Information on EC 3.6.1.5 - apyrase and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC3.6.1.5
Word Map on EC 3.6.1.5
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
This record set is specific for:
Homo sapiens


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


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
3.6.1.5
-
RECOMMENDED NAME
GeneOntology No.
apyrase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
UTP and CTP dephosphorylation II
-
-
UTP and CTP dephosphorylation I
-
-
non-pathway related
-
-
pyrimidine metabolism
-
-
Purine metabolism
-
-
Pyrimidine metabolism
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + 2 H2O
adenosine + 2 phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
in the presence of NTPDase2, extracellular ATP is hydrolyzed and converted into ADP. Knocking down NTPDase2 expression using siRNA or inhibiting NTPDases activity with ARL 67156 simultaneously reduces ATP hydrolysis and ADP formation. The amount of generated ADP is proportional to the amount of ATP hydrolyzed in all treatments
-
?
CDP + H2O
CMP + phosphate
show the reaction diagram
CTP + 2 H2O
CMP + 2 phosphate
show the reaction diagram
GDP + H2O
GDP + phosphate
show the reaction diagram
-
35% of the activity with ATP
-
-
?
GDP + H2O
GMP + phosphate
show the reaction diagram
GTP + 2 H2O
GMP + 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 + 2 H2O
uridine + 2 phosphate
show the reaction diagram
-
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
UTP + H2O
UMP + phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + 2 H2O
adenosine + 2 phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
show the reaction diagram
GDP + H2O
GMP + phosphate
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
preferred to Co2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ARL 67156
CDTA
-
-
detergent NP-40
-
at low concentration inhibition of the membrane-bound enzyme, not of the soluble enzyme
dicylcohexylcarbodiimid
-
DCCD, slightly inhibited
EGTA
-
-
fluoride
-
-
NaN3
-
60% inhibition
orthovanadate
p-Chloromercuriphenylsulfonic acid
-
1 mM, 56% of inhibition
p-hydroxymercuribenzoate
-
1 mM, 35% of inhibition
Sodium azide
-
hydrolysis of both ATP and ADP
Sodium fluoride
-
20 mM, 50% residual ATPase activity, 56% residual ADPase activity
suramin
-
0.3 mM, 44% residual ATPase activity, 63% residual ADPase activity
Trifluoperazine
-
0.2 mM, 31% residual ATPase activity, 61% residual ADPase activity
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.107
ADP
-
pH 8.0, 37°C
0.0776
ATP
-
pH 8.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.17
-
recombinant chimeric mutant hu-ck ACR1,5
2.33
-
purified recombinant wild-type enzyme
1020
-
purified recombinant extracellular domain, pH 7.5, in presence of Ca2+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62
-
above, enzyme, recombinant soluble His-tagged secreted NTPDase2 extracellular domain
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 60
-
native full-length enzyme
30 - 62
-
and above, recombinant soluble His-tagged secreted NTPDase2 extracellular domain
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
HaCaT keratinocyte
Manually annotated by BRENDA team
-
mRNA found in this tissue
Manually annotated by BRENDA team
highest expression
Manually annotated by BRENDA team
-
mRNA found in this tissue
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
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
associated with membrane
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60500
-
radiation-inactivation, ADPase
62000
-
x * 62000, recombinant soluble His-tagged secreted NTPDase2 extracellular domain, SDS-PAGE
62700
-
radiation-inactivation, ATPase
64000
-
SDS-PAGE
71000
-
-
78000
-
-
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 62000, recombinant soluble His-tagged secreted NTPDase2 extracellular domain, SDS-PAGE
dimer
-
crosslinking experiments
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivated by Tween 20
-
unstable to detergent Triton X-100
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, octylglucoside, stable
-
4°C, purified recombinant extracellular domain, stable for several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partially
-
recombinant His-tagged soluble NTPDase2 extracellular domain from HEK-293 cells by ammonium sulfate fractionation, ultrafiltration, nickel affinity chromatography, and gel filtration
-
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
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
gene LALP70 cloned into the mammalian expression vector pCl-Neo, expression on the surface of COS-7 cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
C509S
-
148% of wild-type ATPase activity, 155% of wild-type ADPase activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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