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1,N6-etheno-ADP + H2O
1,N6-etheno-AMP + phosphate
-
-
-
-
?
1,N6-etheno-ATP + H2O
1,N6-etheno-AMP + phosphate
-
-
-
-
?
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-nitrophenyl thymidine 5'-phosphate + H2O
4-nitrophenol + TMP
-
-
-
-
?
4-nitrophenylphosphate + H2O
4-nitrophenol + phosphate
-
low activity
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
23% of activity compared to ATP
-
-
?
8-oxo-dGTP + 2 H2O
8-oxo-dGMP + 2 phosphate
-
-
-
-
?
a ribonucleoside 5'-triphosphate + H2O
a ribonucleoside 5'-phosphate + 2 phosphate + 2 H+
adenosine (5')-tetraphospho-(5')-adenosine + H2O
?
-
-
-
-
?
adenosine 5'-tetraphosphate + H2O
adenosine 5'-monophosphate + phosphate
-
-
-
-
?
adenosine 5'-[(alpha,beta)-methyleno] triphosphate + H2O
?
-
-
-
?
ADP + 2 H2O
adenosine + 2 phosphate
ADP + H2O
?
isoform MP67 demonstrates substantially higher substrate specificity for ADP than for ATP
-
-
?
ADP + H2O
AMP + phosphate
ADP-ribose + H2O
?
-
-
-
-
?
AMP + H2O
adenosine + phosphate
AMPCPP + H2O
?
low activity
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
ATP + H2O
ADP + phosphate
CDP + H2O
CMP + phosphate
CTP + 2 H2O
CMP + 2 phosphate
CTP + H2O
CDP + phosphate
dATP + 2 H2O
dAMP + 2 phosphate
-
-
-
-
?
dATP + H2O
dAMP + phosphate
-
-
-
-
?
dATP + H2O
dAMP + phosphate + H+
-
-
-
-
?
dCTP + 2 H2O
dCMP + 2 phosphate
-
-
-
-
?
dCTP + H2O
dCMP + phosphate + H+
-
-
-
-
?
dGTP + 2 H2O
dGMP + 2 phosphate
-
-
-
-
?
dGTP + H2O
dGMP + phosphate + H+
-
-
-
-
?
diphosphate + H2O
2 phosphate
-
low activity
-
-
?
dTTP + H2O
dTMP + phosphate
-
-
-
-
?
dTTP + H2O
dTMP + phosphate + H+
-
-
-
-
?
dUTP + H2O
dUMP + phosphate + H+
-
-
-
-
?
GDP + H2O
GMP + phosphate
GTP + 2 H2O
GMP + 2 phosphate
GTP + H2O
GDP + phosphate
IDP + H2O
IMP + phosphate
ITP + 2 H2O
IMP + 2 phosphate
ITP + H2O
IDP + phosphate
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
oligophosphates + H2O
?
-
n = 3, 15, 40, 60
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
-
-
-
?
TDP + H2O
TMP + phosphate
tetraamine(imidodiphosphato)cobalt + H2O
?
-
-
-
-
?
thiamine diphosphate + 2 H2O
thiamine + 2 phosphate
-
-
-
-
?
thio-dATP + H2O
thio-dAMP + phosphate
-
-
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
TTP + H2O
TDP + phosphate
-
low activity
-
-
?
UDP + 2 H2O
uridine + 2 phosphate
UDP + H2O
?
best substrate
-
-
?
UDP + H2O
UMP + phosphate
UDP-glucose + H2O
?
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
UTP + H2O
UDP + phosphate
additional information
?
-
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 + 2 H2O
adenosine + 2 phosphate
-
-
-
-
?
ADP + 2 H2O
adenosine + 2 phosphate
-
-
-
-
?
ADP + 2 H2O
adenosine + 2 phosphate
-
-
-
-
?
ADP + 2 H2O
adenosine + 2 phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
maximum activity at 7 mM
-
-
?
ADP + H2O
AMP + phosphate
-
about 90% relative activity of ATP
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
high activity
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
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
-
67% of activity compared to ATP
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
very low activity
-
-
?
ADP + H2O
AMP + phosphate
-
97% of the activity with ATP
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
104% of activity compared to ATP
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
Orchopeas howardi
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
Oropsylla bacchi
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
210151, 210158, 210160, 210161, 210163, 210166, 654862, 656682, 656685, 656869, 664550 -
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
as CaADP- only
-
-
?
ADP + H2O
AMP + phosphate
-
87% relative activity compared to ATP
-
-
?
ADP + H2O
AMP + phosphate
-
ATP and ADP are hydrolyzed equivalently
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
68% activity compared to ATP
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
71% of activity compared to ATP
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
activity in decreasing order: ADP, IDP, CDP, GDP
-
-
?
ADP + H2O
AMP + phosphate
-
119% of activity compared to ATP
-
-
?
ADP + H2O
AMP + phosphate
Triticosecale Wittmack
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
hydrolysis of extracellular ADP
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
?
ADP + H2O
AMP + phosphate
-
37.7% of the activity with ATP
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
ADP + H2O
AMP + phosphate
-
-
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
-
?
AMP + H2O
adenosine + phosphate
-
very low activity
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
-
?
AMP + H2O
adenosine + phosphate
-
low activity
-
-
?
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
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
maximum activity at 8 mM
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
inhibition of platelet aggregation
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
high activity
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
100% activity
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
100% activity
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
best substrate
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
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
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
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
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
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
-
regulation of extracellular ATP-level
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
overall reaction
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
overall reaction
-
-
?
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
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
slight preference for ATP as substrate
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
highest activity
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
highest activity
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
isoform APY2 demonstrates slightly higher substrate specificity for ATP than for ADP
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
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
-
best substrate in hepatic stellate cells
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
Orchopeas howardi
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
Orchopeas howardi
-
inhibition of platelet aggregation
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
Oropsylla bacchi
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
better substrate then ADP
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
overall reaction
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
overall reaction
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
210134, 210151, 210158, 210160, 210161, 210163, 210166, 654862, 656682, 656685, 656869, 664550 -
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
as CaATP2- only
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
100% relative activity
-
-
?
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
-
-
-
?
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
-
-
-
-
ir
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
100% activity
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
overall reaction
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
ir
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
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
activity in decreasing order: ATP, CTP, GTP, UTP, ITP
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
Triticosecale Wittmack
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
inhibition of platelet aggregation
-
-
?
ATP + 2 H2O
AMP + 2 phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
high activity
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
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 + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
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
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
hydrolysis of extracellular ATP
-
-
?
CDP + H2O
CMP + phosphate
best substrate
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
-
?
CDP + H2O
CMP + phosphate
-
high enzyme activity by hLALP70v
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
-
?
CDP + H2O
CMP + phosphate
-
lowest relative activity with 61%
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
-
?
CDP + H2O
CMP + phosphate
-
3.34% activity compared to ATP
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
-
?
CDP + H2O
CMP + phosphate
-
42% of activity compared to ATP
-
-
?
CDP + H2O
CMP + phosphate
-
-
-
-
?
CDP + H2O
CMP + phosphate
activity in decreasing order: ADP, IDP, CDP, GDP
-
-
?
CDP-choline + H2O
?
-
-
-
-
?
CDP-choline + H2O
?
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
two steps, very low activity with CDP
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
15.9% activity compared to ATP
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
highest enzyme activity by hLALP70v
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
UTP, GTP and CTP are preferred substrates
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
60% of activity compared to ATP
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
better substrate then ATP
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
-
-
-
ir
CTP + 2 H2O
CMP + 2 phosphate
-
12.5% activity compared to ATP
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
87% of activity compared to ATP
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
-
-
-
-
?
CTP + 2 H2O
CMP + 2 phosphate
activity in decreasing order: ATP, CTP, GTP, UTP, ITP
-
-
?
CTP + H2O
CDP + phosphate
-
-
-
?
CTP + H2O
CDP + phosphate
-
-
-
-
?
CTP + H2O
CDP + phosphate
-
-
-
-
?
CTP + H2O
CDP + phosphate
-
17.4% of the activity with ATP
-
-
?
FAD + H2O
?
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
high activity
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
best substrate
-
-
?
GDP + H2O
GMP + phosphate
-
35% of the activity with ATP
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
ir
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
69.2% activity compared to ATP
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
-
61% of activity compared to ATP
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
-
?
GDP + H2O
GMP + phosphate
activity in decreasing order: ADP, IDP, CDP, GDP
-
-
?
GDP + H2O
GMP + phosphate
-
-
-
?
GDP-mannose + H2O
?
-
-
-
-
?
GDP-mannose + H2O
?
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
comparative hydrolysis to ATP
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
20.7% activity compared to ATP
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
20.7% activity compared to ATP
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
hLALP70v
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
37% of the activity with ATP
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
UTP, GTP and CTP are preferred substrates
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
23% of activity compared to ATP
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
better substrate than UTP
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
best substrate
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
ir
GTP + 2 H2O
GMP + 2 phosphate
-
84.6% activity compared to ATP
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
91% of activity compared to ATP
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
-
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
activity in decreasing order: ATP, CTP, GTP, UTP, ITP
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
best substrate
-
-
?
GTP + 2 H2O
GMP + 2 phosphate
-
51.4% of the activity with ATP
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
best substrate
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
ir
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
-
?
IDP + H2O
IMP + phosphate
-
comparative hydrolysis to ADP
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
-
?
IDP + H2O
IMP + phosphate
-
-
-
-
?
IDP + H2O
IMP + phosphate
activity in decreasing order: ADP, IDP, CDP, GDP
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
-
-
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
-
comparative hydrolysis to ATP
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
-
70.7% activity compared to ATP
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
-
70.7% activity compared to ATP
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
-
-
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
-
-
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
-
-
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
-
-
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
-
-
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
-
-
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
-
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
-
-
-
-
ir
ITP + 2 H2O
IMP + 2 phosphate
-
-
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
-
78% of activity compared to ATP
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
activity in decreasing order: ATP, CTP, GTP, UTP, ITP
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
-
109% of activity compared to ATP
-
-
?
ITP + 2 H2O
IMP + 2 phosphate
-
84.8% of the activity with ATP
-
-
?
ITP + H2O
IDP + phosphate
-
-
-
?
ITP + H2O
IDP + phosphate
-
best substrate
-
-
?
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
TDP + H2O
TMP + phosphate
-
-
-
-
?
TDP + H2O
TMP + phosphate
-
-
-
?
TDP + H2O
TMP + phosphate
-
-
-
-
?
TDP + H2O
TMP + phosphate
-
44% of activity compared to ATP
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
-
-
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
-
high enzyme activity by hLALP70
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
-
-
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
-
better substrate then CTP
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
-
-
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
weak substrate
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
-
-
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
-
82% of activity compared to ATP
-
-
?
TTP + 2 H2O
TMP + 2 phosphate
-
-
-
-
?
UDP + 2 H2O
uridine + 2 phosphate
-
-
-
-
?
UDP + 2 H2O
uridine + 2 phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
very low activity with UDP
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
31% of activity compared to ATP
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
hLALP70v
-
-
?
UDP + H2O
UMP + phosphate
-
18% of the activity with ATP
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
-
best substrate in myofibroblasts
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
6.8% activity compared to ATP
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
-
?
UDP + H2O
UMP + phosphate
-
56% of activity compared to ATP
-
-
?
UDP + H2O
UMP + phosphate
-
104% of activity compared to ATP
-
-
?
UDP + H2O
UMP + phosphate
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
43.3% activity compared to ATP
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
43.3% activity compared to ATP
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
25% of activity compared to ATP
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
highest enzyme activity by hLALP70
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
40% of the activity with ATP
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
UTP, GTP and CTP are preferred substrates
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
150% of activity compared to ATP
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
better substrate then TTP
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
overall reaction
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
best substrate
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
ir
UTP + 2 H2O
UMP + 2 phosphate
-
28.2% activity compared to ATP
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
94% of activity compared to ATP
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
activity in decreasing order: ATP, CTP, GTP, UTP, ITP
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
-
25.2% of the activity with ATP
-
-
?
UTP + H2O
UDP + phosphate
-
-
-
?
UTP + H2O
UDP + phosphate
-
-
-
?
UTP + H2O
UDP + phosphate
-
-
-
?
UTP + H2O
UDP + phosphate
-
-
-
-
?
UTP + H2O
UDP + phosphate
-
-
-
?
UTP + H2O
UDP + phosphate
-
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additional information
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enzyme inhibits ADP-, collagen-, and thrombin-induced human platelet aggregation in dose-dependent manner
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additional information
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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
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?
additional information
?
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apyrases hydrolyze the phosphodiester bonds of nucleoside tri- and diphosphates to orthophosphate and mononucleodides
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?
additional information
?
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apyrases hydrolyze the phosphodiester bonds of nucleoside tri- and diphosphates to orthophosphate and mononucleodides
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?
additional information
?
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ATP, ADP, and AMP as well as ITP, UTP, CTP, GTP, TTP, and TDP are not hydrolyzed
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?
additional information
?
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no substrate: ADP
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?
additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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-
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additional information
?
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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
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-
-
additional information
?
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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
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-
-
additional information
?
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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
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-
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additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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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
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additional information
?
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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)
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additional information
?
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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)
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additional information
?
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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)
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additional information
?
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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)
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additional information
?
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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)
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additional information
?
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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)
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additional information
?
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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
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-
-
additional information
?
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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
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-
-
additional information
?
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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
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-
-
additional information
?
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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
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-
-
additional information
?
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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
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-
-
additional information
?
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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
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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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-
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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 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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no hydrolysis of GMP, UMP
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?
additional information
?
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neglible hydrolysis of AMP
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?
additional information
?
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neglible hydrolysis of AMP
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?
additional information
?
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neglible hydrolysis of AMP
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?
additional information
?
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neglible hydrolysis of AMP
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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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?
additional information
?
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neglible hydrolysis of AMP
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?
additional information
?
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neglible hydrolysis of AMP
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?
additional information
?
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neglible hydrolysis of AMP
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?
additional information
?
-
UDP and GDP, rather than ADP or ATP, are the preferred substrates of CApy
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?
additional information
?
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UDP and GDP, rather than ADP or ATP, are the preferred substrates of CApy
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?
additional information
?
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neglible hydrolysis of AMP
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?
additional information
?
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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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additional information
?
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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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?
additional information
?
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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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?
additional information
?
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no substrate: CTP, CDP, GTP, GDP
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-
?
additional information
?
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neglible hydrolysis of AMP
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?
additional information
?
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neglible hydrolysis of AMP
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?
additional information
?
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neglible hydrolysis of AMP
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?
additional information
?
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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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APY-1 has also NDPase activity
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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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
?
-
-
neglible hydrolysis of AMP
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-
?
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
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?
additional information
?
-
-
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
?
-
-
the purified MP67 shows extremely high substrate specificity toward ADP in the presence of Ca2+
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-
?
additional information
?
-
the purified MP67 shows extremely high substrate specificity toward ADP in the presence of Ca2+
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-
?
additional information
?
-
-
the recombinant MpAPY2 hydrolyzes ATP and ADP to the same extent
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-
?
additional information
?
-
the recombinant MpAPY2 hydrolyzes ATP and ADP to the same extent
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-
?
additional information
?
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no substrate: AMP
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-
?
additional information
?
-
-
no substrate: AMP
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-
?
additional information
?
-
-
enzyme abrogates platelet aggregation and recruitment in intact vessels
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?
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
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-
?
additional information
?
-
-
substrate specificity in myofibroblasts and quiescent-like hepatic stellate cells, overview
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-
?
additional information
?
-
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
?
-
-
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
?
-
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
-
-
-
additional information
?
-
-
neglible hydrolysis of AMP
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-
?
additional information
?
-
Orchopeas howardi
-
neglible hydrolysis of AMP
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-
?
additional information
?
-
-
neglible hydrolysis of AMP
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-
?
additional information
?
-
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
?
-
salivary apyrases are nucleotide-metabolising enzymes that blood-feeding parasites utilise for modulation of extracellular nucleotides to prevent platelet activation and aggregation
-
-
?
additional information
?
-
-
salivary apyrases are nucleotide-metabolising enzymes that blood-feeding parasites utilise for modulation of extracellular nucleotides to prevent platelet activation and aggregation
-
-
?
additional information
?
-
Oropsylla bacchi
-
neglible hydrolysis of AMP
-
-
?
additional information
?
-
-
released inorganic phosphate is measured using the malachite green method
-
-
-
additional information
?
-
the enzyme does not hydrolyze AMP, GDP, CDP or UDP
-
-
?
additional information
?
-
the enzyme does not hydrolyze AMP, GDP, CDP or UDP
-
-
?
additional information
?
-
-
the enzyme does not hydrolyze AMP, GDP, CDP or UDP
-
-
?
additional information
?
-
-
neglible hydrolysis of AMP
-
-
?
additional information
?
-
-
neglible hydrolysis of AMP
-
-
?
additional information
?
-
-
relative efficacy for substrate in decreasing order: CTP, ADP, UTP, TTP, GTP, ATP
-
-
?
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
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-
?
additional information
?
-
-
both ATP and ADP hydrolysis occur at the same active site of enzyme
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-
?
additional information
?
-
-
enzyme is involved in regulating ATP signaling associated primarily with auditory neurotransmission
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-
?
additional information
?
-
establishment of a kinetic isothermal titration calorimetry assay. Substrate recognition by NTPDase1, overview
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-
?
additional information
?
-
no hydrolysis of AMPCP
-
-
?
additional information
?
-
production of inorganic phosphate is measured using the malachite green method
-
-
-
additional information
?
-
-
neglible hydrolysis of AMP
-
-
?
additional information
?
-
-
neglible hydrolysis of AMP
-
-
?
additional information
?
-
-
ATPDase2 plays a non-redundant role in the parasite-host interplay
-
-
?
additional information
?
-
ATPDase2 plays a non-redundant role in the parasite-host interplay
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-
?
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
?
-
-
introduction of large groups in the ribose does not produce steric hindrance in substrate binding, but causes a reduction in kcat-value
-
-
?
additional information
?
-
-
apyrases hydrolyze nucleoside triphosphates and diphosphates
-
-
?
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
?
-
-
optimization of a luminescence-based high-throughput screening assay for detecting apyrase activity, overview
-
-
-
additional information
?
-
-
phosphate release is measured using the malachite green method
-
-
-
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
?
-
-
enzyme terminates P2 receptor-mediated signal transmission
-
-
?
additional information
?
-
-
the enzyme hydrolyzes purine and pyrimidine nucleoside 5'-di- and 5'-triphosphates, substrate specificity and competition, overview
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
enzyme inhibits ADP-induced human platelet aggregation
-
-
?
additional information
?
-
enzyme inhibits ADP-induced human platelet aggregation
-
-
?
additional information
?
-
-
no substrate: nucleoside 5-monophosphates, glycerol phosphate, glycose 6-phosphate, UDP-galactose
-
-
?
additional information
?
-
no substrate: nucleoside 5-monophosphates, glycerol phosphate, glycose 6-phosphate, UDP-galactose
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme plays a role in the salvage of purines from the extracellular medium in the organism
-
-
?
additional information
?
-
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
?
-
-
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
?
-
-
neglible hydrolysis of AMP
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cl-
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
MgCl2
-
5 mM, stimulation up to 20fold, best activating kation
MnCl2
-
5 mM, stimulation up to 10fold
ZnCl2
-
5 mM, stimulation
Ca2+
-
-
Ca2+
1 mM, about 3fold stimulation. Ca2+ and Mn2+ are best activators
Ca2+
-
either Mg2+ or Ca2+ required for activity
Ca2+
-
ADP and UDP hydrolysis either from non-galled or globose gall tissues are 10-38% stimulated by 5 mM Ca2+
Ca2+
-
either Mg2+ or Ca2+ required for activity
Ca2+
-
either Mg2+ or Ca2+ required for activity
Ca2+
-
required for activity
Ca2+
-
Ca2+ preferred to Mg2+
Ca2+
-
about 30% of the activity with Mg2+, at 5 mM and pH 7.4
Ca2+
-
the most effective activating divalent cation
Ca2+
absolute requirement
Ca2+
-
either Mg2+ or Ca2+ required for activity
Ca2+
-
maximum activity at 0.5 mM
Ca2+
-
Ca2+ preferred to Mg2+
Ca2+
-
hLALP70v either Md2+ or Ca2+ dependent
Ca2+
-
hLALP70 prefers Ca2+ to Mg2+
Ca2+
-
best activating kation
Ca2+
-
ATP hydrolysis is more effective in the presence of 1 mM CaCl2 than in the presence of 1 mM MgCl2
Ca2+
-
either Mg2+ or Ca2+ required for activity
Ca2+
absolute requirement
Ca2+
absolute requirement for divalent cation, Ca2+ fulfilling requirement best
Ca2+
or Mg2+, required, Ca2+ is preferred
Ca2+
required, activates at 1.5 mM
Ca2+
-
either Mg2+ or Ca2+ required for activity
Ca2+
Orchopeas howardi
-
function enhanced, not essential
Ca2+
-
only ADP hydrolysed in the presence of Ca2+
Ca2+
Oropsylla bacchi
-
function enhanced, not essential
Ca2+
strictly dependent on Ca2+
Ca2+
-
required for activity
Ca2+
-
either Mg2+ or Ca2+ required for activity
Ca2+
-
or Mg2+, required, Km-value 0.377 mM
Ca2+
-
required for activity
Ca2+
-
either Mg2+ or Ca2+ required for activity
Ca2+
-
best activator of isoform APY6
Ca2+
-
required, apyrase is a calcium-activated enzyme
Ca2+
-
either Mg2+ or Ca2+ required for activity
Ca2+
-
Ca2+ preferred to Mg2+
Ca2+
-
function enhanced, not essential
Co2+
-
activates
Co2+
-
stimulates ecto-ATPase activity
Co2+
-
at 1 mM, 73% of ATPase activity compared to Ca2+
Co2+
-
lower activation than Ca2+, Mg2+, Mn2+
Co2+
-
activator of isoform APY6
Co2+
required, may be substituted by Mg2+, Mg2+
Cu2+
-
activates
Mg2+
1 mM, 2.5fold stimulation
Mg2+
-
maximum activity at 6 and 9 mM with ADP and ATP respectively
Mg2+
-
either Mg2+ or Ca2+ required for activity
Mg2+
-
activates, best metal ion
Mg2+
-
ecto-ATPase activity is increased in the presence of 5 mM Mg2+
Mg2+
-
either Mg2+ or Ca2+ required for activity
Mg2+
-
either Mg2+ or Ca2+ required for activity
Mg2+
-
cannot be activated by Mg2+
Mg2+
-
activates, less effective than Ca2+
Mg2+
-
Mg2+ preferred to Mn2+
Mg2+
-
either Mg2+ or Ca2+ required for activity
Mg2+
-
hLALP70v either Mg2+ or Ca2+ required for activity
Mg2+
-
required for activity
Mg2+
-
at 1 mM, 61% of ATPase activity compared to Ca2+
Mg2+
-
up to 3fold activation
Mg2+
-
ATP hydrolysis is more effective in the presence of 1 mM CaCl2 than in the presence of 1 mM MgCl2
Mg2+
-
either Mg2+ or Ca2+ required for activity
Mg2+
absolute requirement for divalent cation, Ca2+ fulfilling requirement best
Mg2+
or Ca2+, required, Ca2+ is preferred
Mg2+
-
either Mg2+ or Ca2+ required for activity
Mg2+
Orchopeas howardi
-
function enhanced, not essential
Mg2+
Oropsylla bacchi
-
function enhanced, not essential
Mg2+
-
either Mg2+ or Ca2+ required for activity
Mg2+
-
or Ca2+, required, Km-value 0.595 mM
Mg2+
-
either Mg2+ or Ca2+ required for activity
Mg2+
-
an increase in ADPase activity in presence of Mg2+ ions occurs in case of isoform APY5
Mg2+
-
either Mg2+ or Ca2+ required for activity
Mg2+
-
most effective as activating cation, but not absolutely required
Mg2+
-
dependent on, inhibitory at 11 mM
Mg2+
required, may be substituted by Mn2+, Co2+
Mg2+
-
activates, most effect divalent cation, activity profile, overview
Mg2+
-
function enhanced, not essential
Mn2+
1 mM, about 3fold stimulation. Ca2+ and Mn2+ are best activators
Mn2+
-
15% residual activity compared with Mg2+
Mn2+
-
stimulates ecto-ATPase activity
Mn2+
-
cannot be activated by Mn2+
Mn2+
-
lower activation than Ca2+ and Mg2+
Mn2+
-
at 1 mM, 65% of ATPase activity compared to Ca2+
Mn2+
-
lower activation than Ca2+, Mg2+
Mn2+
-
lower activation than Ca2+ and Mg2+
Mn2+
-
activator of isoform APY6
Mn2+
required, may be substituted by Mg2+, Co2+
Mn2+
-
activates, most effect divalent cation
Zn2+
-
activates
Zn2+
-
cannot be activated by Zn2+
Zn2+
-
lower activation than Ca2+ ,Mg2+ and Mn2+
Zn2+
-
at 1 mM, 70% of ATPase activity compared to Ca2+
Zn2+
-
lower activation than Ca2+, Mg2+
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
-
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
additional information
-
Lpg1905 is dependent on divalent metal cations
additional information
Ca2+-ATP and Ca2+-ADP hydrolysis are superior to hydrolysis with Mg2+-ATP and Mg2+-ADP as substrates
additional information
-
Ca2+-ATP and Ca2+-ADP hydrolysis are superior to hydrolysis with Mg2+-ATP and Mg2+-ADP as substrates
additional information
not dependent on Mg2+
additional information
not dependent on Mg2+
additional information
-
not dependent on Mg2+
additional information
-
the ATP-hydrolyzing activity of PeAPY2 is enhanced with all the cations tested, except Ni2+. The descending order of preference is as follows: Mg2+, Ca2+, Zn2+, Cd2+, Mn2+, Co2+, Cu2+, Ni2+. Of note, Ca2+ and Mg2+ exhibit an additive effect in enhancing PeAPY2 apyrase activity. Moreover, both Ca2+ and Mg2+ enhancements of PeAPY2 activities are significantly reduced by EDTA
additional information
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
-
no effect: Na+ at 100 mM or K+ at 4 mM
additional information
-
Ca2+ is the most effective cofactor. The preference is in desecending order: Ca2+, Mg2+, Zn2+. Apyrase activity is dependent on ions as cofactors
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(3,5-dimethyl-1H-pyrazol-1-yl) (m-tolyl)methanone
-
(3,5-dimethyl-1H-pyrazol-1-yl) (naphthalen-2-yl)methanone
-
(3,5-dimethyl-1H-pyrazol-1-yl) (o-tolyl)methanone
-
(3,5-dimethyl-1H-pyrazol-1-yl) (pyridin-4-yl)methanone
-
(4-aminophenyl) (3,5-dimethyl-1H-pyrazol-1-yl)methanone
-
(4-aminophenyl) (3,5-dimethyl-4-(p-tolyloxy)-1H-pyrazol-1-yl)methanone
-
(4-aminophenyl) (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl)methanone
-
(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (4-chlorophenyl)methanone
-
(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (m-tolyl)methanone
-
(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (naphthalen-2-yl)methanone
-
(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (o-tolyl)methanone
-
(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (p-tolyl)methanone
-
(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (pyridin-4-yl)methanone
-
(4-chlorophenyl) (3,5-dimethyl-1H-pyrazol-1-yl)methanone
-
(4-chlorophenyl) (3,5-dimethyl-4-(p-tolyloxy)-1H-pyrazol-1-yl)methanone
-
(E)-1-(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl)-3-phenylprop-2-en-1-one
-
(R)-1-(4-chloro-3,5-dimethyl-1H-pyrazol-1-yl)-2-(4-isobutylphenyl)propan-1-one
-
1-(4-aminobenzoyl)-5-methyl-1H-pyrazol-3(2H)-one
-
1-amino-4-[(naphthalen-1-yl)amino]-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid
1-hydroxy-naphthalene-3,6-disulfonic acid
-
-
3,5-dimethyl-4-(naphthalen-2-yloxy)-1H-pyrazole
-
3-methyl-2-(4-methylbenzoyl)-1,2-dihydropyrazol-5-one
-
3-[N-(4-bromophenyl)sulfamoyl]-N-(3-nitrophenyl) benzamide
-
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
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
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
-
-
ammonium heptamolybdate
AHM, (NH4)6[Mo7O24]
citrate
-
20% inhibition at 0.5 mM
CMP
-
complete inhibition at 0.5 mM
CTP
-
free substrate inhibition
detergent NP-40
at low concentration inhibition of the membrane-bound enzyme, not of the soluble enzyme
dicylcohexylcarbodiimid
-
DCCD, slightly inhibited
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
Evans blue
-
complete inhibition at 0.1 mM
Furosemide
-
20% inhibition at 1 mM
gadolinium
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
GMP
-
complete inhibition at 0.5 mM
IDP
-
59% inhibition at 0.5 mM
IMP
-
95% inhibition at 0.5 mM
ITP
-
42% inhibition at 0.5 mM
Mn2+
-
at higher concentrations
N'-(2-hydroxy-5-methybenzylidene)-2-(1-naphthyl) acetohydrazide
-
p-chloromercuriphenylsulfonic acid
-
1 mM, 56% of inhibition
p-hydroxymercuribenzoate
-
1 mM, 35% of inhibition
pentamidine isethionate
-
PEN, inhibits 74% and 35% of the ATPase and ADPase activities, respectively of the purified enzyme NTPDase 1, no inhibition of NTPDase 2
polytungstate salt POM-1
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
PSB-POM141
i.e. [TiW11CoO40]8-; i.e. [TiW11CoO40]8-; i.e. [TiW11CoO40]8-; i.e. [TiW11CoO40]8-
-
pyridoxal-phosphate-6-azophenyl-2',4'-disulfonate
-
i.e.PPADS
succinate
-
55% inhibition at 0.5 mM
Trifluoperazine
-
0.2 mM, 31% residual ATPase activity, 61% residual ADPase activity
UDP
-
68% inhibition at 0.5 mM
UTP
-
inhibitory at 0.6 mM and above, 34% inhibition at 0.5 mM
XTP
-
60% inhibition at 0.5 mM
Zn2+
-
63% (ADPase) and 71% (ATPase) inhibition at 2 mM
1-amino-4-[(naphthalen-1-yl)amino]-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid
PSB-06126, an anthraquinone derivative, competitive mechanism of inhibition
1-amino-4-[(naphthalen-1-yl)amino]-9,10-dioxo-9,10-dihydroanthracene-2-sulfonic acid
-
5'-p-fluorosulfonylbenzoyladenosine
-
-
5'-p-fluorosulfonylbenzoyladenosine
-
50% inhibition at 2 mM
ADP
-
75% inhibition at 0.5 mM
ADP
-
hydrolysis of CaATP2- and CaADP- decreased by 50% at 0.48 mM free ADP
ADP
-
competitive inhibition
ADP
-
free substrate inhibition
ADP
-
50% inhibition at 5 mM
AMP
-
complete inhibition at 0.5 mM
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)
ARL 67156
selective inhibitor
ARL 67156
knocking down NTPDase2 expression using siRNA or inhibiting NTPDases activity with ARL 67156 simultaneously reduces ATP hydrolysis and ADP formation
ARL 67156
selective inhibitor
ATP
-
68% inhibition at 0.5 mM
ATP
-
hydrolysis of CaATP2- and CaADP- decreased by 50% at 0.3 mM free ATP
ATP
-
free substrate inhibition
azide
10 mM, 42% inhibition
azide
-
at 10 mM and pH 7.4, 21% inhibition of ATP hydrolysis, 85% inhibition of ADP hydrolysis
azide
-
inhibition of NTPDase activity of the Toxoplasma gondii is directly proportional to the largest concentration of azide used to ATP and ADP substratum
Ca2+
-
-
Ca2+
-
inhibitory at 11 mM
CDP
-
59% inhibition at 0.5 mM
CDP
-
free substrate inhibition
Cu2+
1 mM, about 3fold inhibition
DTT
-
-
EDTA
-
activity restored by adding Ca2+ or Mg2+
EDTA
-
ADP and UDP hydrolysis either from non-galled or globose gall tissues drastically reduced (66-99%) by the addition of 5 mM EDTA
EDTA
-
analyzed in presence and absence of, control reaction
EDTA
-
complete inhibition at 1 M
EDTA
-
complete inhibition at 5 mM
EDTA
analyzed in presence and absence of, control reaction
EDTA
-
activity not restored with 5 mM Ca2+ or Mg2+ for periods up to 24h
EDTA
-
complete inhibition at 10 mM
EDTA
-
about 40% inhibition at 5 mM
EGTA
-
ADP and UDP hydrolysis either from non-galled or globose gall tissues drastically reduced (66-99%) by the addition of 5 mM EGTA
EGTA
-
complete inhibition at 5 mM
erythrosine B
-
-
erythrosine B
does not affect the ATPase activity but inhibits ADPase activity of MP67 to a minor extent
fluoride
10 mM, 27% inhibition
fluoride
-
at 10 mM and pH 7.4, 2% inhibition of ATP hydrolysis, 91% inhibition of ADP hydrolysis
GDP
-
81% inhibition at 0.5 mM
GDP
-
free substrate inhibition
GTP
-
70% inhibition at 0.5 mM
GTP
-
free substrate inhibition
HgCl
-
-
Mg2+
-
-
Mg2+
-
dependent on, inhibitory at 11 mM
N3-
-
-
NaF
-
-
NaN3
-
-
NaN3
-
an inhibitor of F-type ATPases, 25% inhibition at 5 mM
NaN3
inhibition from 30-70% depending on tissue, inhibition of ADP hydrolysis slightly more pronounced
NaN3
-
58% inhibition at 10 mM
orthovanadate
-
-
orthovanadate
-
hydrolysis of ADP
orthovanadate
-
0.1 mM, 45% inhibition of ATPase activity
orthovanadate
-
inhibition profile at 0-10 mM
Sodium azide
-
hydrolysis of both ATP and ADP
Sodium azide
-
58% inhibition of the ATPase activity at 5 mM
Sodium azide
-
24% inhibition at 1 mM
Sodium azide
-
not inhibitory at 1 mM, 25% inhibition of ATPase activity at 20 mM
Sodium azide
-
not inhibitory at 5 mM, up to 37% inhibition at 20 mM
sodium deoxycholate
-
-
sodium deoxycholate
Triticosecale Wittmack
-
-
Sodium fluoride
-
20 mM, 50% residual ATPase activity, 56% residual ADPase activity
Sodium fluoride
inhibits the ADPase activity rather than the ATPase activity of MP67
sodium orthovanadate
-
53% inhibition of the ATPase activity at 5 mM
sodium orthovanadate
has a strong inhibitory effect on ATPase activity and a weaker effect on ADPase activity of MP67
suramin
-
0.5 mM suramin reduces enzyme activity in yeast living cells by 81.8%
suramin
-
0.1 mM, 10% residual activity
suramin
-
0.3 mM, 44% residual ATPase activity, 63% residual ADPase activity
suramin
noncompetitive inhibition, inhibition mechanism analysis, overview
suramin
-
0.25 mM, 19% inhibition of ATPase activity
suramin
-
a P2 purinoreceptor antagonist, 50% inhibition at 0.05-0.5 mM
suramin
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
triflupromazine
-
-
UMP
-
92% inhibition at 0.5 mM
vanadate
1 mM, 54% inhibition
vanadate
-
at 10 mM and pH 7.4, 7% inhibition of ATP hydrolysis, 54% inhibition of ADP hydrolysis
vanadate
1 mM, inhibition
vanadate
-
15% inhibition at 1 mM
vanadate
1 mM, about 65% inhibition
additional information
-
no inhibition by orthovanadate; no inhibition by ouabain; no inhibition by P1,P5-di(adenosine-5'-)pentanphospate
-
additional information
-
no inhibition by ouabain
-
additional information
-
no inhibition by Ap5A; no inhibition by ouabain; no inhibition by tetramisole
-
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
-
no inhibition by NaN3; no inhibition by ouabain; no inhibition by p-NPP, beta-GP
-
additional information
antibodies directed against CApy block Cryptosporidium parvum sporozoite invasion of HCT-8 cells
-
additional information
-
antibodies directed against CApy block Cryptosporidium parvum sporozoite invasion of HCT-8 cells
-
additional information
-
the catalytic activity and platelet deaggregation property of Ruviapyrase is significantly inhibited by EDTA, DTT, and iodoacetamide, and neutralized by commercial monovalent and polyvalent antivenom. Poor inhibition by PMSF
-
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
-
not inhibitory: Concanavalin A, suramin
-
additional information
the chicken enzyme does not show substrate inhibition
-
additional information
-
the chicken enzyme does not show substrate inhibition
-
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
-
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
the activity of the GS52 enzyme is not significantly affected by Nod factor addition
-
additional information
-
not inhibitory: sodium orthovanadate, sodium fluoride, ammonium molybdate, oligomycin, sodium azide, bafilomycin A, ouabain, levamizole
-
additional information
-
not being altered by P-type, F-type or V-type NTPase inhibitors
-
additional information
-
no inhibition by ouabain
-
additional information
-
no inhibition by ouabain
-
additional information
-
no inhibition by Ap5A; no inhibition by ouabain
-
additional information
-
not inhibitory: N-ethylmaleimide, iodoacetamide, iodoacetic acid
-
additional information
-
not inhibitory: P1,P5-di(adenosine-5)pentaphosphate, ouabain, levamisole, oligomycin, N-ethylmaleimide, sodium azide
-
additional information
the enzyme shows substrate inhibition
-
additional information
-
the enzyme shows substrate inhibition
-
additional information
identification of subtype-selective inhibitors, and 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, for inhibitor screening. Methods comparisons, overview. The evaluated 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); identification of subtype-selective inhibitors, and 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, for inhibitor screening. Methods comparisons, overview. The evaluated 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); identification of subtype-selective inhibitors, and 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, for inhibitor screening. Methods comparisons, overview. The evaluated 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); identification of subtype-selective inhibitors, and 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, for inhibitor screening. Methods comparisons, overview. The evaluated 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)
-
additional information
identification of subtype-selective inhibitors, and 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, for inhibitor screening. Methods comparisons, overview. The evaluated 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); identification of subtype-selective inhibitors, and 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, for inhibitor screening. Methods comparisons, overview. The evaluated 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); identification of subtype-selective inhibitors, and 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, for inhibitor screening. Methods comparisons, overview. The evaluated 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); identification of subtype-selective inhibitors, and 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, for inhibitor screening. Methods comparisons, overview. The evaluated 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)
-
additional information
identification of subtype-selective inhibitors, and 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, for inhibitor screening. Methods comparisons, overview. The evaluated 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); identification of subtype-selective inhibitors, and 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, for inhibitor screening. Methods comparisons, overview. The evaluated 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); identification of subtype-selective inhibitors, and 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, for inhibitor screening. Methods comparisons, overview. The evaluated 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); identification of subtype-selective inhibitors, and 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, for inhibitor screening. Methods comparisons, overview. The evaluated 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)
-
additional information
identification of subtype-selective inhibitors, and 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, for inhibitor screening. Methods comparisons, overview. The evaluated 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); identification of subtype-selective inhibitors, and 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, for inhibitor screening. Methods comparisons, overview. The evaluated 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); identification of subtype-selective inhibitors, and 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, for inhibitor screening. Methods comparisons, overview. The evaluated 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); identification of subtype-selective inhibitors, and 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, for inhibitor screening. Methods comparisons, overview. The evaluated 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)
-
additional information
-
not inhibitory: vanadate, ouabain, thapsigargin, dicyclohexylcarbodiimide, oligomycin, bafilomycin A, levamisole, ammonium molybdate
-
additional information
-
not inhibitory: Triton X-100
-
additional information
-
ATPase activity is not inhibited by DCCD
-
additional information
-
0.1 mM N,N'-dicyclohexylcarbodiimide does not affect significantly ATP hydrolysis
-
additional information
-
amphotericin B, fluconazole, ketoconazole or allopurinol do not significantly affect ATPase and/or ADPase activity of promastigotes preparation, no or poor to low (at high concentrations) inhibition
-
additional information
-
recombinant MpAPY2 shows no significant effect in the presence of vanadate
-
additional information
recombinant MpAPY2 shows no significant effect in the presence of vanadate
-
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
-
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
oligomycin (an inhibitor of mitochondrial ATPases), orthovanadate (an inhibitor of transport ATPases, acid phosphatases, and phosphotyrosine phosphatases), Ap5A (an inhibitor of adenylate kinase [AK]), ouabain (a classic inhibitor of Na+-ATPase and K+-ATPase), NEM (Ca2+-ATPases and Mg2+-ATPases, AK and sulfhydryl group modifier), levamisole (inhibitor of alkaline phosphatase), tetramisole (inhibitor of alkaline phosphatase), and sodium azide (inhibitor of mitochondrial ATPases) below 10 mM do not show an inhibitory effect on ATP and ADP hydrolysis by E-NTPDase
-
additional information
-
oligomycin (an inhibitor of mitochondrial ATPases), orthovanadate (an inhibitor of transport ATPases, acid phosphatases, and phosphotyrosine phosphatases), Ap5A (an inhibitor of adenylate kinase [AK]), ouabain (a classic inhibitor of Na+-ATPase and K+-ATPase), NEM (Ca2+-ATPases and Mg2+-ATPases, AK and sulfhydryl group modifier), levamisole (inhibitor of alkaline phosphatase), tetramisole (inhibitor of alkaline phosphatase), and sodium azide (inhibitor of mitochondrial ATPases) below 10 mM do not show an inhibitory effect on ATP and ADP hydrolysis by E-NTPDase
-
additional information
-
no inhibition by azide; no inhibition by orthovanadate; no inhibition by ouabain
-
additional information
-
infection with bovine herpesvirus type 5 (BoHV-5) strain SV-507/99 leads to a decrease in ectonucleotidase activity in synaptosomes from the cerebral cortex of infected rabbits, whereas an increased ectonucleotidase activity in synaptosomes from the hippocampus is observed. BoHV-5 replication results in changes in ectonucleotidase activity in the brain, which may contribute to the neurological signs commonly observed in the disease herpetic meningoencephalitis
-
additional information
-
no or poor inhibition by NaF (inhibitor of pyrophosphatase), NaNO3 (inhibitor of V-type ATPases), Na3VO4 (inhibitor of P-type ATPases), Na2MoO4 (inhibitor of acid phosphatases) and N-(3-methylphenyl)-[1,1-biphenyl]-4-sulfonamide (NGXT191, inhibitor of apyrases)
-
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 oligomycin; no inhibition by ouabain
-
additional information
-
no inhibition by oligomycin; no inhibition by orthovanadate; 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
-
not inhibitory: oligomycin, ouabain, bafilomycin A, theophylline, thapsigarin, ethacrynic acid, P1,P5-(adenosine-5)pentyphosphate, omeprazole
-
additional information
-
not inhibitory: ouabain, N-ethylmaleimide, lanthanum, oligomycin, levamisole, cAMP
-
additional information
inhibition mechanism of polyoxometallates, overview
-
additional information
synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases; synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases; synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases; synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases
-
additional information
synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases; synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases; synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases; synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases
-
additional information
synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases; synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases; synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases; synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases
-
additional information
synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases; synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases; synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases; synthesis of aryl pyrazole derivatives using 1,3-dicarbonyl motifs. Synthesis of (3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones and (4-chloro-3,5-dimethyl-1H-pyrazol-1-yl) (phenyl)methanones by grinding equimolar concentrations of pentane-2,4-dione and 3-chloropentane-2,4-dione with different arylhydrazides, respectively. The compounds can be regarded as 1H-pyrazol-1-yl-one analogues and represent drug like molecules. Structure-activity relationships, FT-IR, 1H NMR, 13C NMR and mass spectroscopic structure analysis, overview. Effects of these synthesized compounds on different isozymes of nucleoside triphosphate diphosphohydrolases, NTPDases
-
additional information
-
development of a high-throughput screening (HTS)-compatible format for inhibitor screening, a luminescence-based detection system as cost-effective biochemical assay in microplates, overview. 0.1% DMSO and 0.01% Tween 20 have no effect on enzyme stability and activity
-
additional information
-
not inhibitory: N,N'-dicyclohexylcarbodiimide, azide, oligomycin, N'-ethylmaleimide, p-chloromercuribenzoate, orthovanadate, or ouabain
-
additional information
-
no inhibition by NaN3
-
additional information
-
-
-
additional information
-
not inhibitory: ouabain, N-ethylmaleimide, orthovanadate, levamisole, P1,P5-di(adenosine 5)pentaphosphate
-
additional information
-
no inhibition by oligomycin, ouabain, and molybdate
-
additional information
not inhibitory: sodium azide, bafilomycin A, ammonium molybdate, DMSO
-
additional information
inhibition of Ecto-ATPDase by ant-Ecto-NTPDase-anti-serum, inhibition of Ecto-ATPDase activities and of trypomastigotes infectivity in vivo
-
additional information
-
inhibition of Ecto-ATPDase by ant-Ecto-NTPDase-anti-serum, inhibition of Ecto-ATPDase activities and of trypomastigotes infectivity in vivo
-
additional information
-
not inhibitory: oligomycin, sodium azide, bafilomycin A1, ouabain, furosemide, vanadate, molybdate, sodium fluoride, tartrate, levamizole
-
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0.073 - 0.114
1,N6-etheno-ADP
0.024 - 0.031
1,N6-Etheno-ATP
0.009 - 0.019
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate
0.008 - 0.018
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate
0.014 - 0.017
3'(2')-O-(methylanthranoyl)adenosine 5'-diphosphate
0.012 - 0.018
3'(2')-O-(methylanthranoyl)adenosine 5'-triphosphate
0.43
8-oxo-dGTP
-
pH 8.5, 37°C
0.1712
AMPCPP
recombinant wild-type enzyme, pH 7.4, 25°C
0.777
CDP
-
pH 7.5, 37°C, presence of Mg2+
0.148
CTP
-
pH 7.5, 37°C, presence of Mg2+
0.0133 - 0.105
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate
0.7495
TDP
recombinant wild-type enzyme, pH 7.4, 25°C
additional information
additional information
-
0.073
1,N6-etheno-ADP
-
30°C, pH 6.0, presence of Ca2+
0.114
1,N6-etheno-ADP
-
30°C, pH 6.0, presence of Ca2+
0.024
1,N6-Etheno-ATP
-
30°C, pH 6.0, presence of Ca2+
0.031
1,N6-Etheno-ATP
-
30°C, pH 6.0, presence of Ca2+
0.009
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate
-
30°C, pH 6.0, presence of Ca2+
0.019
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate
-
30°C, pH 6.0, presence of Ca2+
0.008
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate
-
30°C, pH 6.0, presence of Ca2+
0.018
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate
-
30°C, pH 6.0, presence of Ca2+
0.014
3'(2')-O-(methylanthranoyl)adenosine 5'-diphosphate
-
30°C, pH 6.0, presence of Ca2+
0.017
3'(2')-O-(methylanthranoyl)adenosine 5'-diphosphate
-
30°C, pH 6.0, presence of Ca2+
0.012
3'(2')-O-(methylanthranoyl)adenosine 5'-triphosphate
-
30°C, pH 6.0, presence of Ca2+
0.018
3'(2')-O-(methylanthranoyl)adenosine 5'-triphosphate
-
30°C, pH 6.0, presence of Ca2+
0.0025
ADP
recombinant mutant EDC K257M, pH 7.4, 25°C
0.0025
ADP
recombinant mutant EDC Y314F, pH 7.4, 25°C
0.0047
ADP
recombinant wild-type enzyme, pH 7.4, 25°C
0.0051
ADP
recombinant mutant EDC Y409F, pH 7.4, 25°C
0.00577
ADP
-
pH 7.4, 37°C
0.0059
ADP
recombinant mutant EDC DELTA MIL, pH 7.4, 25°C
0.0125
ADP
-
pH 7.5, 37°C
0.042
ADP
-
free enzyme, pH 7.4, 22°C
0.056
ADP
-
immobilized enzyme, pH 7.4, 22°C
0.07
ADP
-
variety Desiree, 20°C
0.1
ADP
-
variety Desiree, 30°C
0.13
ADP
-
variety Desiree, 40°C
0.14
ADP
-
variety Pimpernel, 20°C
0.15
ADP
-
pH 7.5, 37°C, presence of Mg2+
0.167
ADP
-
pH 7.4, 37°C, presence of Ca2+
0.196
ADP
-
pH 7.5, 37°C, presence of Ca2+
0.25
ADP
-
variety Pimpernel, 30°C
0.27
ADP
-
variety Pimpernel, 40°C
0.309
ADP
-
pH and temperature not specified in the publication
1
ADP
-
pH 7.4, 37°C, recombinant enzyme
0.00254
ATP
-
pH 7.4, 37°C
0.00929
ATP
-
pH 6.0, 22°C
0.017
ATP
pH 7.5, 37°C, recombinant enzyme
0.07
ATP
pH 7.5, 37°C, recombinant enzyme
0.075
ATP
pH 7.5, 37°C, recombinant enzyme
0.0776
ATP
-
pH 8.0, 37°C
0.081 - 0.226
ATP
pH 7.5, 37°C, recombinant enzyme
0.083
ATP
-
pH 7.5, 37°C, presence of Mg2+
0.084
ATP
mutant enzyme E493G, at pH 7.4, temperature not specified in the publication
0.085
ATP
-
pH 7.5, 37°C, presence of Ca2+
0.12
ATP
mutant enzyme R492G/E493G, at pH 7.4, temperature not specified in the publication
0.141
ATP
-
pH 7.4, 37°C, presence of Ca2+
0.4
ATP
-
pH 7.4, 37°C, recombinant enzyme
0.424
ATP
-
pH and temperature not specified in the publication
0.6
ATP
-
at 30°C in 50 mM HEPES, pH 7.2
2.5 - 3
ATP
mutant enzyme R492G, at pH 7.4, temperature not specified in the publication
3.4
ATP
wild type enzyme, at pH 7.4, temperature not specified in the publication
8.7
ATP
-
TaAPY3-1, 37°C, pH 5.5, 8 mM Ca2+
0.018
dATP
-
30°C, pH 6.0, presence of Ca2+
0.031
dATP
-
30°C, pH 6.0, presence of Ca2+
0.029
dCTP
-
30°C, pH 6.0, presence of Ca2+
0.032
dCTP
-
30°C, pH 6.0, presence of Ca2+
0.028
dGTP
-
30°C, pH 6.0, presence of Ca2+
0.133
dGTP
-
30°C, pH 6.0, presence of Ca2+
0.027
dTTP
-
30°C, pH 6.0, presence of Ca2+
0.093
dTTP
-
30°C, pH 6.0, presence of Ca2+
0.0114
GDP
recombinant wild-type enzyme, pH 7.4, 25°C
0.0131
GDP
in presence of 0.1 mM UMP, recombinant wild-type enzyme, pH 7.4, 25°C
0.0488
GDP
in presence of 0.1 mM AMP, recombinant wild-type enzyme, pH 7.4, 25°C
0.149
GDP
in presence of 0.1 mM AHM, recombinant wild-type enzyme, pH 7.4, 25°C
0.357
GDP
-
pH 7.5, 37°C, presence of Mg2+
0.009
GTP
recombinant wild-type enzyme, pH 7.4, 25°C
0.164
GTP
-
pH 7.5, 37°C, presence of Mg2+
0.0105
IDP
recombinant wild-type enzyme, pH 7.4, 25°C
0.622
IDP
-
pH 7.5, 37°C, presence of Mg2+
0.0108
ITP
recombinant wild-type enzyme, pH 7.4, 25°C
0.259
ITP
-
pH 7.5, 37°C, presence of Mg2+
0.0133
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate
pH 6.5, temperature not specified in the publication, NTPDase3
0.0196
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate
pH 6.5, temperature not specified in the publication, NTPDase1
0.0555
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate
pH 6.5, temperature not specified in the publication, NTPDase2
0.105
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate
pH 6.5, temperature not specified in the publication, NTPDase8
0.021
thio-dATP
-
30°C, pH 6.0, presence of Ca2+
0.048
thio-dATP
-
30°C, pH 6.0, presence of Ca2+
0.0113
UDP
recombinant wild-type enzyme, pH 7.4, 25°C
0.0175
UDP
recombinant mutant EDC DELTA MIL, pH 7.4, 25°C
0.555
UDP
-
pH 7.5, 37°C, presence of Mg2+
0.01
UTP
-
0.01
UTP
recombinant wild-type enzyme, pH 7.4, 25°C
0.0129
UTP
recombinant mutant EDC DELTA MIL, pH 7.4, 25°C
0.207
UTP
-
pH 7.5, 37°C, presence of Mg2+
additional information
additional information
kinetic analysis
-
additional information
additional information
-
kinetic analysis
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
kinetics, overview
-
additional information
additional information
-
kinetics with different substrates, overview
-
additional information
additional information
-
substrate specificity and Michaelis-Menten kinetics, overview
-
additional information
additional information
-
the enzyme shows Michaelis-Menten kinetics with all substrates except for UTP
-
additional information
additional information
-
Michaelis-Menten kinetic modeling of free and immobilized enzymes, overview
-
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86 - 1384
1,N6-etheno-ADP
682 - 1642
1,N6-Etheno-ATP
70 - 328
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate
191 - 982
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate
23 - 828
3'(2')-O-(methylanthranoyl)adenosine 5'-diphosphate
800 - 965
3'(2')-O-(methylanthranoyl)adenosine 5'-triphosphate
0.96
8-oxo-dGTP
-
pH 8.5, 37°C
40.5
AMPCPP
recombinant wild-type enzyme, pH 7.4, 25°C
80.9
GTP
recombinant wild-type enzyme, pH 7.4, 25°C
79.9
IDP
recombinant wild-type enzyme, pH 7.4, 25°C
105.3
ITP
recombinant wild-type enzyme, pH 7.4, 25°C
0.0225 - 0.119
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate
80.2
TDP
recombinant wild-type enzyme, pH 7.4, 25°C
86
1,N6-etheno-ADP
-
30°C, pH 6.0, presence of Ca2+
1384
1,N6-etheno-ADP
-
30°C, pH 6.0, presence of Ca2+
682
1,N6-Etheno-ATP
-
30°C, pH 6.0, presence of Ca2+
1642
1,N6-Etheno-ATP
-
30°C, pH 6.0, presence of Ca2+
70
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate
-
30°C, pH 6.0, presence of Ca2+
328
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate
-
30°C, pH 6.0, presence of Ca2+
191
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate
-
30°C, pH 6.0, presence of Ca2+
982
2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate
-
30°C, pH 6.0, presence of Ca2+
23
3'(2')-O-(methylanthranoyl)adenosine 5'-diphosphate
-
30°C, pH 6.0, presence of Ca2+
828
3'(2')-O-(methylanthranoyl)adenosine 5'-diphosphate
-
30°C, pH 6.0, presence of Ca2+
800
3'(2')-O-(methylanthranoyl)adenosine 5'-triphosphate
-
30°C, pH 6.0, presence of Ca2+
965
3'(2')-O-(methylanthranoyl)adenosine 5'-triphosphate
-
30°C, pH 6.0, presence of Ca2+
31.1
ADP
recombinant mutant EDC Y409F, pH 7.4, 25°C
50.4
ADP
recombinant mutant EDC K257M, pH 7.4, 25°C
77.3
ADP
recombinant wild-type enzyme, pH 7.4, 25°C
86.1
ADP
recombinant mutant EDC Y314F, pH 7.4, 25°C
86.9
ADP
recombinant mutant EDC DELTA MIL, pH 7.4, 25°C
100
ATP
-
pH 6.0, 22°C
280
ATP
wild type enzyme, at pH 7.4, temperature not specified in the publication
1230
ATP
mutant enzyme R492G, at pH 7.4, temperature not specified in the publication
1410
ATP
mutant enzyme E493G, at pH 7.4, temperature not specified in the publication
2200
ATP
mutant enzyme R492G/E493G, at pH 7.4, temperature not specified in the publication
1.5
dATP
-
pH 8.5, 37°C
636
dATP
-
30°C, pH 6.0, presence of Ca2+
2222
dATP
-
30°C, pH 6.0, presence of Ca2+
490
dCTP
-
30°C, pH 6.0, presence of Ca2+
2174
dCTP
-
30°C, pH 6.0, presence of Ca2+
0.74
dGTP
-
pH 8.5, 37°C
573
dGTP
-
30°C, pH 6.0, presence of Ca2+
3019
dGTP
-
30°C, pH 6.0, presence of Ca2+
455
dTTP
-
30°C, pH 6.0, presence of Ca2+
2841
dTTP
-
30°C, pH 6.0, presence of Ca2+
82.6
GDP
in presence of 0.1 mM AMP, recombinant wild-type enzyme, pH 7.4, 25°C
83.2
GDP
recombinant wild-type enzyme, pH 7.4, 25°C
83.2
GDP
in presence of 0.1 mM UMP, recombinant wild-type enzyme, pH 7.4, 25°C
103.7
GDP
in presence of 0.1 mM AHM, recombinant wild-type enzyme, pH 7.4, 25°C
0.0225
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate
pH 6.5, temperature not specified in the publication, NTPDase3
0.0387
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate
pH 6.5, temperature not specified in the publication, NTPDase8
0.0494
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate
pH 6.5, temperature not specified in the publication, NTPDase2
0.119
N-[5-[4-carboxy-3-(3-oxo-9,9a-dihydro-3H-xanthen-9-yl)benzamido]pentyl]adenosine 5'-triphosphate
pH 6.5, temperature not specified in the publication, NTPDase1
595
thio-dATP
-
30°C, pH 6.0, presence of Ca2+
1101
thio-dATP
-
30°C, pH 6.0, presence of Ca2+
80.9
UDP
recombinant wild-type enzyme, pH 7.4, 25°C
93
UDP
recombinant mutant EDC DELTA MIL, pH 7.4, 25°C
103.4
UTP
recombinant wild-type enzyme, pH 7.4, 25°C
121.2
UTP
recombinant mutant EDC DELTA MIL, pH 7.4, 25°C
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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
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
the enzyme is a member of the eukaryotic NTPDase family
evolution
nucleoside triphosphate diphosphohydrolases (NTPDases) belong to the GDA1/CD39 protein superfamily, E-NTPDase family. Existence of several isoforms with different specificities with respect to divalent cations (magnesium, calcium, manganese, and zinc) and substrates
evolution
-
the enzyme belongs to the APY gene family
evolution
-
the enzyme belongs to the NTPDase family
evolution
the seven member Arabidopsis apyrase family contains representatives in each clade and are clustered into the AtAPY1-2 clade I (GDA1-like), the AtAPY3-6 (clade II) and AtAPY7 in clade III. Isozymes AtAPY3, AtAPY4, and AtAPY5 occur as recurrent tandem duplications and share 68% identity, all three are expressed during Arabidopsis thaliana development with AtAPY3 predominately in the roots and both AtAPY4/AtAPY5 in the vegetative rosette. The protein structure of the seven Arabidopsis apyrase proteins outline the apyrase conserved domain GDA1_CD39 and predicted transmembrane helices
evolution
the seven member Arabidopsis apyrase family contains representatives in each clade and are clustered into the AtAPY1-2 clade I (GDA1-like), the AtAPY3-6 (clade II) and AtAPY7 in clade III. The clade I (GDA-like) Arabidopsis members (AtAPY1 andAtAPY2) form a distinct clade with the other characterized plant apyrases, human apyrases and the yeast GDA1 enzyme. The protein structure of the seven Arabidopsis apyrase proteins outline the apyrase conserved domain GDA1_CD39 and predicted transmembrane helices
evolution
the seven member Arabidopsis apyrase family contains representatives in each clade and are clustered into the AtAPY1-2 clade I (GDA1-like), the AtAPY3-6 (clade II) and AtAPY7 in clade III. The protein structure of the seven Arabidopsis apyrase proteins outline the apyrase conserved domain GDA1_CD39 and predicted transmembrane helices
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
the inactivated, functionally disrupted enzyme is not active in stimulating nodulation
malfunction
downregulation of NTPDase3 expression in MIN-6 cells inhibits extracellular ATP hydrolysis and insulin secretion
malfunction
-
single knockout mutants of isoforms APY6 and 7 display a minor change in pollen exine pattern without obvious change in fertility, while double knockout mutants of APY6 and 7 display severe defects in pollen exine pattern, deformed pollen shape and reduced male fertility
malfunction
the excessive levels of extracellular ATP in the enzyme knockout animals desensitize the P2X receptors associated with nerve fibers, thereby depressing taste responses
malfunction
-
the suppression of isoforms APY1 and APY2 blocks growth in Arabidopsis thaliana. The basal halves of apyrase-suppressed hypocotyls contain considerably lower free indole-3-acetic acid levels when compared with wild type plants, and disrupted auxin transport in the apyrase-suppressed roots is reflected by their significant morphological abnormalities, such as unusual root hair distribution and meristematic disorganization. A critical step connecting apyrase suppression to growth suppression is the inhibition of polar auxin transport
malfunction
apy2 single knockout roots show increased skewing compared with wild-type roots when grown on phytagel
malfunction
immunochemical and genetic suppression of AtAPY1 and AtAPY2 results in an increase in extracellular ATP
malfunction
-
infection with bovine herpesvirus type 5 (BoHV-5) strain SV-507/99 leads to a decrease in ectonucleotidase activity in synaptosomes from the cerebral cortex of infected rabbits, whereas an increased ectonucleotidase activity in synaptosomes from the hippocampus is observed. On day 7 p.i., NTPDase activity (ATP and ADP hydrolysis) are decreased in synaptosomes from the cerebral cortex of rabbits infected with BoHV-5 in relation to the control group. BoHV-5 replication results in changes in ectonucleotidase activity in the brain, which may contribute to the neurological signs commonly observed in the disease herpetic meningoencephalitis
malfunction
the primary roots of seedlings overexpressing APY1 show less skewing than wild-type plants. Plants suppressed in their expression of APY1 show more skewing than wild-type plants. The primary roots of apy1 single knockout (APY1 KO) seedlings (Ws background) exhibit increased rightward skewing and have an HGI that is significantly higher than that of wild-type roots. The apy1 single knockout roots show increased skewing compared with wild-type roots when grown on phytagel. Treatment of R2-4A seedlings with estradiol induces 70% suppression of APY1 expression in the null background of APY2 and results in shortened roots with swollen root tips. Apy1 mutant roots show altered cell file rotation. Phenotypes, overview
malfunction
-
under cold stress, PeAPY2-overexpressing transgenic plants maintain plasma membrane integrity and show reduced cold-elicited electrolyte leakage compared with wild-type plants. These responses probably result from efficient plasma membrane repair via vesicular trafficking. Transgenic plants show accelerated endocytosis and exocytosis during cold stress and recovery. Low doses of extracellular ATP accelerate vesicular trafficking, but high extracellular ATP inhibit trafficking and reduce cell viability. Cold stress causes significant increases in root medium extracellular ATP. Under these conditions, PeAPY2-overexpressing transgenic lines show greater control of extracellular ATP levels than wild-type plants
metabolism
plasma membrane-bound NTPDases, namely NTPDase1/CD39, NTPDase2/CD39L1, and NTPDase8, represent the major liver ectonucleotidase activities
metabolism
roles of the Arabidopsis thaliana apyrase family in regulating endomembrane NDP/NMP homoeostasis, overview. The AtAPY1-6 Arabidopsis thaliana enzymes all exhibit classic apyrase-like NTPase and/or NDPases activities, with an absence of NMP activity
metabolism
-
plasma membrane-bound NTPDases, namely NTPDase1/CD39, NTPDase2/CD39L1, and NTPDase8, represent the major liver ectonucleotidase activities
-
physiological function
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
antibodies directed against CApy block Cryptosporidium parvum sporozoite invasion of HCT-8 cells
physiological function
apyrases can inhibit platelet activation by depletion of adenosine diphosphate
physiological function
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
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
physiological function
-
apyrase enzyme blocks abscisic acid-induced stomatal closure
physiological function
isoform APY1 exerts its growth and developmental effects by possibly regulating glycosylation reactions in the Golgi
physiological function
-
isoforms APY6 and AtAPY7 play an important role in exine development of pollen grains, possibly through regulating the production of key polysaccharides needed for proper assembly of the exine layer
physiological function
pharmacological inhibition by ARL 67156 or gene silencing of the endogenous ecto-nucleoside triphosphate diphosphohydrolase isoform 2 results in a 25% reduction in both ATP hydrolysis and ADP formation. NTPDase2 hydrolyzes ATP and generates sustainable ADP levels. Knocking down NTPDase2 potentiates the nanomolar ATP-induced intracellular calcium increase
physiological function
-
the basal halves of apyrase-suppressed hypocotyls contain considerably lower free indole-3-acetic acid levels when compared with wild type plants, and disrupted auxin transport in the apyrase-suppressed roots is reflected by their significant morphological abnormalities, such as unusual root hair distribution and meristematic disorganization
physiological function
the enzyme blocks platelet aggregation and supports blood flow
physiological function
the enzyme modulates insulin secretion by controlling activation of purinergic receptors
physiological function
the enzyme modulates insulin secretion by controlling activation of purinergic receptors
physiological function
-
apyrase and extracellular ATP play crucial roles in mediating plant growth and defense responses. Cold stress causes significant increases in root medium extracellular ATP
physiological function
-
apyrase decreases microglial ramification and surveillance. Applying the ATPase apyrase, an enzyme which hydrolyzes ATP and ADP, reduces microglial process ramification and surveillance in acutely prepared postnatal day (P)12 rat hippocampal slices, suggesting that ambient ATP/ADP maintains microglial surveillance. But attempting to raise the level of ATP/ADP by blocking the endogenous ecto-ATPase (termed NTPDase1/CD39), which also hydrolyzes ATP/ADP, does not affect the cells' ramification or surveillance, nor their membrane currents, which respond to even small rises of extracellular [ATP] or [ADP] with the activation of K+ channels. This indicates a lack of detectable ambient ATP/ADP and ecto-ATPase activity, contradicting the results with apyrase. Contamination of commercially available apyrase by a high K+ concentration reduces ramification and surveillance by depolarizing microglia. Exposure to the same K+ concentration (without apyrase added) reduced ramification and surveillance as with apyrase. Dialysis of apyrase to remove K+ retains its ATP-hydrolyzing activity but abolishes the microglial depolarization and decrease of ramification produced by the undialyzed enzyme. Microglia are very sensitive to increases of extracellular ATP concentration, to which they respond by activating P2Y12 receptor-gated THIK-1 K+ channels, generating an outward K+ current which leads to a hyperpolarization of their membrane
physiological function
-
apyrases, which directly regulate intra- and extracellular ATP homeostasis, play a pivotal role in the regulation of various stress adaptations in mammals, bacteria and plants
physiological function
biochemical analysis of AtAPY4 results in the lowest NDPase activates measured, exhibiting a substrate preference for CTP. But even with this reduced NDPase activity, the isozyme's localization to the Golgi lumen probably assists in the positive complementation phenotype in Saccharomyces cerevisiae DELTAgda1DELTAynd1 dKO. The Arabidopsis apyrases family members have possible roles in regulating endomembrane NDP/NMP (nucleoside monophosphate) homoeostasis
physiological function
-
BjAPY2 is closely associated with the expansion of stems but not of leaves in the tuber mustard. Cloning and analysis of the promoter region of BjAPY2 reveal that there are several types of motifs in the promoter region, including the light and temperature responsive elements suggesting that BjAPY2 might play an important role during the stem expansion of the tuber mustard
physiological function
both AtAPY1 and AtAPY2 have been shown to play numerous physiological roles in pollen development, vegetative growth and stomata opening/closure. AtAPY1 and AtAPY2 function as plant endo-apyrases and are necessary for lumenal glycosylation. The Arabidopsis apyrases family members have possible roles in regulating endomembrane NDP/NMP (nucleoside monophosphate) homoeostasis. AtAPY 1 and AtAPY2 are able to function as internal Golgi lumenal NDPases
physiological function
differential effect of apyrase treatment and hCD39 overexpression on chronic renal fibrosis after ischemia-reperfusion injury (IRI), overview. Hydrolysis of ATP to adenosine diphosphate (ADP) by the ectonucleotidase CD39 (ENTPDase1) is an important step in reducing the proinflammatory effects of ATP CD39 also hydrolyses ADP to adenosine monophosphate (AMP), which is subsequently converted to adenosine by CD73 (5' ectonucleotidase). Augmenting CD39 activity is a potential therapy to improve both short- and long-term outcomes of IRI by reducing the extracellular concentration of proinflammatory ATP and promoting adenosine generation. hCD39 transgene expression in CD39Tg mice (C57BL/6 wild-type expressing human CD39) reduces ischemia-induced acute renal injury, but exacerbates chronic renal injury. Apyrase does not modify baseline ATP, ADP, AMP, adenosine or inosine levels, but reduces ATP, ADP, and AMP levels during ischemia. Apyrase attenuates the increase in A2BR mRNA levels at week 4 post-IRI
physiological function
ecto-nucleoside triphosphate diphosphohydrolase1 (NTPDase1, CD39) is a major ectonucleotidase that hydrolyzes proinflammatory ATP via ADP to AMP, which is subsequently converted by ecto-5'-nucleotidase (CD73) to immunosuppressive adenosine
physiological function
ectoapyrases (ect-NTPDases) function to decrease levels of extracellular ATP and ADP in animals and plants. Ectopic expression of a pea ectoapyrase, psNTP9, enhances growth in Arabidopsis thaliana seedlings and the overexpression of the two Arabidopsis apyrases most closely related to psNTP9 enhances auxin transport and growth in Arabidopsis thaliana. Ectopic expression of psNTP9 can promote a more extensive root system architecture (RSA) in Arabidopsis thaliana. Transgenic Arabidopsis thaliana seedlings have longer primary roots, more lateral roots, and more and longer root hairs than wild-type plants. Transcriptomic analyses reveal gene expression changes in the transgenic plants that help account for their enhanced RSA and improved drought tolerance
physiological function
ectoapyrases (ecto-NTPDases) function to decrease levels of extracellular ATP and ADP in animals and plants. Ectopic expression of a pea ectoapyrase, psNTP9, enhances growth in Arabidopsis thaliana seedlings and the overexpression of the two Arabidopsis apyrases most closely related to psNTP9 enhances auxin transport and growth in Arabidopsis thaliana. Ectopic expression of psNTP9 can promote a more extensive root system architecture (RSA) in Arabidopsis thaliana. Transgenic Arabidopsis thaliana seedlings have longer primary roots, more lateral roots, and more and longer root hairs than wild-type plants. Transcriptomic analyses reveal gene expression changes in the transgenic plants that help account for their enhanced RSA and improved drought tolerance
physiological function
ectoapyrases (ecto-NTPDases) function to decrease levels of extracellular ATP and ADP in animals and plants. Ectopic expression of a pea ectoapyrase, psNTP9, enhances growth in Arabidopsis thaliana seedlings. Ectopic expression of psNTP9 can promote a more extensive root system architecture (RSA) in Arabidopsis thaliana. Transgenic Arabidopsis thaliana seedlings have longer primary roots, more lateral roots, and more and longer root hairs than wild-type plants. Transgenic Glycine max plants show improved RSA, growth and seed yield, and supports higher survival in response to drought
physiological function
isozyme AtAPY6 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant, demonstrating that the enzyme is also able to function as internal Golgi lumenal NDPases. Analysis of atapy6 mutants indicate a minor role in pollen development associated with abnormal exine patterning. An endoapyrase role for AtAPY6. The Arabidopsis apyrases family members have possible roles in regulating endomembrane NDP/NMP (nucleoside monophosphate) homoeostasis
physiological function
modulation of root skewing in Arabidopsis thaliana by apyrases and extracellular ATP. Skewing is induced by touch stimuli which the roots experience as they grow along the surface. Touch stimuli also induce the release of extracellular ATP (eATP) into the plant's extracellular matrix, and two apyrases (NTPDases) in Arabidopsis thaliana, APY1 and APY2, can help regulate the concentration of eATP. Exogenous application of ATP or ATPgammaS also increases skewing in wild-type roots, which can be blocked by co-incubation with a purinergic receptor antagonist. APY1 and, to a lesser extent, APY2 help control root skewing in Arabidopsis thaliana, and application of extracellular nucleotides also affects this directional growth response of roots. Treatment with ATP and ATPgammaS increases root skewing. Blocking auxin transport with 1-N-naphthylphthalamic acid (NPA) also increases root skewing
physiological function
mosquitoes infected by sporozoites, the infectious stage of malaria, bite more frequently than uninfected mosquitoes. One of the mechanisms underlying this behavioural change appears to be that the sporozoites decrease the activity of apyrase, an ADP-degrading enzyme that helps the mosquitoes to locate blood. Using the parasite Plasmodium berghei and the mosquito Anopheles gambiae, it is confirmed that sporozoite infection alters the hostseeking behaviour of mosquitoes by making them more likely to refeed after a first blood meal, and that apyrase activity is one of the mechanisms of the increased biting persistence and motivation of infectious mosquitoes. Apyrase activity decreases as the sporozoite load increases, and mosquitoes with lower apyrase activity take up less blood
physiological function
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occlusion of vein grafts (VGs) after bypass surgery due to thrombosis and intimal hyperplasia (IH) is a major clinical problem. Apyrases are enzymes that scavenge extracellular ATP and ADP and promote adenosine formation at sites of vascular injury and hence have potential to inhibit vein graft pathology. Recombinant soluble apyrase APT102 inhibits thrombosis and intimal hyperplasia in vein grafts without adversely affecting hemostasis or re-endothelialization. Effects of recombinant soluble human apyrase, APT102, on platelets, smooth muscle cells (SMCs), and endothelial cells (ECs) in vitro and thrombosis and IH in murine VGs from C57BL/6J male mice, overview. While potently inhibiting ADP-induced platelet aggregation and VG thrombosis, APT102 does not impair surgical hemostasis. APT102 does not directly inhibit SMC or EC proliferation, but significantly attenuates the effects of ATP on SMC and EC proliferation. APT102 significantly inhibits SMC migration, but does not inhibit EC migration, which may be mediated, at least in part, by inhibition of SMC, but not EC, migration by adenosine. At 4 weeks after surgery, IH is significantly less in VGs of APT102-treated mice than in control VGs. APT102 significantly inhibit cell proliferation in VGs, but does not inhibit re-endothelialization
physiological function
the Arabidopsis apyrases family members have possible roles in regulating endomembrane NDP/NMP (nucleoside monophosphate) homoeostasis
physiological function
Arabidopsis thaliana ecotype Columbia, CS907
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ectoapyrases (ecto-NTPDases) function to decrease levels of extracellular ATP and ADP in animals and plants. Ectopic expression of a pea ectoapyrase, psNTP9, enhances growth in Arabidopsis thaliana seedlings and the overexpression of the two Arabidopsis apyrases most closely related to psNTP9 enhances auxin transport and growth in Arabidopsis thaliana. Ectopic expression of psNTP9 can promote a more extensive root system architecture (RSA) in Arabidopsis thaliana. Transgenic Arabidopsis thaliana seedlings have longer primary roots, more lateral roots, and more and longer root hairs than wild-type plants. Transcriptomic analyses reveal gene expression changes in the transgenic plants that help account for their enhanced RSA and improved drought tolerance
-
physiological function
Arabidopsis thaliana ecotype Columbia, CS907
-
ectoapyrases (ect-NTPDases) function to decrease levels of extracellular ATP and ADP in animals and plants. Ectopic expression of a pea ectoapyrase, psNTP9, enhances growth in Arabidopsis thaliana seedlings and the overexpression of the two Arabidopsis apyrases most closely related to psNTP9 enhances auxin transport and growth in Arabidopsis thaliana. Ectopic expression of psNTP9 can promote a more extensive root system architecture (RSA) in Arabidopsis thaliana. Transgenic Arabidopsis thaliana seedlings have longer primary roots, more lateral roots, and more and longer root hairs than wild-type plants. Transcriptomic analyses reveal gene expression changes in the transgenic plants that help account for their enhanced RSA and improved drought tolerance
-
additional information
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
additional information
immune sera that recognize specifically the B domain of NTPDase 1 are produced against synthetic peptides (LbB1LJ (residues 82-103, RERFKRIEPGLSSFATDQEGAK) and LbB2LJ (residues 102-121, AKQSLAGLLRFAEKAVPRSY) synthetic peptides belong to the N- and C-terminal portions, respectively) derived from this domain. The polyclonal antibodies have effective anti-leishmanial effect, reducing significantly in vitro promastigotes growth (21-25%), an antiproliferative effect is also demonstrated by immune sera produced against recombinant r-pot B domain, and two other synthetic peptides (potB1LJ and potB2LJ). In addition, using these biomolecules in ELISA technique, IgG1 and IgG2 subclasses reactivities of either healthy dogs or infected by Leishmania infantum and classified clinically as asymptomatic, oligosymptomatic and symptomatic are tested. The peptides have have high identity with their Leishmnia infantum NTPDase 1 counterparts. Analysis of distinct IgG1 and IgG2 seropositivities patterns suggest antibody subclasses binding epitopes along B domain for protection against infection, indicating this domain as a tool for prophylactic and immunotherapeutic investigations
additional information
immune sera that recognize specifically the B domain of NTPDase 1 are produced against synthetic peptides (LbB1LJ and LbB2LJ) derived from this domain. The polyclonal antibodies have effective anti-leishmanial effect, reducing significantly in vitro promastigotes growth (21-25%), an antiproliferative effect is also demonstrated by immune sera produced against recombinant r-pot B domain, and two other synthetic peptides (potB1LJ and potB2LJ). The LbB1LJ (residues 82-103, RERFKRIEPGLSSFATDQEGAK) and LbB2LJ (residues 102-121, AKQSLAGLLRFAEKAVPRSY) synthetic peptides belong to the N- and C-terminal portions, respectively, from conserved B domain (82-121) of Leishmania braziliensis NTPDase 1 (UniProt ID A4H7X3), and have high identity with their Leishmnia infantum NTPDase 1 counterparts. In addition, using these biomolecules in ELISA technique, IgG1 and IgG2 subclasses reactivities of either healthy dogs or infected by Leishmania infantum and classified clinically as asymptomatic, oligosymptomatic and symptomatic are tested. Analysis of distinct IgG1 and IgG2 seropositivities patterns suggest antibody subclasses binding epitopes along B domain for protection against infection, indicating this domain as a tool for prophylactic and immunotherapeutic investigations
additional information
-
the transcript abundance of seven intrinsic Arabidopsis apyrase genes, AtAPY1, AtAPY2, AtAPY3, AtAPY4, AtAPY5, AtAPY6, and AtAPY7, is not altered by the overexpression of exogenous PeAPY2
additional information
-
immune sera that recognize specifically the B domain of NTPDase 1 are produced against synthetic peptides (LbB1LJ and LbB2LJ) derived from this domain. The polyclonal antibodies have effective anti-leishmanial effect, reducing significantly in vitro promastigotes growth (21-25%), an antiproliferative effect is also demonstrated by immune sera produced against recombinant r-pot B domain, and two other synthetic peptides (potB1LJ and potB2LJ). The LbB1LJ (residues 82-103, RERFKRIEPGLSSFATDQEGAK) and LbB2LJ (residues 102-121, AKQSLAGLLRFAEKAVPRSY) synthetic peptides belong to the N- and C-terminal portions, respectively, from conserved B domain (82-121) of Leishmania braziliensis NTPDase 1 (UniProt ID A4H7X3), and have high identity with their Leishmnia infantum NTPDase 1 counterparts. In addition, using these biomolecules in ELISA technique, IgG1 and IgG2 subclasses reactivities of either healthy dogs or infected by Leishmania infantum and classified clinically as asymptomatic, oligosymptomatic and symptomatic are tested. Analysis of distinct IgG1 and IgG2 seropositivities patterns suggest antibody subclasses binding epitopes along B domain for protection against infection, indicating this domain as a tool for prophylactic and immunotherapeutic investigations
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trimer
-
or dimer, of isoforms with molecular masses of 88000, 82000, 79000, 68000, or 67000 Da
?
-
x * 68000, SDS-PAGE
?
-
x * 50000, about, isozymes APY1 and APY2, SDS-PAGE
?
x * 52000, recombinant protein with His-tag, SDS-PAGE
?
x * 80000, protein with green fluorescent protein tag, SDS-PAGE
?
-
x * 49000, about, sequence calculation
?
x * 36932, sequence calculation, x * 50000, about, recombinant enzyme, SDS-PAGE
?
x * 62000, recombinant soluble His-tagged secreted NTPDase2 extracellular domain, SDS-PAGE
?
x * 53773, calculated from amino acid sequence
?
-
x * 47689, calculated from amino acid sequence
?
-
x * 48000, SDS-PAGE
-
?
-
x * 47689, calculated from amino acid sequence
-
?
x * 54650, deduced from gene sequence
?
x * 58950, deduced from gene sequence
?
x * 70000, deduced from gene sequence
?
x * 54650, calculated from amino acid sequence
?
x * 67000, recombinant, secreted isozyme I, SDS-PAGE
?
-
x * 65000-90000, glycosilated protein, x * 48000, deglycosilated protein, SDS-PAGE
?
-
x * 36989, isoform APY6, calculated from amino acid sequence
?
-
x * 48748, isoform APY5, calculated from amino acid sequence
?
-
x * 49765, isoform APY4, calculated from amino acid sequence
?
-
x * 50004, isoform APY9, calculated from amino acid sequence
?
-
x * 50032, isoform APY8, calculated from amino acid sequence
?
-
x * 50062, isoform APY10, calculated from amino acid sequence
?
-
x * 50077, isoform APY7, calculated from amino acid sequence
?
x * 79000, glycosylated form, SDS-PAGE, x * 59800, unglycosylated mature form, calculated
?
x * 88000, 82000, 79000, 68000, or 67000, SDS-PAGE
?
-
x * 36015-54540, TaAPY6, sequence calculation
?
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x * 46446-49036, TaAPY3-2, sequence calculation
?
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x * 46720-47258, TaAPY3-4, sequence calculation
?
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x * 48910-50034, TaAPY2, sequence calculation
?
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x * 49178-49979, TaAPY3-3, sequence calculation
?
-
x * 49209-54652, TaAPY5, sequence calculation
?
-
x * 49471-49555, TaAPY3-1, sequence calculation
?
-
x * 52225-52261, TaAPY1, sequence calculation
?
-
x * 77472-77557, TaAPY7, sequence calculation
?
x * 58000, SDS-PAGE, x * 69000, deduced from gene sequence
dimer
-
crosslinking experiments
dimer
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2 * 70000-80000, SDS-PAGE
dimer
-
or trimer, of isoforms with molecular masses of 88000, 82000, 79000, 68000, or 67000 Da
monomer
-
1 * 60200, SDS-PAGE
monomer
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1 * 50000, SDS-PAGE
monomer
-
x * 79400, glycosylated enzyme, SDS-PAGE, x * 33000, deglycosylated enzyme, SDS-PAGE
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
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
additional information
-
GS52 apyrase structure modeling of apo-form and tertiary complex with the nonhydrolyzable ATP analogue AMPPNP and cofactor Ca2+, overview
additional information
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the enzyme contains five apyrase conserved regions
additional information
comparisons of predicted isozyme tertiary structure, N-terminal Edman sequence analysis and mass spectrometry, overview
additional information
comparisons of predicted isozyme tertiary structure, N-terminal Edman sequence analysis and mass spectrometry, overview
additional information
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comparisons of predicted isozyme tertiary structure, N-terminal Edman sequence analysis and mass spectrometry, overview
additional information
comparisons of predicted isozyme tertiary structures, N-terminal Edman sequence analysis and mass spectrometry, overview
additional information
comparisons of predicted isozyme tertiary structures, N-terminal Edman sequence analysis and mass spectrometry, overview
additional information
-
comparisons of predicted isozyme tertiary structures, N-terminal Edman sequence analysis and mass spectrometry, overview
additional information
-
detection of bands of 95000, 80000, 60000 Da by antibody
additional information
structure comparison and molecular modelling, evolutionary structural relationships, overview
additional information
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structure comparison and molecular modelling, evolutionary structural relationships, overview
additional information
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identification of ACR regions in residues 40-454 possibly involved in metal binding, sequence comparison, and structure analysis and modeling, overview
additional information
structure comparison and molecular modelling
additional information
-
structure comparison and molecular modelling
additional information
structure comparison and molecular modelling, evolutionary structural relationships, overview
additional information
-
structure comparison and molecular modelling, evolutionary structural relationships, overview
additional information
-
three-dimensional structure, overview
additional information
-
TaAPY1, three-dimensional structure, overview
additional information
-
TaAPY2, three-dimensional structure, overview
additional information
-
TaAPY3-1 three-dimensional structure, overview
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D209A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
E182A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
Q216A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
S214A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
C10S
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112% of wild-type ATPase activity, 105% of wild-type ADPase activity, residue responsible for dimer formation
C10S/C501S
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148% of wild-type ATPase activity, 133% of wild-type ADPase activity
C10S/C501S/C509S
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79% of wild-type ATPase activity, 77% of wild-type ADPase activity
C10S/C509S
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103% of wild-type ATPase activity, 99% of wild-type ADPase activity
C501S
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130% of wild-type ATPase activity, 130% of wild-type ADPase activity, site of modification by p-chloromercuriphenylsulfonic acid
C501S/C509S
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138% of wild-type ATPase activity, 134% of wild-type ADPase activity
C509S
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148% of wild-type ATPase activity, 155% of wild-type ADPase activity
E159A
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site-directed mutagenesis, inactive mutant
N168A
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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
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site-directed mutagenesis, inactive mutant
R122A
-
site-directed mutagenesis, inactive mutant
W384A
-
site-directed mutagenesis, inactive mutant
A75S
the Km value for ADP of the isoform APY2 mutant is decreased compared to the wild type enzyme, while the Km value for ATP is substantially increased. The mutant shows higher specific acitivity for ADP than ATP
S63A
the ratio of the velocity of ATP/ADP hydrolysis is higher for the isoform MP67 mutant (approximately 1) compared to the wild type enzyme
E174A
site-directed mutagenesis, inactive mutant
K257M
site-directed mutagenesis
Y409F
site-directed mutagenesis
Y413F
site-directed mutagenesis
E493G
the mutant of isoform NTPDase1 shows conversion of ATP/ADP specificity compared to the wild type enzyme
R492G
the mutant of isoform NTPDase1 shows conversion of ATP/ADP specificity compared to the wild type enzyme
R492G/E493G
the mutant of isoform NTPDase1 shows conversion of ATP/ADP specificity compared to the wild type enzyme
additional information
AtAPY4 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
additional information
AtAPY4 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
additional information
AtAPY4 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
additional information
AtAPY4 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
additional information
AtAPY4 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
additional information
AtAPY4 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. The ability to recover mannose in cell wall extracts of the DELTAynd1DELTAgda1 dKO mutant probably reflects the activity of the apyrase with respect to the substrate GDP (derived from lumenal GDP-mannose)
additional information
AtAPY6 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. Construction of atapy6 mutants. dKO mutants lacking both isozymes AtAPY6 and AtAPY7 produce relatively normal plants but with low male fertility from collapsed pollen which further results in reduced seed set. Synergistic effects observed in atapy6atapy7 double mutant
additional information
AtAPY6 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. Construction of atapy6 mutants. dKO mutants lacking both isozymes AtAPY6 and AtAPY7 produce relatively normal plants but with low male fertility from collapsed pollen which further results in reduced seed set. Synergistic effects observed in atapy6atapy7 double mutant
additional information
AtAPY6 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. Construction of atapy6 mutants. dKO mutants lacking both isozymes AtAPY6 and AtAPY7 produce relatively normal plants but with low male fertility from collapsed pollen which further results in reduced seed set. Synergistic effects observed in atapy6atapy7 double mutant
additional information
AtAPY6 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. Construction of atapy6 mutants. dKO mutants lacking both isozymes AtAPY6 and AtAPY7 produce relatively normal plants but with low male fertility from collapsed pollen which further results in reduced seed set. Synergistic effects observed in atapy6atapy7 double mutant
additional information
AtAPY6 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. Construction of atapy6 mutants. dKO mutants lacking both isozymes AtAPY6 and AtAPY7 produce relatively normal plants but with low male fertility from collapsed pollen which further results in reduced seed set. Synergistic effects observed in atapy6atapy7 double mutant
additional information
AtAPY6 is able to complement the growth defect phenotype of the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. Construction of atapy6 mutants. dKO mutants lacking both isozymes AtAPY6 and AtAPY7 produce relatively normal plants but with low male fertility from collapsed pollen which further results in reduced seed set. Synergistic effects observed in atapy6atapy7 double mutant
additional information
generation of apy1 single knockout (APY1 KO) seedlings by RNAi. Treatment of R2-4A seedlings with estradiol induces 70% suppression of APY1 expression in the null background of APY2 and results in shortened roots with swollen root tips
additional information
generation of apy1 single knockout (APY1 KO) seedlings by RNAi. Treatment of R2-4A seedlings with estradiol induces 70% suppression of APY1 expression in the null background of APY2 and results in shortened roots with swollen root tips
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant reveals that AtAPY3 exhibits relatively weak complementation compared with other members of this clade. The AtAPY3 construct is the least able to recover cell wall mannose, reflecting the reduced growth phenotype
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant reveals that AtAPY3 exhibits relatively weak complementation compared with other members of this clade. The AtAPY3 construct is the least able to recover cell wall mannose, reflecting the reduced growth phenotype
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant reveals that AtAPY3 exhibits relatively weak complementation compared with other members of this clade. The AtAPY3 construct is the least able to recover cell wall mannose, reflecting the reduced growth phenotype
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant reveals that AtAPY3 exhibits relatively weak complementation compared with other members of this clade. The AtAPY3 construct is the least able to recover cell wall mannose, reflecting the reduced growth phenotype
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant reveals that AtAPY3 exhibits relatively weak complementation compared with other members of this clade. The AtAPY3 construct is the least able to recover cell wall mannose, reflecting the reduced growth phenotype
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant reveals that AtAPY3 exhibits relatively weak complementation compared with other members of this clade. The AtAPY3 construct is the least able to recover cell wall mannose, reflecting the reduced growth phenotype
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. AtAPY5 is able to complement the growth defect phenotype of the mutant. The proportion of mannose in cell wall extracts significantly increases in all the complemented strains with the AtAPY5 construct resulting in near wild-type levels
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. AtAPY5 is able to complement the growth defect phenotype of the mutant. The proportion of mannose in cell wall extracts significantly increases in all the complemented strains with the AtAPY5 construct resulting in near wild-type levels
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. AtAPY5 is able to complement the growth defect phenotype of the mutant. The proportion of mannose in cell wall extracts significantly increases in all the complemented strains with the AtAPY5 construct resulting in near wild-type levels
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. AtAPY5 is able to complement the growth defect phenotype of the mutant. The proportion of mannose in cell wall extracts significantly increases in all the complemented strains with the AtAPY5 construct resulting in near wild-type levels
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. AtAPY5 is able to complement the growth defect phenotype of the mutant. The proportion of mannose in cell wall extracts significantly increases in all the complemented strains with the AtAPY5 construct resulting in near wild-type levels
additional information
heterologous expression of the clade II Arabidopsis apyrase members (AtAPY3-6) in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant. AtAPY5 is able to complement the growth defect phenotype of the mutant. The proportion of mannose in cell wall extracts significantly increases in all the complemented strains with the AtAPY5 construct resulting in near wild-type levels
additional information
when clade I Arabidopsis apyrases are expressed in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant, both AtAPY1 and AtAPY2 are able to complement the growth phenotype compared to the yeast mutant harbouring the empty vector
additional information
when clade I Arabidopsis apyrases are expressed in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant, both AtAPY1 and AtAPY2 are able to complement the growth phenotype compared to the yeast mutant harbouring the empty vector
additional information
when clade I Arabidopsis apyrases are expressed in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant, both AtAPY1 and AtAPY2 are able to complement the growth phenotype compared to the yeast mutant harbouring the empty vector
additional information
when clade I Arabidopsis apyrases are expressed in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant, both AtAPY1 and AtAPY2 are able to complement the growth phenotype compared to the yeast mutant harbouring the empty vector
additional information
when clade I Arabidopsis apyrases are expressed in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant, both AtAPY1 and AtAPY2 are able to complement the growth phenotype compared to the yeast mutant harbouring the empty vector
additional information
when clade I Arabidopsis apyrases are expressed in the DELTAynd1DELTAgda1 dKO Saccharomyces cerevisiae mutant, both AtAPY1 and AtAPY2 are able to complement the growth phenotype compared to the yeast mutant harbouring the empty vector
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
-
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
additional information
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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
additional information
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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
additional information
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
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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
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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
additional information
construction of hCD39 transgene expressing CD39Tg mice from C57BL/6 wild-type expressing human CD39, hCD39 transgene expression in CD39Tg mice reduces ischemia-induced acute renal injury, but exacerbates chronic renal injury. In comparison with wild-type littermates, hCD39 transgenic mice are protected from acute renal injury at 24 hours, but have increased renal fibrosis at 4 weeks post-ischemia-reperfusion injury (IRI), hCD39 transgene expression is localized to the vascular endothelium at baseline and does not affect total renal nucleotide and nucleoside levels during ischemia. But hCD39 transgene is more widespread at 4 weeks post-IRI and is associated with higher renal adenosine levels at 4 weeks post-IRI compared with wild-type littermates
additional information
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construction of hCD39 transgene expressing CD39Tg mice from C57BL/6 wild-type expressing human CD39, hCD39 transgene expression in CD39Tg mice reduces ischemia-induced acute renal injury, but exacerbates chronic renal injury. In comparison with wild-type littermates, hCD39 transgenic mice are protected from acute renal injury at 24 hours, but have increased renal fibrosis at 4 weeks post-ischemia-reperfusion injury (IRI), hCD39 transgene expression is localized to the vascular endothelium at baseline and does not affect total renal nucleotide and nucleoside levels during ischemia. But hCD39 transgene is more widespread at 4 weeks post-IRI and is associated with higher renal adenosine levels at 4 weeks post-IRI compared with wild-type littermates
additional information
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following intratracheal inoculation of A/J mice, none of the Lpg1905 mutants is able to restore virulence to an lpg1905 mutant during lung infection
additional information
purified recombinant LicNTPDase-2 is covalently immobilized onto a fused silica capillary tube to create an immobilized capillary enzyme reactor (ICER) based on LicNTPDase-2(LicNTPDase-2-ICER), development of a label-free online screening method, evaluation of the activity and stability of the enzyme by the multidimensional LicNTPDase-2-ICER method, overview
additional information
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purified recombinant LicNTPDase-2 is covalently immobilized onto a fused silica capillary tube to create an immobilized capillary enzyme reactor (ICER) based on LicNTPDase-2(LicNTPDase-2-ICER), development of a label-free online screening method, evaluation of the activity and stability of the enzyme by the multidimensional LicNTPDase-2-ICER method, overview
additional information
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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
additional information
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under cold stress, PeAPY2-overexpressing transgenic plants maintain plasma membrane integrity and show reduced cold-elicited electrolyte leakage compared with wild-type plants. These responses probably result from efficient plasma membrane repair via vesicular trafficking. Transgenic plants show accelerated endocytosis and exocytosis during cold stress and recovery. Low doses of extracellular ATP accelerate vesicular trafficking, but high extracellular ATP inhibit trafficking and reduce cell viability. The transcript abundance of seven intrinsic Arabidopsis apyrase genes, AtAPY1, AtAPY2, AtAPY3, AtAPY4, AtAPY5, AtAPY6, and AtAPY7, is not altered by the overexpression of exogenous PeAPY2
additional information
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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
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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
additional information
efficient PiggyBac-mediated transposition of the recombinant soluble enzymes, method overview. Transfected cells secrete an enzymatically active wild-type soluble NTPDase1/CD39
additional information
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mutational analysis of residues involved in catalysis, overview
additional information
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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
additional information
development of a two-dimensional array ATP/ADP sensitive image sensor with a uniform distribution of chemically immobilized apyrase, immobilization via the two different methods 3-APTES and CEST, analysis method evaluation and optimization, overview. The surface of the ATP image sensor with 3-APTES method is polluted with the precipitation and shows heterogeneity. The ATP image sensor with CEST method shows a clear surface as well as that before the immobilization of apyrase. Potential disributions, and durability analysis
additional information
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immobilization of the enzyme in a two-step process: in the first step, carboxyl group on polyethylene terephthalate (PET) surface is activated by the crosslinker 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride, and in the second step, the enzyme is covalently attached to the activated carboxyl group, method development and evaluation. Kinetic study of NTPDase immobilization and its effect of hemocompatibility on PET, overview. Surface morphology and chemical composition of the unmodified and modified PET films are examined using scanning electron microscope with energy dispersive X-ray spectroscopy analysis
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Bacillus subtilis gene ytkD cloned and expressed in Escherichia coli
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CD39, expression in COS-7 cells
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cloning of His-tagged wild-type and mutant NTPDase8s in Escherichia coli strain DH5alpha and stable expression in HEK293 cell plasma membranes
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
DNA and amino acid sequence determination and analysis of isozyme II, phylogenetic analysis
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
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ectopic expression of pea ectoapyrase, psNTP9, in Arabidopsis thaliana ecotype Columbia, CS907, and Glycine max genotype Williams 82
expressed as a thioredoxin-His-tagged fusion protein in Escherichia coli BL21 cells
expressed in Arabidopsis thaliana, fused to a SNAP-(O6-alkylguanine-DNA alkyltransferase)-tag, green fluorescent protein or yellow fluorescent protein
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta cells
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expressed in Escherichia coli Rosetta pLysS cells
expressed in HEK-293T cells and COS-7 cells
expression in cells of chinese hamster ovaries
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expression in COS-7 cells
expression in Spodoptera frugiperda Sf9 cells using the baculovirus infection system
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expression of a His6-tagged Lpg1905 using plasmid pRSET:lpg1905 in Escherichia coli BL21(DE3) C41 strain
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expression of GS52 in Escherichia coli and in tabacco
expression of His-tagged enzyme in Escherichia coli
expression of mutant hu-ck ACR1,5 chimeric enzymes in HEK-293 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
expression of the C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
expression of the full-length protein and a soluble form without the transmembrane domain near the N-terminus in HEK-293 cells
gene APY1, real-time PCR enzyme expression analysis
gene APY2, real-time PCR enzyme expression analysis by RNAi
gene AtAPY1, sequence comparisons and phylogenetic analysis
gene AtAPY2, sequence comparisons and phylogenetic analysis
gene AtAPY3, sequence comparisons and phylogenetic analysis, apyrase members AtAPY3, AtAPY4 and AtAPY5 are recurrent tandem gene duplications on chromosome 1, recombinant expression of C-terminally YFP-tagged isozyme AtAPY3 in Arabidopsis thaliana resulting in an internal punctate signal with minimal cis-Golgi marker overlap
gene AtAPY4, sequence comparisons and phylogenetic analysis, apyrase members AtAPY3, AtAPY4 and AtAPY5 are recurrent tandem gene duplications on chromosome 1, recombinant expression of YFP-tagged isozyme AtAPY4 in Arabidopsis thaliana in the cis-Golgi of rosette leaves
gene AtAPY5, apyrase members AtAPY3, AtAPY4 and AtAPY5 are recurrent tandem gene duplications on chromosome 1, sequence comparisons and phylogenetic analysis
gene AtAPY6, sequence comparisons and phylogenetic analysis. recombinant expression of C-terminally YFP-tagged isozyme AtAPY6 in Arabidopsis thaliana in colocalization with the endoplasmic reticulum marker
gene BjAPY2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, cloning and analysis of the promoter region of BjAPY2 reveal that there are several types of motifs in the promoter region, including the light and temperature responsive elements, quantitative real-time PCR analysis
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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)
gene encoding ATPDase2, DNA and amino acid sequence determination and analysis, sequence comparison
gene Entpd1, recombinant expression in COS-7 cells
gene Entpd2, recombinant expression in COS-7 cells
gene Entpd3, recombinant expression in COS-7 cells
gene Entpd8, recombinant expression in COS-7 cells
gene Entpdase1, the sequence is constructed comprising the rat coding sequence from Thr38 to Thr476, which removes the nucleotides coding for the hydrophobic regions at the N- and C-terminals, and fused to a sequence coding for the rat IL-2-derived leader sequence that allows the enzyme to be secreted. Donor constructs are driven by EF1A promoter. Stable recombinant expression of wild-type and mutant enzymes in C6 glioma cells by the non-viral transfection with transposon PiggyBac-based method, real-time PCR expression analysis, transfected cells secrete an enzymatically active wild-type soluble NTPDase1/CD39
gene LALP70 cloned into the mammalian expression vector pCl-Neo, expression on the surface of COS-7 cells
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gene LMJF_15_0030, sequence comparisons
gene PeAPY2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, ectopic expression in Arabidopsis thaliana leading to enhanced cold tolerance based on root growth measurements and survival rates. PeAPY2 overexpression enhances vesicular trafficking in Arabidopsis thaliana roots
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genes Entpd1, 2, 3, 5, 6, and Entpd8
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GS50 and GS52 expression analysis, overexpression of the ecto-apyrase in Lotus japonicus increasing the level of rhizobial infection and enhanced nodulation
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isoforms APY4, APY5 and APY6 are expressed in Escherichia coli BL21(DE3) cells with thioredoxin-tag, His6-tag and S-tag
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isozymes APY1 and APY2, expression analysis, APY1 and APY2 promoter activity is high under conditions that induced stomata opening
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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
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
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recombinant expression of human enzyme in C57BL/6 mice
recombinant expression of LicNTPDase-2
recombinant expression of the isozyme in COS-7 cells
recombinant expression of the mutant NTPDase1 ECD DELTAMIL in Escherichia coli in soluble form and refolding to the active state
TaAPY1, gene IDs TraesCS4A01G131300.1, TraesCS4B01G173300.1, and TraesCS4D01G175400.1, three different gene copies, sequence analysis and comparisons. Gene structure and conserved motif analysis of the APY genes in wheat, overview
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TaAPY2, gene IDs TraesCS2A01G102100.1, TraesCS2B01G119200.1, and TraesCS2D01G101500.1, three different gene copies, sequence analysis and comparisons. Gene structure and conserved motif analysis of the APY genes in wheat, overview
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TaAPY3-1, gene IDs TraesCS5A01G532000.1, TraesCS4B01G363700.1, and TraesCS4D01G357100.1, three different gene copies, sequence analysis and comparisons. Gene structure and conserved motif analysis of the APY genes in wheat, overview
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TaAPY3-2, gene IDs TraesCS5A01G547700.1, TraesCS4B01G381600.1, and TraesCS4D01G357100.1, three different gene copies, sequence analysis and comparisons. Gene structure and conserved motif analysis of the APY genes in wheat, overview
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TaAPY3-3, gene IDs TraesCS7A01G160900.1, TraesCS2B01G025000.1, and TraesCS2D01G020200.2, three different gene copies, sequence analysis and comparisons. Gene structure and conserved motif analysis of the APY genes in wheat, overview
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TaAPY3-4, gene IDs TraesCS7B01G004400.2, TraesCS7D01G100000.1, and TraesCSU01G095000.1, three different gene copies, sequence analysis and comparisons. Gene structure and conserved motif analysis of the APY genes in wheat, overview
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TaAPY5, gene IDs TraesCS6A01G105900.1, TraesCS7B01G178800.1, and TraesCS7D01G280900.1, three different gene copies, sequence analysis and comparisons. Gene structure and conserved motif analysis of the APY genes in wheat, overview
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TaAPY6, gene IDs TraesCS6A01G105900.2, TraesCS6B01G135200.1, and TraesCS6D01G094400.2, three different gene copies, sequence analysis and comparisons. Gene structure and conserved motif analysis of the APY genes in wheat, overview
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TaAPY7, gene IDs TraesCS1A01G288900.1, TraesCS1B01G298200.1, and TraesCS1D01G287900.1, three different gene copies, sequence analysis and comparisons. Gene structure and conserved motif analysis of the APY genes in wheat, overview
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expressed in HEK-293T cells and COS-7 cells
expressed in HEK-293T cells and COS-7 cells
expression in COS-7 cells
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expression in COS-7 cells
phylogenetic analysis
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