphosphohydrolase, entpd1, atpase 2, ecto-apyrase, ectonucleoside triphosphate diphosphohydrolase, atpdase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosine diphosphatase
-
-
-
-
ADPase
-
-
-
-
ATP-diphosphatase
-
-
-
-
ATP-diphosphohydrolase
-
-
-
-
ATPDase
-
-
-
-
CD39 antigen
-
-
-
-
Golgi nucleoside diphosphatase
-
-
-
-
HB6
-
-
-
-
Lymphoid cell activation antigen
-
-
-
-
NTPDase1
-
-
-
-
NTPDase3
-
-
-
-
nucleoside triphosphate diphosphohydrolase-1, NDPDase 1
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-95-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + H2O
AMP + phosphate
show the reaction diagram
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
CDP + H2O
CMP + phosphate
show the reaction diagram
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
GDP + H2O
GMP + phosphate
show the reaction diagram
GTP + 2 H2O
GMP + 2 phosphate
show the reaction diagram
IDP + H2O
IMP + phosphate
show the reaction diagram
-
-
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
show the reaction diagram
TDP + H2O
TMP + phosphate
show the reaction diagram
TTP + 2 H2O
TMP + 2 phosphate
show the reaction diagram
UDP + H2O
UMP + phosphate
show the reaction diagram
UTP + 2 H2O
UMP + 2 phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
additional information
?
-
-
enzyme terminates P2 receptor-mediated signal transmission
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
activation
Zn2+
-
-
additional information
-
no effect: Na+ at 100 mM or K+ at 4 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NaN3
inhibition from 30-70% depending on tissue, inhibition of ADP hydrolysis slightly more pronounced
1-hydroxy-naphthalene-3,6-disulfonic acid
-
-
5'-p-fluorosulfonylbenzoyladenosine
-
50% inhibition at 2 mM
AMP
-
-
Ba2+
-
-
Cibacron blue
-
-
Cu2+
-
-
Ethacrynic acid
-
-
Mg2+
-
-
N3-
-
-
Sodium azide
-
-
suramin
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0056 - 0.1
ADP
0.0031 - 0.1
ATP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
860
ATP
-
pH 7.6, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07 - 0.103
1-hydroxy-naphthalene-3,6-disulfonic acid
2
5'-p-fluorosulfonylbenzoyladenosine
-
-
5 - 12
Sodium azide
1.7 - 1.8
suramin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.3
-
pH 7.6, 37°C, presence of 1.5 mM Cu2+
10.8
-
pH 7.6, 37°C, presence of 5 mM EDTA
13
-
ADP
15.2
-
ATP
19.4
-
pH 7.6, 37°C, presence of 1.5 mM Zn2+
2.4
-
ATP
25.6
-
pH 7.6, 37°C
4.1
-
pH 7.6, 37°C, presence of 1.5 mM Ba2+
69.2
-
ADP
69.4
-
pH 7.6, 37°C, presence of 1.5 mM Ca2+
8.4
-
-
84.2
-
pH 7.6, 37°C, presence of 1.5 mM Mn2+
94.7
-
pH 7.6, 37°C, presence of 1.5 mM Mg2+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 8
-
-
7.6
-
-
8 - 9
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.5
-
50% activity at pH 6, no activity at pH 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 75
-
37-45°C optimum, 75°C no activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
aortic endothelial cells
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
synaptosome from brain cortex
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
ectonucleotidase/ectoenzyme
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ENTP1_PIG
510
2
57757
Swiss-Prot
Secretory Pathway (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57760
calculated from amino-acid composition
65000
-
SDS-PAGE
72000
-
x * 72000, SDS-PAGE
75000
-
highly glycosylated protein, N-linked oligosaccarides, immunoaffinity techniques, SDS-PAGE
78000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 72000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified from liver
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in COS-7 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Laliberte, J.F.; Beaudoin, A.R.
Sequential hydrolysis of the gamma- and beta-phosphate groups of ATP by the ATP diphosphohydrolase from pig pancreas
Biochim. Biophys. Acta
742
9-15
1983
Sus scrofa
Manually annotated by BRENDA team
Laliberte, J.F.; St.Jean, P.; Beaudoin, A.R.
Kinetic effects of Ca2+ and Mg2+ on ATP hydrolysis by the purified ATP diphosphohydrolase
J. Biol. Chem.
257
3869-3874
1982
Sus scrofa
Manually annotated by BRENDA team
LeBel, D.; Poirier, G.G.; Phaneuf, S.; St-Jean, P.; Laliberte, J.F.; Beaudoin, A.R.
Characterization and purification of a calcium-sensitive ATP diphosphohydrolase from pig pancreas
J. Biol. Chem.
255
1227-1233
1980
Sus scrofa
Manually annotated by BRENDA team
Lemmens, R.; Kupers, L.; Sevigny, J.; Beaudoin, A.R.; Grondin, G.; Kittel, A.; Waelkens, E.; Vanduffel, L.
Purification, characterization, and localisation of an ATP diphosphohydrolase in porcine kidney
Am. J. Physiol.
278
978-988
2000
Sus scrofa
-
Manually annotated by BRENDA team
Sevigny, J.; Robson, S.C.; Waelkens, E.; Csizmadia, E.; Smith, R.N.; Lemmens, R.
Identification and characterization of a novel hepatic canalicular ATP diphosphohydrolase
J. Biol. Chem.
275
5640-5647
2000
Sus scrofa
Manually annotated by BRENDA team
Lemmens, R.; Vanduffel, L.; Kittel, A.; Beaudoin, A.R.; Benrezzak, O.; Sevigny, J.
Distribution, cloning, and characterisation of porcine nucleoside triphosphate disphosphohydrolase-1
Eur. J. Biochem.
267
4106-4114
2000
Sus scrofa (Q9MYU4), Sus scrofa
Manually annotated by BRENDA team
Kaczmarek, E.; Koziak, K.; Sevigny, J.; Siegel, J.B.; Anrather, J.; Beaudoin, A.R.; Bach, F.H.; Robson, S.C.
Identification and characterization of CD39/vascular ATP diphosphohydrolase
J. Biol. Chem.
271
33116-33122
1996
Bos taurus, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Kukulski, F.; Komoszynski, M.
Purification and characterization of NTPDase1 (ecto-apyrase) and NTPDase2 (ecto-ATPase) from porcine brain cortex synaptosomes
Eur. J. Biochem.
270
3447-3454
2003
Sus scrofa
Manually annotated by BRENDA team