3.6.1.5: apyrase
This is an abbreviated version!
For detailed information about apyrase, go to the full flat file.
Word Map on EC 3.6.1.5
-
3.6.1.5
-
platelet
-
purinergic
-
agonist
-
endothelial
-
suramin
-
ntpdases
-
5'-nucleotidase
-
thrombin
-
utp
-
fibrinogen
-
thromboxane
-
salivary
-
blocker
-
ecto-nucleotidases
-
ecto-5\'-nucleotidase
-
purinoceptors
-
platelet-rich
-
aspirin
-
5'-triphosphate
-
ecto-enzymes
-
ouabain
-
ppads
-
oligomycin
-
adp-induced
-
synaptosomes
-
serca2
-
hirudin
-
blood-feeding
-
atp-mediated
-
carbenoxolone
-
tyrode
-
hemichannels
-
alpha,beta-methylene
-
arl
-
pannexins
-
atp-hydrolyzing
-
luciferin-luciferase
-
adenosinergic
-
agriculture
-
e-type
-
phlebotomus
-
analysis
-
pharmacology
-
hematophagous
-
adp-dependent
-
medicine
-
preretinal
-
gel-filtered
-
ap5a
-
aggregometry
-
bzatp
-
drug development
-
ectonucleotide
-
3.1.3.5
-
atpgammas
- 3.6.1.5
- platelet
-
purinergic
- agonist
- endothelial
- suramin
- ntpdases
- 5'-nucleotidase
- thrombin
- utp
- fibrinogen
-
thromboxane
-
salivary
-
blocker
- ecto-nucleotidases
-
ecto-5\'-nucleotidase
-
purinoceptors
-
platelet-rich
- aspirin
- 5'-triphosphate
-
ecto-enzymes
- ouabain
-
ppads
- oligomycin
-
adp-induced
-
synaptosomes
- serca2
- hirudin
-
blood-feeding
-
atp-mediated
- carbenoxolone
-
tyrode
-
hemichannels
-
alpha,beta-methylene
- arl
-
pannexins
-
atp-hydrolyzing
- luciferin-luciferase
-
adenosinergic
- agriculture
-
e-type
- phlebotomus
- analysis
- pharmacology
-
hematophagous
-
adp-dependent
- medicine
-
preretinal
-
gel-filtered
- ap5a
-
aggregometry
-
bzatp
- drug development
-
ectonucleotide
-
3.1.3.5
- atpgammas
Reaction
Synonyms
5' ectonucleotidase, 5'-nucleotidase, adenosine diphosphatase, adenosine pyrophosphatase, adenylpyrophophatase, ADPase, APT102, Apy, Apy 1, Apy 2, APY-1, APY1, APY10, APY2, APY2-type apyrase, APY4, APY5, APY6, APY7, APY8, APY9, Apyrase, apyrase 2, APYRASE2, At1g14230, At1g14240, At1g14250, At2g02970, At3g04080, At5g18280, AtAPY1, AtAPY2, AtAPY3, AtAPY4, AtAPY5, AtAPY6, ATP diphosphohydrolase, ATP diphosphohyrolase, ATP-diphosphatase, ATP-diphosphohydrolase, ATP-diphosphohydrolase 2, ATPase, ATPase 2, ATPDase, ATPDase1, ATPDase2, BjAPY2, Ca2+-activated nucleoside diphosphatase, CApy, CD39, CD39 antigen, CD39-like ATP diphosphohydrolase, CD39L1, Def11, E-NTPDase, E-NTPDase 3, ecto-5'-nucleotidase, ecto-apyrase, ecto-ATP diphosphohydrolase, ecto-ATP-diphosphohydrolase, ecto-ATPase, ecto-ATPDase, ecto-NTPDase, Ecto-NTPDase1, ecto-nucleoside triphosphate diphosphohydrolase, ecto-nucleoside triphosphate diphosphohydrolase 1, ecto-nucleoside triphosphate diphosphohydrolase 2, ecto-nucleoside triphosphate diphosphohydrolase1, ecto-nucleoside triphosphate diphosphohydrolase2, ecto-nucleoside triphosphate diphosphohydrolase3, ecto-nucleoside triphosphate diphosphohydrolase8, ecto-nucleoside triphosphate-diphosphohydrolase, ecto-nucleoside-triphosphate-diphosphohydrolase, ectoapyrase, ectonucleoside triphosphate diphosphohydrolase, ectonucleoside triphosphate diphosphohydrolase 3, ectonucleotidase, ENTPD1, ENTPD2, ENTPD3, Entpd8, ENTPDase1, esctonucleoside triphosphate diphosphohydrolase 1, esctonucleoside triphosphate diphosphohydrolase 2, esctonucleoside triphosphate diphosphohydrolase 8, Golgi nucleoside diphosphatase, GS50, GS52, HB6, hCD39, LALP1, LBRM_15_0030, LicNTPDase-2, LINJ_15_0030, LmjF15.0030, LmNTPDase 1, Lpg1905, lumenal NDPase, Lymphoid cell activation antigen, More, MP67, MpAPY2, NTPase, NTPD1, NTPDase, NTPDase 1, NTPDase 2, NTPDase 3, NTPDase 5, NTPDase 6, NTPDase 8, NTPDase1, NTPDase1/CD39, NTPDase2, NTPDase2/CD39L1, NTPDase3, NTPDase8, nucleoside triphosphatase, nucleoside triphosphate diphosphohydrolase, nucleoside triphosphate diphosphohydrolase 1, nucleoside triphosphate diphosphohydrolase 2, nucleoside triphosphate diphosphohydrolase 8, nucleoside triphosphate diphosphohydrolase-1, NDPDase 1, nucleoside triphosphate diphosphohydrolase-2, nucleoside triphosphate diphosphohydrolase-3, nucleoside triphosphate diphosphohydrolase-8, nucleoside triphosphate disphophohydrolase, nucleoside triphosphate-diphosphohydrolase, nucleotide triphosphate diphosphohydrolase, PeAPY2, potato-specific apyrase, PsAPY1, psNTP9, r-NTPDase 1, r-NTPDase 2, r-NTPDase 3, r-NTPDase 8, Ruviapyrase, SCAN-1, snake venom apyrase, SolCD39/NTPDase1, soluble apyrase, soluble calcium-activated nucleotidase 1, soluble CD39, TaAPY1, TaAPY2, TaAPY3-1, TaAPY3-2, TaAPY3-3, TaAPY3-4, TaAPY5, TaAPY6, TaAPY7, XAPY
ECTree
3.6.1.5 apyraseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.6.1.5 - apyrase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate + H2O
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-phosphate + phosphate
-
-
-
-
?
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate + H2O
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-phosphate + phosphate
-
-
-
-
?
3'(2')-O-(methylanthranoyl)adenosine 5'-diphosphate + H2O
3'(2')-O-(methylanthranoyl)adenosine 5'-phosphate + phosphate
-
-
-
-
?
3'(2')-O-(methylanthranoyl)adenosine 5'-triphosphate + H2O
3'(2')-O-(methylanthranoyl)adenosine 5'-phosphate + phosphate
-
-
-
-
?
4-nitrophenylphosphate + H2O
4-nitrophenol + phosphate
-
low activity
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
23% of activity compared to ATP
-
-
?
adenosine 5'-tetraphosphate + H2O
adenosine 5'-monophosphate + phosphate
-
-
-
-
?
ADP + H2O
?
isoform MP67 demonstrates substantially higher substrate specificity for ADP than for ATP
-
-
?
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate + H2O
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-phosphate + diphosphate
a ribonucleoside 5'-triphosphate + H2O
a ribonucleoside 5'-phosphate + 2 phosphate + 2 H+
-
-
-
?
a ribonucleoside 5'-triphosphate + H2O
a ribonucleoside 5'-phosphate + 2 phosphate + 2 H+
-
-
-
?
ADP + 2 H2O
adenosine + 2 phosphate
-
82.2% activity compared to ATP
-
-
?
ADP + 2 H2O
adenosine + 2 phosphate
-
82.2% activity compared to ATP
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
ADPase activity of GS52 is consistently more than 1.5fold higher than the ATPase activity
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
activity in decreasing order: ADP, IDP, CDP, GDP
-
-
?
AMP + H2O
adenosine + phosphate
-
hydrolysis of extracellular AMP, low activity
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
CG5276 functions as apyrase converting extracellular ATP to ADP and AMP
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
ADPase activity of GS52 is consistently more than 1.5fold higher than the ATPase activity
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
inhibition of platelet aggregation in the placenta
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
ATP is hydrolyzed by NTPDase1 via ADP to AMP, without significant release of ADP
-
-
ir
ATP + 2 H2O
AMP + 2 phosphate
-
slight preference for ATP as substrate
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
highest activity
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
isoform APY2 demonstrates slightly higher substrate specificity for ATP than for ADP
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
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
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
salvage of purine nucleobases in primary urine
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
regulation of extracellular ATP-level
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
ATP and ADP are hydrolyzed equivalently
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
sequential dephosphorylation of ATP to ADP and then AMP
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
sequential dephosphorylation of ATP to ADP and then AMP
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
ATP-diphosphohydrolase releases ADP during the catalytic cycle, mechanism of ATP hydrolysis, overview
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
activity in decreasing order: ATP, CTP, GTP, UTP, ITP
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
high activity
-
-
?
ATP + H2O
ADP + phosphate
-
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
-
?
ATP + H2O
ADP + phosphate
ATP incubated with NTPDase2 is readily converted into ADP, but very poorly into AMP
-
-
?
ATP + H2O
ADP + phosphate
ATP incubated with NTPDase2 is readily converted into ADP, but very poorly into AMP
-
-
?
CDP + H2O
CMP + phosphate
best substrate
-
-
?
CDP + H2O
CMP + phosphate
activity in decreasing order: ADP, IDP, CDP, GDP
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
two steps, very low activity with CDP
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
UTP, GTP and CTP are preferred substrates
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
activity in decreasing order: ATP, CTP, GTP, UTP, ITP
-
-
?
CTP + H2O
CDP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
activity in decreasing order: ADP, IDP, CDP, GDP
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
20.7% activity compared to ATP
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
UTP, GTP and CTP are preferred substrates
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
activity in decreasing order: ATP, CTP, GTP, UTP, ITP
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
best substrate
-
-
?
IDP + H2O
IMP + phosphate
activity in decreasing order: ADP, IDP, CDP, GDP
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
-
70.7% activity compared to ATP
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
activity in decreasing order: ATP, CTP, GTP, UTP, ITP
-
-
?
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate + H2O
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-phosphate + diphosphate
developement of a selective and highly sensitive capillary electrophoresis (CE) assay using a fluorescent CD39 substrate, a fluorescein-labelled ATP, i.e. N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate that is converted to its AMP derivative (N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-phosphate). To accelerate the assays, a two-directional (forward and reverse) CE system is implemented using 96-well plates, which is suitable for the screening of compound libraries. Achievement of a large enhancement in sensitivity as compared to previous methods (e.g. malachite-green assay: 1000000fold, CE-UV assay: 500000fold, fluorescence polarization immunoassay: 12500fold). The assay is validated by performing inhibition assays with several standard CD39 inhibitors. N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate is preferably hydrolyzed by CD39 as compared to other ectonucleotidases
-
-
ir
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate + H2O
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-phosphate + diphosphate
i.e. PSB-170621A, developement of a selective and highly sensitive capillary electrophoresis (CE) assay using a fluorescent CD39 substrate, a fluorescein-labelled ATP, i.e. N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate that is converted to its AMP derivative (N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-phosphate). To accelerate the assays, a two-directional (forward and reverse) CE system is implemented using 96-well plates, which is suitable for the screening of compound libraries. Achievement of a large enhancement in sensitivity as compared to previous methods (e.g. malachite-green assay: 1000000fold, CE-UV assay: 500000fold, fluorescence polarization immunoassay: 12500fold). The assay is validated by performing inhibition assays with several standard CD39 inhibitors. N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate is preferably hydrolyzed by CD39 as compared to other ectonucleotidases
-
-
ir
UDP + H2O
UMP + phosphate
very low activity with UDP
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
43.3% activity compared to ATP
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
UTP, GTP and CTP are preferred substrates
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
150% of activity compared to ATP
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
activity in decreasing order: ATP, CTP, GTP, UTP, ITP
-
-
?
UTP + H2O
UDP + phosphate
-
-
-
?
additional information
?
-
-
enzyme inhibits ADP-, collagen-, and thrombin-induced human platelet aggregation in dose-dependent manner
-
-
?
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
?
-
apyrases hydrolyze the phosphodiester bonds of nucleoside tri- and diphosphates to orthophosphate and mononucleodides
-
-
?
additional information
?
-
-
apyrases hydrolyze the phosphodiester bonds of nucleoside tri- and diphosphates to orthophosphate and mononucleodides
-
-
?
additional information
?
-
ATP, ADP, and AMP as well as ITP, UTP, CTP, GTP, TTP, and TDP are not hydrolyzed
-
-
?
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY1 exhibits a clear preference towards substrate UDP , supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY1 exhibits a clear preference towards substrate UDP , supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY1 exhibits a clear preference towards substrate UDP , supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY1 exhibits a clear preference towards substrate UDP , supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY1 exhibits a clear preference towards substrate UDP , supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY1 exhibits a clear preference towards substrate UDP , supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY2 exhibits a clear preference towards the substrate UDP/GDP, supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY2 exhibits a clear preference towards the substrate UDP/GDP, supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY2 exhibits a clear preference towards the substrate UDP/GDP, supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY2 exhibits a clear preference towards the substrate UDP/GDP, supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY2 exhibits a clear preference towards the substrate UDP/GDP, supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
isozymes AtAPY1 and AtAPY2 appear to have a substrate preference for NDPs. AtAPY2 exhibits a clear preference towards the substrate UDP/GDP, supporting previous reports indicating that it functions as UDP/GDPase, see also EC 3.6.1.6
-
-
-
additional information
?
-
no significant NTPase or NDPase activity is detected for AtAPY4 except for a slight affinity for CTP. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
-
-
-
additional information
?
-
no significant NTPase or NDPase activity is detected for AtAPY4 except for a slight affinity for CTP. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
-
-
-
additional information
?
-
no significant NTPase or NDPase activity is detected for AtAPY4 except for a slight affinity for CTP. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
-
-
-
additional information
?
-
no significant NTPase or NDPase activity is detected for AtAPY4 except for a slight affinity for CTP. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
-
-
-
additional information
?
-
no significant NTPase or NDPase activity is detected for AtAPY4 except for a slight affinity for CTP. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
-
-
-
additional information
?
-
no significant NTPase or NDPase activity is detected for AtAPY4 except for a slight affinity for CTP. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
-
-
-
additional information
?
-
the clade II member AtAPY3 has a strong preference toward NTPs but also has significant activities toward ADP and GDP. No activity with CDP, CMP, and GMP
-
-
-
additional information
?
-
the clade II member AtAPY3 has a strong preference toward NTPs but also has significant activities toward ADP and GDP. No activity with CDP, CMP, and GMP
-
-
-
additional information
?
-
the clade II member AtAPY3 has a strong preference toward NTPs but also has significant activities toward ADP and GDP. No activity with CDP, CMP, and GMP
-
-
-
additional information
?
-
the clade II member AtAPY3 has a strong preference toward NTPs but also has significant activities toward ADP and GDP. No activity with CDP, CMP, and GMP
-
-
-
additional information
?
-
the clade II member AtAPY3 has a strong preference toward NTPs but also has significant activities toward ADP and GDP. No activity with CDP, CMP, and GMP
-
-
-
additional information
?
-
the clade II member AtAPY3 has a strong preference toward NTPs but also has significant activities toward ADP and GDP. No activity with CDP, CMP, and GMP
-
-
-
additional information
?
-
the clade II member AtAPY6 significantly prefers NDPs but also has significant activities toward NTPs. No activity with CMP and GMP. Broad substrate specificity
-
-
-
additional information
?
-
the clade II member AtAPY6 significantly prefers NDPs but also has significant activities toward NTPs. No activity with CMP and GMP. Broad substrate specificity
-
-
-
additional information
?
-
the clade II member AtAPY6 significantly prefers NDPs but also has significant activities toward NTPs. No activity with CMP and GMP. Broad substrate specificity
-
-
-
additional information
?
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the clade II member AtAPY6 significantly prefers NDPs but also has significant activities toward NTPs. No activity with CMP and GMP. Broad substrate specificity
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additional information
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the clade II member AtAPY6 significantly prefers NDPs but also has significant activities toward NTPs. No activity with CMP and GMP. Broad substrate specificity
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additional information
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the clade II member AtAPY6 significantly prefers NDPs but also has significant activities toward NTPs. No activity with CMP and GMP. Broad substrate specificity
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additional information
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the enzyme acts in a multienzyme complex transforming ATP into adenosine without accumulation of intermediates
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UDP and GDP, rather than ADP or ATP, are the preferred substrates of CApy
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UDP and GDP, rather than ADP or ATP, are the preferred substrates of CApy
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Ruviapyrase does not show cytotoxicity against breast cancer (MCF-7) cells and haemolytic activity, it exhibits marginal anticoagulant and strong antiplatelet activity, and dose-dependently reverses the ADP-induced platelet aggregation. The catalytic activity and platelet deaggregation property of Ruviapyrase is significantly inhibited by EDTA, DTT and IAA, and neutralized by commercial monovalent and polyvalent antivenom
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Ruviapyrase hydrolysed adenosine triphosphate (ATP) to a significantly greater extent as compared to adenosine diphosphate (ADP). The enzyme is devoid of 5'-nucleotidase and phosphodiesterase activities. The specificity constant or kinetic efficiency of Ruviapyrase in hydrolysing ATP is 3.7folds higher compared to hydrolysis of ADP under identical experimental conditions
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additional information
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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
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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
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only one enzymatic site is responsible for hydrolysis of both ATP and ADP
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additional information
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development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrat, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview
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additional information
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development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrat, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview
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additional information
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development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrat, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview
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additional information
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development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrat, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview
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additional information
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isozymes NTPDase2 hydrolyzes ATP to ADP, which is released from the enzyme. NTPDase2 shows much higher preference for ATP over ADP, and therefore produces ADP as its main product. Development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrat, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview
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additional information
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isozymes NTPDase2 hydrolyzes ATP to ADP, which is released from the enzyme. NTPDase2 shows much higher preference for ATP over ADP, and therefore produces ADP as its main product. Development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrat, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview
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additional information
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isozymes NTPDase2 hydrolyzes ATP to ADP, which is released from the enzyme. NTPDase2 shows much higher preference for ATP over ADP, and therefore produces ADP as its main product. Development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrat, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview
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additional information
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isozymes NTPDase2 hydrolyzes ATP to ADP, which is released from the enzyme. NTPDase2 shows much higher preference for ATP over ADP, and therefore produces ADP as its main product. Development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrat, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview
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additional information
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isozymes NTPDase3 and -8 hydrolyze ATP to ADP, which is released from the enzyme, and ADP is subsequently hydrolyzed to AMP. Development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrat, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview
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additional information
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isozymes NTPDase3 and -8 hydrolyze ATP to ADP, which is released from the enzyme, and ADP is subsequently hydrolyzed to AMP. Development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrat, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview
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additional information
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isozymes NTPDase3 and -8 hydrolyze ATP to ADP, which is released from the enzyme, and ADP is subsequently hydrolyzed to AMP. Development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrat, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview
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additional information
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isozymes NTPDase3 and -8 hydrolyze ATP to ADP, which is released from the enzyme, and ADP is subsequently hydrolyzed to AMP. Development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrat, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview
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additional information
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isozymes NTPDase3 and -8 hydrolyze ATP to ADP, which is released from the enzyme, and ADP is subsequently hydrolyzed to AMP. Development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrate, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview
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additional information
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isozymes NTPDase3 and -8 hydrolyze ATP to ADP, which is released from the enzyme, and ADP is subsequently hydrolyzed to AMP. Development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrate, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview
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additional information
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isozymes NTPDase3 and -8 hydrolyze ATP to ADP, which is released from the enzyme, and ADP is subsequently hydrolyzed to AMP. Development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrate, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview
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additional information
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isozymes NTPDase3 and -8 hydrolyze ATP to ADP, which is released from the enzyme, and ADP is subsequently hydrolyzed to AMP. Development of a sensitive, reproducible method, a fluorescence polarization immunoassay, which allows the detection of NTPDase activity with its natural substrate, with fluorescence polarization (FP) readout. The methodology is generally applicable for ADP-, AMP- or GMP-producing enzymes. It enables the direct detection of the enzymatic reaction product ADP when using ATP as a substrate (for NTPDase2, NTPDase3, and NTPDase8) or of AMP upon using ADP as a substrate (for NTPDase1), evaluation and validation, overview
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additional information
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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
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additional information
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the enzyme shows the ability to hydrolyze nucleoside tri- and diphosphates, but has limited activity against CTP, CDP, UTP, and UDP
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additional information
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the purified MP67 shows extremely high substrate specificity toward ADP in the presence of Ca2+
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the purified MP67 shows extremely high substrate specificity toward ADP in the presence of Ca2+
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the recombinant MpAPY2 hydrolyzes ATP and ADP to the same extent
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the recombinant MpAPY2 hydrolyzes ATP and ADP to the same extent
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enzyme abrogates platelet aggregation and recruitment in intact vessels
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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
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additional information
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substrate specificity in myofibroblasts and quiescent-like hepatic stellate cells, overview
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additional information
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adenine nucleotides are the best substrates. The other nucleotides (GTP, UTP, GDP, and UDP) are also hydrolyzed when added to the reaction instead of ATP or ADP, which demonstrates a broad substrate specificity for E-NTPDase expressed on the surface of peritoneal cavity cells
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adenine nucleotides are the best substrates. The other nucleotides (GTP, UTP, GDP, and UDP) are also hydrolyzed when added to the reaction instead of ATP or ADP, which demonstrates a broad substrate specificity for E-NTPDase expressed on the surface of peritoneal cavity cells
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additional information
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adenine nucleotides are the best substrates. The other nucleotides (GTP, UTP, GDP, and UDP) are also hydrolyzed when added to the reaction instead of ATP or ADP, which demonstrates a broad substrate specificity for E-NTPDase expressed on the surface of peritoneal cavity cells
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salivary apyrases are nucleotide-metabolising enzymes that blood-feeding parasites utilise for modulation of extracellular nucleotides to prevent platelet activation and aggregation
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additional information
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salivary apyrases are nucleotide-metabolising enzymes that blood-feeding parasites utilise for modulation of extracellular nucleotides to prevent platelet activation and aggregation
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additional information
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salivary apyrases are nucleotide-metabolising enzymes that blood-feeding parasites utilise for modulation of extracellular nucleotides to prevent platelet activation and aggregation
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additional information
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released inorganic phosphate is measured using the malachite green method
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additional information
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the enzyme does not hydrolyze AMP, GDP, CDP or UDP
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additional information
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the enzyme does not hydrolyze AMP, GDP, CDP or UDP
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additional information
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the enzyme does not hydrolyze AMP, GDP, CDP or UDP
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relative efficacy for substrate in decreasing order: CTP, ADP, UTP, TTP, GTP, ATP
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additional information
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both ATP and ADP hydrolysis occur at the same active site of enzyme
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enzyme is involved in regulating ATP signaling associated primarily with auditory neurotransmission
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establishment of a kinetic isothermal titration calorimetry assay. Substrate recognition by NTPDase1, overview
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additional information
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production of inorganic phosphate is measured using the malachite green method
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ATPDase2 plays a non-redundant role in the parasite-host interplay
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ATPDase2 plays a non-redundant role in the parasite-host interplay
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introduction of large groups in the ribose does not produce steric hindrance in substrate binding, but causes a reduction in kcat-value
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apyrases hydrolyze nucleoside triphosphates and diphosphates
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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
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additional information
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optimization of a luminescence-based high-throughput screening assay for detecting apyrase activity, overview
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phosphate release is measured using the malachite green method
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enzyme terminates P2 receptor-mediated signal transmission
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the enzyme hydrolyzes purine and pyrimidine nucleoside 5'-di- and 5'-triphosphates, substrate specificity and competition, overview
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the activity of NTPDase for substrate ATP is superior to ADP. For the hydrolysis of ATP, a decreasing curve is observed, since increased concentration of substrate consequently reduces NTPDase activity. The opposite occurs with the hydrolysis of ADP, since increases in NTPDase activity are directly proportional to the elevation of substrate in the reaction
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additional information
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the activity of NTPDase for substrate ATP is superior to ADP. For the hydrolysis of ATP, a decreasing curve is observed, since increased concentration of substrate consequently reduces NTPDase activity. The opposite occurs with the hydrolysis of ADP, since increases in NTPDase activity are directly proportional to the elevation of substrate in the reaction
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enzyme inhibits ADP-induced human platelet aggregation
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enzyme inhibits ADP-induced human platelet aggregation
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no substrate: nucleoside 5-monophosphates, glycerol phosphate, glycose 6-phosphate, UDP-galactose
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additional information
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no substrate: nucleoside 5-monophosphates, glycerol phosphate, glycose 6-phosphate, UDP-galactose
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APY3-1 exhibits slightly lower enzymatic activity when degrading the ADP compared with ATP, but has very low activity during the degradation of TTP, GTP, and CTP, suggesting that TaAPY3-1 has a high substrate specificity
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additional information
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the enzyme plays a role in the salvage of purines from the extracellular medium in the organism
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additional information
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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
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additional information
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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
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