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(2'-pdA)AppppA + H2O
?
-
cleavage to produce ATP and 2'-deoxyadenylated AMP rather than 2'-deoxyadenylated ATP + AMP occurs with a ratio of 60:40 with the wild-type enzyme and the mutant enzymes R54Q, E58D and E125Q. With the mutants R54Q, E58D and E125Q, releasing ATP is increased to 70% of total hydrolysis. Activity of mutants E55Q, E59D and E59Q is to low to be detected
-
-
?
2'-deoxyadenosine adenosine tetraphosphate + H2O
ATP + 2'-dAMP + 2'-dATP + AMP
-
-
80% dAMP, 20% AMP
?
5',5''-diadenosine pentaphosphate + H2O
ATP + ADP
-
42% of the activity with 5',5''-diadenosine tetraphosphate
-
?
5',5''-diadenosine tetraphosphate + H2O
ATP + AMP
-
-
-
?
5',5'-diadenosine hexaphosphate + H2O
2 ATP
diadenosine hexaphosphate is efficiently hydrolysed to ATP only at pH 7.5 with 20 mM Mg2+
-
-
?
5',5'-diadenosine pentaphosphate + H2O
ATP + ADP
-
-
-
?
5',5'-diadenosine tetraphosphate + H2O
ATP + AMP
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
A-5'-p-alpha,beta,alpha',beta'-bis(oxymethylene)p-5'-A + H2O
2 alpha,beta-oxymethylene-ADP
adenosine-5'-pentaphospho-5'-guanosine + H2O
?
-
-
-
?
adenosine-5'-tetraphospho-5'-guanosine + H2O
?
-
-
-
?
Ap6A + H2O
Ap5 + AMP
-
-
-
-
?
Ap6A + H2O
ATP + ATP
-
7% of the activity with Ap4A
-
-
?
betabeta'-methyleneoxy-Ap4A + H2O
AMP + beta,gamma-methyleneoxy-ATP
di-2,6-diaminopurine beta-D-ribofuranoside tetraphosphate + H2O
?
-
-
-
-
?
diadenosine 5',5''''-P1,P4-tetraphosphate + H2O
AMP + ATP
diadenosine 5',5''-P1,P4-tetraphosphate + H2O
ATP + AMP
diadenosine 5',5''-P1,P5-pentaphosphate + H2O
adenosine 5'-tetraphosphate + AMP
-
-
-
-
?
diadenosine 5',5''-P1,P5-pentaphosphate + H2O
ATP + ADP
-
19% of the activity with Ap4A
-
-
?
diadenosine 5',5'-P1,P4-tetraphosphate + H2O
ATP + AMP
diadenosine 5',5'-P1,P4-tetraphosphate + H2O
ATP + AMP + ?
key enzyme controlling the in vivo concentration of diadenosine 5',5'-P1,P4 tetraphosphate (Ap4A) - an important signaling molecule involved in regulation of DNA replication and repair, signaling in stress response and apoptosis
-
-
?
diadenosine 5',5'-P1,P5-pentaphosphate + H2O
ATP + ADP
-
-
-
?
diguanosine 5',5'-P1,P4-tetraphosphate + H2O
GTP + GMP
-
-
-
?
DNA + H2O
?
-
poor substrate
-
-
?
P1,P3-bis(5'-adenosyl)triphosphate + H2O
AMP + ADP
-
-
-
?
P1,P3-bis(5'-guanosyl) triphosphate + H2O
?
-
poor substrate
-
-
?
P1,P4-bis(5'-(2'-deoxy)adenosyl) tetraphosphate + H2O
?
-
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
AMP + ATP
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
P1,P4-bis(5'-uridyl) tetraphosphate + H2O
UTP + UMP
P1,P4-bis(5'-xanthosyl) tetraphosphate + H2O
XTP + XMP
P1,P5-bis(5'-adenosyl) pentaphosphate + H2O
ADP + ATP
P1,P5-bis(5'-adenosyl) pentaphosphate + H2O
ATP + ADP
-
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
AMP + adenosine 5'-tetraphosphate
P1,P6-bis(5'-adenosyl) hexaphosphate + H2O
2 ATP
P1,P6-bis(5'-adenosyl) hexaphosphate + H2O
ATP
-
-
-
?
p4A + H2O
ATP + phosphate
-
14% of the activity with Ap4A
-
-
?
p5A + H2O
ATP + diphosphate
-
29% of the activity with Ap4A
-
-
?
RNA + H2O
?
-
poor substrate
-
-
?
additional information
?
-
2-oxo-dATP + H2O
?
less efficient hydrolysis compared to 8-oxo-dGTP
-
-
?
2-oxo-dATP + H2O
?
less efficient hydrolysis compared to 8-oxo-dGTP
-
-
?
5',5'-diadenosine tetraphosphate + H2O
ATP + AMP
-
-
-
?
5',5'-diadenosine tetraphosphate + H2O
ATP + AMP
best substrate
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
the enzyme does not show a strong preference for 8-oxo-dGTP and is able to hydrolyze unmodified dATP and dGTP with comparable efficiency
-
-
?
8-oxo-dGTP + H2O
8-oxo-dGMP + diphosphate
the enzyme does not show a strong preference for 8-oxo-dGTP and is able to hydrolyze unmodified dATP and dGTP with comparable efficiency
-
-
?
A-5'-p-alpha,beta,alpha',beta'-bis(oxymethylene)p-5'-A + H2O
2 alpha,beta-oxymethylene-ADP
-
diadenosine polyphosphate analog
-
-
?
A-5'-p-alpha,beta,alpha',beta'-bis(oxymethylene)p-5'-A + H2O
2 alpha,beta-oxymethylene-ADP
-
diadenosine polyphosphate analog
-
-
?
Ap4A + H2O
?
-
-
-
-
?
betabeta'-methyleneoxy-Ap4A + H2O
AMP + beta,gamma-methyleneoxy-ATP
-
diadenosine polyphosphate analog
-
-
?
betabeta'-methyleneoxy-Ap4A + H2O
AMP + beta,gamma-methyleneoxy-ATP
-
diadenosine polyphosphate analog
-
-
?
dATP + H2O
?
-
-
-
?
dGTP + H2O
?
-
-
-
?
diadenosine 5',5''''-P1,P4-tetraphosphate + H2O
AMP + ATP
-
-
-
?
diadenosine 5',5''''-P1,P4-tetraphosphate + H2O
AMP + ATP
-
-
-
?
diadenosine 5',5''-P1,P4-tetraphosphate + H2O
ATP + AMP
-
-
-
-
?
diadenosine 5',5''-P1,P4-tetraphosphate + H2O
ATP + AMP
-
-
-
-
?
diadenosine 5',5''-P1,P4-tetraphosphate + H2O
ATP + AMP
-
-
-
-
?
diadenosine 5',5''-P1,P4-tetraphosphate + H2O
ATP + AMP
-
-
-
-
?
diadenosine 5',5'-P1,P4-tetraphosphate + H2O
ATP + AMP
-
-
-
-
?
diadenosine 5',5'-P1,P4-tetraphosphate + H2O
ATP + AMP
-
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
best substrate
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
Lupinus sp.
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
Lupinus sp.
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
Lupinus sp.
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
Lupinus sp.
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
possible role as reporter for luciferase gene
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
Scenedesmus sp.
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
stress response
-
?
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
AMP + ATP
-
-
-
?
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
AMP + ATP
-
in the presence of Mn2+, PrpA hydrolyzes Ap4A mainly into AMP and ATP, whereas in the presence of Co2+ PrpA hydrolyzes Ap4A into two molecules of ADP, reaction of EC 3.6.1.41
-
?
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
AMP + ATP
-
in the presence of Mn2+, PrpA hydrolyzes Ap4A mainly into AMP and ATP, whereas in the presence of Co2+ PrpA hydrolyzes Ap4A into two molecules of ADP, reaction of EC 3.6.1.41
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
ir
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-uridyl) tetraphosphate + H2O
UTP + UMP
-
-
-
?
P1,P4-bis(5'-uridyl) tetraphosphate + H2O
UTP + UMP
-
-
-
?
P1,P4-bis(5'-xanthosyl) tetraphosphate + H2O
XTP + XMP
-
-
-
?
P1,P4-bis(5'-xanthosyl) tetraphosphate + H2O
XTP + XMP
-
-
-
?
P1,P4-bis(5'-xanthosyl) tetraphosphate + H2O
XTP + XMP
-
-
-
?
P1,P5-bis(5'-adenosyl) pentaphosphate + H2O
ADP + ATP
-
-
-
?
P1,P5-bis(5'-adenosyl) pentaphosphate + H2O
ADP + ATP
-
-
-
-
?
P1,P5-bis(5'-adenosyl) pentaphosphate + H2O
ADP + ATP
Lupinus sp.
-
-
-
?
P1,P5-bis(5'-adenosyl) pentaphosphate + H2O
ADP + ATP
-
-
-
?
P1,P5-bis(5'-adenosyl) pentaphosphate + H2O
ADP + ATP
Scenedesmus sp.
-
-
-
?
P1,P5-bis(5'-adenosyl) pentaphosphate + H2O
ADP + ATP
-
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
AMP + adenosine 5'-tetraphosphate
-
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
AMP + adenosine 5'-tetraphosphate
-
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
AMP + adenosine 5'-tetraphosphate
-
-
-
?
P1,P6-bis(5'-adenosyl) hexaphosphate + H2O
2 ATP
-
-
-
?
P1,P6-bis(5'-adenosyl) hexaphosphate + H2O
2 ATP
-
-
-
?
P1,P6-bis(5'-adenosyl) hexaphosphate + H2O
2 ATP
Scenedesmus sp.
-
-
-
?
P1,P6-bis(5'-adenosyl) hexaphosphate + H2O
2 ATP
-
-
-
?
additional information
?
-
enzyme hydrolyses bis(5'-nucleosidyl) polyphosphates (Np4-6N') in such a way that a nucleosidyl triphosphate is always one of the products
-
-
?
additional information
?
-
-
enzyme hydrolyses bis(5'-nucleosidyl) polyphosphates (Np4-6N') in such a way that a nucleosidyl triphosphate is always one of the products
-
-
?
additional information
?
-
-
no activity with Ap3A
-
-
?
additional information
?
-
Apf always produces an NTP product, with substrate preference depending on pH and divalent ion
-
-
?
additional information
?
-
-
Apf always produces an NTP product, with substrate preference depending on pH and divalent ion
-
-
?
additional information
?
-
enzyme is a diphosphoinositol polyphosphate phosphohydrolase, EC 3.6.1.52
-
-
?
additional information
?
-
PrpA exhibits a phosphatase activity towards p-nitrophenyl phosphate, tyrosine phosphopeptide and tyrosine-phosphorylated protein and a weak hydrolase activity towards ATP
-
-
?
additional information
?
-
PrpA exhibits a phosphatase activity towards p-nitrophenyl phosphate, tyrosine phosphopeptide and tyrosine-phosphorylated protein and a weak hydrolase activity towards ATP
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5',5'-diadenosine tetraphosphate + H2O
ATP + AMP
-
-
-
?
diadenosine 5',5'-P1,P4-tetraphosphate + H2O
ATP + AMP
diadenosine 5',5'-P1,P4-tetraphosphate + H2O
ATP + AMP + ?
key enzyme controlling the in vivo concentration of diadenosine 5',5'-P1,P4 tetraphosphate (Ap4A) - an important signaling molecule involved in regulation of DNA replication and repair, signaling in stress response and apoptosis
-
-
?
diadenosine 5',5'-P1,P5-pentaphosphate + H2O
ATP + ADP
-
-
-
?
diguanosine 5',5'-P1,P4-tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
additional information
?
-
diadenosine 5',5'-P1,P4-tetraphosphate + H2O
ATP + AMP
-
-
-
-
?
diadenosine 5',5'-P1,P4-tetraphosphate + H2O
ATP + AMP
-
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
Lupinus sp.
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
Lupinus sp.
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
Lupinus sp.
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
Lupinus sp.
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
possible role as reporter for luciferase gene
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
Scenedesmus sp.
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
-
-
?
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
ATP + AMP
-
stress response
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
ir
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
P1,P4-bis(5'-guanosyl)tetraphosphate + H2O
GTP + GMP
-
-
-
?
additional information
?
-
enzyme hydrolyses bis(5'-nucleosidyl) polyphosphates (Np4-6N') in such a way that a nucleosidyl triphosphate is always one of the products
-
-
?
additional information
?
-
-
enzyme hydrolyses bis(5'-nucleosidyl) polyphosphates (Np4-6N') in such a way that a nucleosidyl triphosphate is always one of the products
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cd2+
no activity in the presence of 1.0 mM Cd2+, weak enzyme activation at 5 mM (4.% compared to 1.5 mM Mn2+)
Ca2+
no activity in the presence of 1.0 and 5.0 mM Ca2+
Ca2+
-
activated by physiological concentration, maximal activity at 2 mM
Co2+
-
divalent cation required, 20% of maximal activity in presence of 1 mM Co2+
Co2+
the enzyme is dependent on divalent cations
Co2+
about 50% of the activity with Mn2+. In the presence of Mn2+, PrpA hydrolyzes P1,P3-bis(5'-adenosyl)tetraphosphate mainly into AMP and ATP, whereas in the presence of Co2+, PrpA hydrolyzes P1,P3-bis(5'-adenosyl)tetraphosphate into two molecules of ADP, reaction of EC 3.6.1.17
Co2+
5 mM, 42% of the activity with Mg2+
Mg2+
no activity in the presence of 1 mM Mg2+, 9.1% relative activity at 5 mM Mg2+ compared to 1.5 mM Mn2+
Mg2+
-
divalent cation required, maximal activity in presence of 3-5 mM Mg2+
Mg2+
-
in the presence of Mn2+ the Km value for diadenosine 5',5''-P1,P4-tetraphosphate is roughly two orders of magnitude tighter than in the presence of Mg2+
Mg2+
the enzyme is dependent on divalent cations, preferred cation, best at 3-10 mM
Mg2+
-
maximum activity at 3 mM
Mg2+
-
required, optimum concentration 3-10 mM
Mg2+
-
activated by physiological concentration, maximal activity at 2 mM
Mg2+
-
5 mM MgCl2 included in assay medium
Mg2+
-
5 mM MgCl2 included in assay medium
Mg2+
-
required, maximum activity at 1 mM
Mg2+
best activator, maximum activity at 5 mM
Mg2+
-
required, maximum activity at 5 mM
Mn2+
enzyme preferentially hydrolyses diadenosine 5',5'-P1P4 tetraphosphate in the form of a Mn2+ complex at a concentration of 1.5 mM, 37.7% relative activity at 0.5 mM compared to 1.5 mM Mn2+
Mn2+
-
able to substitute for Mg2+, 70% of activity at equal metal ion concentration
Mn2+
-
divalent cation required, 20% of maximal activity in presence of 0.1 mM Mn2+
Mn2+
-
in the presence of Mn2+ the Km value for diadenosine 5',5''-P1,P4-tetraphosphate is roughly two orders of magnitude tighter than in the presence of Mg2+
Mn2+
the enzyme is dependent on divalent cations
Mn2+
-
activated by physiological concentration, maximal activity at 0.1 mM
Mn2+
-
required, maximum activity at 0.5 mM
Mn2+
best activator. In the presence of Mn2+, PrpA hydrolyzes Ap4A mainly into AMP and ATP, whereas in the presence of Co2+ PrpA hydrolyzes P1,P3-bis(5'-adenosyl)tetraphosphate into two molecules of ADP, reaction of EC 3.6.1.17
Mn2+
5 mM, 11% of the activity with Mg2+
Mn2+
-
required, more effective than Mg2+
Mn2+
-
15% of maximum activity
Zn2+
enzyme exhibit residual activity in the presence of 1.5 mM Zn2+ ions, 28.4% relative activity at 5 mM Zn2+ compared to 1.5 mM Mn2+
Zn2+
-
divalent cation required, 20% of maximal activity in presence of 0.05 mM Mn2+
Zn2+
-
strongest activation
Zn2+
the enzyme is dependent on divalent cations, high activity
Zn2+
5 mM, 2% of the activity with Mg2+
Zn2+
Scenedesmus sp.
-
strongest activation
additional information
no activation by Cu2+, Fe2+, Ni2+ or Ca2+
additional information
-
no activation by Cu2+, Fe2+, Ni2+ or Ca2+
additional information
no activation by Ca2+
additional information
-
no activation by Ca2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,2,3,4-tetra(adenosine-5'-O-phospho)erythritol
-
-
1,2,3,4-tetra(adenosine-5'-O-phosphorothio)erythritol
1,2,3-tri(adenosine-5'-O-phosphorothio)glycerol
1,3-di(adenosine-5'-O-phospho)-2-phospho-glycerol
-
-
1,3-di(adenosine-5'-O-phospho)-2-phosphorothio-glycerol
1,3-di(adenosine-5'-O-phospho)glycerol
-
-
1,4-di(adenosine-5'-O-phospho)erythritol
1,4-di(adenosine-5'-O-phosphorothio)erythritol
1,4-dihydroxy-5,8-bis[(4-methylphenyl)amino]anthracene-9,10-dione
NSC86169
2-((8-hydroxy-4-(4-methyl-2-sulfoanilino)-9,10-dioxo-9,10-dihydro-1-anthracenyl)amino)-5-methylbenzenesulfonic acid
NSC51531, competitive inhibitor
2-[2-[(4-aminophenyl)amino]-6-phenylpyrimidin-4-yl]phenol
NSC232476
5-hydroxy-1,4-bis[(4-methylphenyl)amino]anthracene-9,10-dione
NSC300513
5-methyl-2-[[4-(methylamino)-9,10-dioxo-9,10-dihydroanthracen-1-yl]amino]benzenesulfonate
NSC401611
A-5'-p-alpha,beta,alpha',beta'-bis(oxymethylene)p-5'-A
A-5'-p-beta,beta'-methyleneoxy-p-5'-A
adenosine 5'-tetraphosphate
di(adenosine-5'-O-phosphorothio)-di(adenosine-5'-phospho)pentaerythritol
-
-
diadenosine 5',5'''-P1,P4-tetraphosphate
-
-
diadenosine triphosphate
-
competitive, also phosphonate analogues of the substance
fructose-6-phosphate
-
slight inhibition
glycerol phosphate
20 mM, 46.1% residual activity
guanosine 5'-tetraphosphate
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,4,5,6-pentaphosphate
competitive
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
competitive
inositol 4-butyl-1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
competitive
iodoacetic acid
10 mM, 58.8% residual activity
Ionic strength
-
significant inhibition at high ionic strength
-
N-ethylmaleimide
1 mM, 73.8% residual activity
perylene-3,4,9,10-tetracarboxylic acid
NSC89768
phosphate
-
inhibitory above 30 mM
trisodium phosphate
20 mM, 24.8% residual activity
uridine 5'-tetraphosphate
-
Ki in nanomolar range
additional information
NSC113427, NSC133815, and NSC305522, do not exhibit any enzyme inhibition at concentrations in excess of 0.1 mM
-
1,2,3,4-tetra(adenosine-5'-O-phosphorothio)erythritol
-
-
1,2,3,4-tetra(adenosine-5'-O-phosphorothio)erythritol
-
-
1,2,3-tri(adenosine-5'-O-phosphorothio)glycerol
-
-
1,2,3-tri(adenosine-5'-O-phosphorothio)glycerol
-
-
1,3-di(adenosine-5'-O-phospho)-2-phosphorothio-glycerol
-
-
1,3-di(adenosine-5'-O-phospho)-2-phosphorothio-glycerol
-
-
1,4-di(adenosine-5'-O-phospho)erythritol
-
-
1,4-di(adenosine-5'-O-phospho)erythritol
-
-
1,4-di(adenosine-5'-O-phosphorothio)erythritol
-
-
1,4-di(adenosine-5'-O-phosphorothio)erythritol
-
-
A-5'-p-alpha,beta,alpha',beta'-bis(oxymethylene)p-5'-A
-
competitive inhibitor
A-5'-p-alpha,beta,alpha',beta'-bis(oxymethylene)p-5'-A
-
competitive inhibitor
A-5'-p-beta,beta'-methyleneoxy-p-5'-A
-
competitive inhibitor
A-5'-p-beta,beta'-methyleneoxy-p-5'-A
-
competitive inhibitor
adenosine 5'-tetraphosphate
-
Ki in nanomolar range
adenosine 5'-tetraphosphate
-
competitive
adenosine 5'-tetraphosphate
-
competitive; Ki in nanomolar range
adenosine 5'-tetraphosphate
-
Ki: 0.006 mM
adenosine 5'-tetraphosphate
-
Ki in nanomolar range
adenosine 5'-tetraphosphate
-
competitive; Ki in nanomolar range
adenosine 5'-tetraphosphate
-
Ki in nanomolar range
ADP
-
-
AMP
-
-
ATP
-
competitive
Ca2+
-
Ki: 0.3 mM
Ca2+
-
50% inhibition at 0.025 mM
EDTA
-
-
EDTA
5 mM, 13.2% residual activity
F-
-
non-competitive
fluoride
-
-
fluoride
-
non-competitive, strong inhibition, reversible
fluoride
-
non-competitive, strong inhibition, reversible
fluoride
fluoride potently inhibits diadenosine tetraphosphate hydrolysis in the presence of Mg2+, whereas it is ineffective in the presence of Zn2+, because inhibition involves a specific, MgF3--containing transition state analogue complex, overview
fluoride
-
non-competitive, strong inhibition, reversible
fluoride
Lupinus sp.
-
inhibition at 0.003 mM F-, Ki: 0.006 mM
fluoride
Lupinus sp.
-
non-competitive, strong inhibition, reversible
fluoride
-
Ki: 0.05; non-competitive
fluoride
-
non-competitive, strong inhibition, reversible
fluoride
Scenedesmus sp.
-
-
GDP
-
competitive
GMP
-
competitive
GTP
-
competitive
guanosine 5'-tetraphosphate
-
Ki in nanomolar range
guanosine 5'-tetraphosphate
-
Ki: 0.01 mM
guanosine 5'-tetraphosphate
-
Ki in nanomolar range
guanosine 5'-tetraphosphate
-
Ki in nanomolar range
Zn2+
-
-
Zn2+
-
non-competitive, reversible with EDTA, very strong inhibitor
Zn2+
-
reversible with fructose-2,6-diphosphate
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.3846
2-oxo-dATP
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37°C
0.0006 - 0.003
5',5''-diadenosine tetraphosphate
0.015
5',5'-diadenosine hexaphosphate
pH 7.5, 20 mM Mg2+
0.009 - 0.012
5',5'-diadenosine tetraphosphate
0.0986
8-oxo-dGTP
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37°C
0.098
Ap5A
-
pH 7.4, 37°C
0.1143
dATP
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37°C
0.182
dGTP
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37°C
0.007
diadenosine 5',5''''-P1,P4-tetraphosphate
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37°C
0.005 - 0.407
diadenosine 5',5''-P1,P4-tetraphosphate
0.002 - 0.0025
diadenosine 5',5'-P1,P4-tetraphosphate
0.0007 - 0.054
P1,P4-bis(5'-adenosyl) tetraphosphate
0.14
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 8.0, 50°C, presence of 1 mM Mn2+
0.001 - 1.03
P1,P4-bis(5'-guanosyl) tetraphosphate
0.01 - 0.011
P1,P4-bis(5'-uridyl) tetraphosphate
0.016 - 0.018
P1,P4-bis(5'-xanthosyl) tetraphosphate
0.183
P1,P5-bis(5'-adenosyl) pentaphosphate
in 50 mM Tris-HCl, 100 mM KCl, 5 mM MgCl2, pH 7.6, at 25°C
0.19
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 8.0, 50°C, presence of 1 mM Mn2+
0.089
P1,P6-bis(5'-adenosyl) hexaphosphate
in 50 mM Tris-HCl, 100 mM KCl, 5 mM MgCl2, pH 7.6, at 25°C
additional information
additional information
-
0.0006
5',5''-diadenosine tetraphosphate
wild-type, pH 7.5, 22°C
0.0008
5',5''-diadenosine tetraphosphate
mutant P133F, pH 7.5, 22°C
0.003
5',5''-diadenosine tetraphosphate
mutant P133A, pH 7.5, 22°C
0.009
5',5'-diadenosine tetraphosphate
pH 6.5, 1 mm Zn2+
0.012
5',5'-diadenosine tetraphosphate
pH 7.5, 20 mM Mg2+
0.0041
Ap4A
-
mutant enzyme H38K
0.0053
Ap4A
-
mutant enzyme E52Q
0.0058
Ap4A
-
mutant enzyme E103Q
0.0058
Ap4A
-
mutant enzyme H38G
0.007
Ap4A
-
pH 7.8, 25°C
0.0079
Ap4A
-
mutant enzyme E56Q
0.0088
Ap4A
-
wild-type enzyme
0.011
Ap4A
-
mutant enzyme Y27A
0.013
Ap4A
-
mutant enzyme K36M
0.015
Ap4A
-
mutant enzyme K79M
0.016
Ap4A
-
mutant enzyme Y27D
0.02
Ap4A
-
mutant enzyme K81M
0.033
Ap4A
-
mutant enzyme Y76A/Y121A
0.038
Ap4A
-
pH 7.4, 37°C
0.059
Ap4A
-
mutant enzyme Y76A
0.073
Ap4A
-
mutant enzyme H31A
0.075
Ap4A
-
mutant enzyme Y121A
0.11
Ap4A
-
mutant enzyme H31V
0.12
Ap4A
-
pH 8.0, 25°C, mutant enzyme E55Q fusion protein containing and N-terminal extension of Gly-Pro-Leu-Gly-Ser
0.14
Ap4A
-
mutant enzyme K83M
0.5
Ap4A
-
pH 8.0, 25°C, mutant enzyme E122Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys
0.5
Ap4A
-
pH 8.0, 25°C, mutant enzyme R54Q fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys
0.96
Ap4A
-
pH 8.0, 25°C, mutant enzyme E58D fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys
1.4
Ap4A
-
pH 8.0, 25°C, mutant enzyme E125Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser
2
Ap4A
-
pH 8.0, 25°C, mutant enzyme E58Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys
2.5
Ap4A
-
pH 8.0, 25°C, wild-type enzyme
5.9
Ap4A
-
pH 8.0, 25°C, mutant enzyme E59Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys
10
Ap4A
-
pH 8.0, 25°C, mutant enzyme E59D, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys
0.005
diadenosine 5',5''-P1,P4-tetraphosphate
-
presence of 5.0 mM MnCl2, pH 7.5, 22°C
0.0073
diadenosine 5',5''-P1,P4-tetraphosphate
-
presence of 1.5 mM MnCl2, pH 7.5, 22°C
0.0093
diadenosine 5',5''-P1,P4-tetraphosphate
-
presence of 3.0 mM MnCl2, pH 7.5, 22°C
0.326
diadenosine 5',5''-P1,P4-tetraphosphate
-
presence of 3.0 mM MgCl2, pH 7.5, 22°C
0.333
diadenosine 5',5''-P1,P4-tetraphosphate
-
presence of 5.0 mM MgCl2, pH 7.5, 22°C
0.407
diadenosine 5',5''-P1,P4-tetraphosphate
-
presence of 1.5 mM MgCl2, pH 7.5, 22°C
0.002
diadenosine 5',5'-P1,P4-tetraphosphate
-
-
0.0025
diadenosine 5',5'-P1,P4-tetraphosphate
-
-
0.0007
P1,P4-bis(5'-adenosyl) tetraphosphate
-
-
0.0019
P1,P4-bis(5'-adenosyl) tetraphosphate
-
-
0.002
P1,P4-bis(5'-adenosyl) tetraphosphate
-
-
0.005
P1,P4-bis(5'-adenosyl) tetraphosphate
-
-
0.007
P1,P4-bis(5'-adenosyl) tetraphosphate
-
-
0.01
P1,P4-bis(5'-adenosyl) tetraphosphate
-
in presence of Mg2+
0.04
P1,P4-bis(5'-adenosyl) tetraphosphate
-
in presence of Zn2+
0.054
P1,P4-bis(5'-adenosyl) tetraphosphate
in 50 mM Tris-HCl, 100 mM KCl, 5 mM MgCl2, pH 7.6, at 25°C
0.001
P1,P4-bis(5'-guanosyl) tetraphosphate
-
-
0.002
P1,P4-bis(5'-guanosyl) tetraphosphate
-
-
0.002
P1,P4-bis(5'-guanosyl) tetraphosphate
-
-
0.005
P1,P4-bis(5'-guanosyl) tetraphosphate
-
-
1.03
P1,P4-bis(5'-guanosyl) tetraphosphate
-
-
0.01
P1,P4-bis(5'-uridyl) tetraphosphate
-
-
0.011
P1,P4-bis(5'-uridyl) tetraphosphate
-
-
0.016
P1,P4-bis(5'-xanthosyl) tetraphosphate
-
-
0.018
P1,P4-bis(5'-xanthosyl) tetraphosphate
-
-
additional information
additional information
kinetics strongly depend on pH and cation, overview
-
additional information
additional information
-
kinetics strongly depend on pH and cation, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.51
2-oxo-dATP
in 5 0mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37°C
0.013 - 0.08
5',5''-diadenosine tetraphosphate
4
5',5'-diadenosine hexaphosphate
pH 7.5, 20 mM Mg2+
13 - 43
5',5'-diadenosine tetraphosphate
0.58
8-oxo-dGTP
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37°C
0.37
dATP
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37°C
0.53
dGTP
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37°C
27
diadenosine 5',5''''-P1,P4-tetraphosphate
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37°C
0.68 - 3.25
diadenosine 5',5''-P1,P4-tetraphosphate
2.5 - 3.6
P1,P4-bis(5'-adenosyl) tetraphosphate
0.055
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 8.0, 50°C, presence of 1 mM Mn2+
1.4
P1,P5-bis(5'-adenosyl) pentaphosphate
in 50 mM Tris-HCl, 100 mM KCl, 5 mM MgCl2, pH 7.6, at 25°C
0.035
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 8.0, 50°C, presence of 1 mM Mn2+
0.2
P1,P6-bis(5'-adenosyl) hexaphosphate
in 50 mM Tris-HCl, 100 mM KCl, 5 mM MgCl2, pH 7.6, at 25°C
0.013
5',5''-diadenosine tetraphosphate
mutant P133F, pH 7.5, 22°C
0.042
5',5''-diadenosine tetraphosphate
wild-type, pH 7.5, 22°C
0.08
5',5''-diadenosine tetraphosphate
mutant P133A, pH 7.5, 22°C
13
5',5'-diadenosine tetraphosphate
pH 7.5, 20 mM Mg2+
43
5',5'-diadenosine tetraphosphate
pH 6.5, 1 mM Zn2+
0.00024
Ap4A
-
mutant enzyme E56Q
0.00031
Ap4A
-
pH 8.0, 25°C, mutant enzyme E59Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys
0.005
Ap4A
-
pH 8.0, 25°C, mutant enzyme E55Q fusion protein containing and N-terminal extension of Gly-Pro-Leu-Gly-Ser
0.0052
Ap4A
-
mutant enzyme E52Q
0.011
Ap4A
-
pH 8.0, 25°C, mutant enzyme E59D, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys
0.16
Ap4A
-
mutant enzyme K79M
0.29
Ap4A
-
pH 8.0, 25°C, mutant enzyme E125Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser
0.6
Ap4A
-
mutant enzyme K83M
0.75
Ap4A
-
mutant enzyme E103Q
1.1
Ap4A
-
mutant enzyme Y76A/Y121A
2
Ap4A
-
mutant enzyme Y76A
2.1
Ap4A
-
mutant enzyme K36M
3.7
Ap4A
-
pH 8.0, 25°C, mutant enzyme E58D fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys
4.2
Ap4A
-
pH 8.0, 25°C, mutant enzyme R54Q fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys
12
Ap4A
-
mutant enzyme H31A
14
Ap4A
-
mutant enzyme H31V
14
Ap4A
-
mutant enzyme Y121A
17.9
Ap4A
-
pH 8.0, 25°C, mutant enzyme E58Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys
20.4
Ap4A
-
pH 8.0, 25°C, mutant enzyme E122Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys
23
Ap4A
-
wild-type enzyme
26
Ap4A
-
mutant enzyme Y27A
29
Ap4A
-
mutant enzyme Y27D
30
Ap4A
-
mutant enzyme K81M
31
Ap4A
-
mutant enzyme H38G
31
Ap4A
-
mutant enzyme H38K
40.8
Ap4A
-
pH 8.0, 25°C, wild-type enzyme
0.68
diadenosine 5',5''-P1,P4-tetraphosphate
-
presence of 5.0 mM MnCl2, pH 7.5, 22°C
1.51
diadenosine 5',5''-P1,P4-tetraphosphate
-
presence of 3.0 mM MnCl2, pH 7.5, 22°C
1.6
diadenosine 5',5''-P1,P4-tetraphosphate
-
presence of 1.5 mM MnCl2, pH 7.5, 22°C
1.78
diadenosine 5',5''-P1,P4-tetraphosphate
-
presence of 1.5 mM MgCl2, pH 7.5, 22°C
2.24
diadenosine 5',5''-P1,P4-tetraphosphate
-
presence of 3.0 mM MgCl2, pH 7.5, 22°C
3.25
diadenosine 5',5''-P1,P4-tetraphosphate
-
presence of 5.0 mM MgCl2, pH 7.5, 22°C
2.5
P1,P4-bis(5'-adenosyl) tetraphosphate
in 50 mM Tris-HCl, 100 mM KCl, 5 mM MgCl2, pH 7.6, at 25°C
3.6
P1,P4-bis(5'-adenosyl) tetraphosphate
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.3
2-oxo-dATP
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37°C
5.9
8-oxo-dGTP
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37°C
3.3
dATP
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37°C
2.9
dGTP
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37°C
3900
diadenosine 5',5''''-P1,P4-tetraphosphate
in 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 20 mM NaCl, 1 mM dithiothreitol, 0.2 mg/ml bovine serum albumin, at 37°C
4.4 - 220
diadenosine 5',5''-P1,P4-tetraphosphate
46
P1,P4-bis(5'-adenosyl) tetraphosphate
in 50 mM Tris-HCl, 100 mM KCl, 5 mM MgCl2, pH 7.6, at 25°C
0.4
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 8.0, 50°C, presence of 1 mM Mn2+
7.6
P1,P5-bis(5'-adenosyl) pentaphosphate
in 50 mM Tris-HCl, 100 mM KCl, 5 mM MgCl2, pH 7.6, at 25°C
0.18
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 8.0, 50°C, presence of 1 mM Mn2+
2.2
P1,P6-bis(5'-adenosyl) hexaphosphate
in 50 mM Tris-HCl, 100 mM KCl, 5 mM MgCl2, pH 7.6, at 25°C
4.4
diadenosine 5',5''-P1,P4-tetraphosphate
-
presence of 1.5 mM MgCl2, pH 7.5, 22°C
6.9
diadenosine 5',5''-P1,P4-tetraphosphate
-
presence of 3.0 mM MgCl2, pH 7.5, 22°C
9.8
diadenosine 5',5''-P1,P4-tetraphosphate
-
presence of 5.0 mM MgCl2, pH 7.5, 22°C
140
diadenosine 5',5''-P1,P4-tetraphosphate
-
presence of 5.0 mM MnCl2, pH 7.5, 22°C
160
diadenosine 5',5''-P1,P4-tetraphosphate
-
presence of 3.0 mM MnCl2, pH 7.5, 22°C
220
diadenosine 5',5''-P1,P4-tetraphosphate
-
presence of 1.5 mM MnCl2, pH 7.5, 22°C
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0.031
1,2,3,4-tetra(adenosine-5'-O-phospho)erythritol
-
pH 7.6, 30°C
0.013 - 0.018
1,2,3,4-tetra(adenosine-5'-O-phosphorothio)erythritol
0.017 - 0.037
1,2,3-tri(adenosine-5'-O-phosphorothio)glycerol
0.066
1,3-di(adenosine-5'-O-phospho)-2-phospho-glycerol
-
pH 7.6, 30°C
0.025 - 0.032
1,3-di(adenosine-5'-O-phospho)-2-phosphorothio-glycerol
0.109
1,3-di(adenosine-5'-O-phospho)glycerol
-
pH 7.6, 30°C
0.0085 - 0.142
1,4-di(adenosine-5'-O-phospho)erythritol
0.00015 - 0.0015
1,4-di(adenosine-5'-O-phosphorothio)erythritol
0.00109
2-((8-hydroxy-4-(4-methyl-2-sulfoanilino)-9,10-dioxo-9,10-dihydro-1-anthracenyl)amino)-5-methylbenzenesulfonic acid
in 100 mM Tris-acetate, pH 7.7, 5 mM magnesium acetate, and 5% DMSO, at 25°C
0.005
2-[2-[(4-aminophenyl)amino]-6-phenylpyrimidin-4-yl]phenol
Ki about 0.005 mM, in 100 mM Tris-acetate, pH 7.7, 5 mM magnesium acetate, and 5% (v/v) DMSO, at 25°C
0.00289
5-methyl-2-[[4-(methylamino)-9,10-dioxo-9,10-dihydroanthracen-1-yl]amino]benzenesulfonate
in 100 mM Tris-acetate, pH 7.7, 5 mM magnesium acetate, and 5% (v/v) DMSO, at 25°C
0.0015 - 0.0025
A-5'-p-alpha,beta,alpha',beta'-bis(oxymethylene)p-5'-A
0.0021 - 0.0022
A-5'-p-beta,beta'-methyleneoxy-p-5'-A
0.00001
adenosine 5'-tetraphosphate
-
pH 7.8, 25°C
0.0037
di(adenosine-5'-O-phosphorothio)-di(adenosine-5'-phospho)pentaerythritol
-
pH 7.6, 30°C
0.01
guanosine 5'-tetraphosphate
-
-
0.00011
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,4,5,6-pentaphosphate
pH not specified in the publication, temperature not specified in the publication
0.00027
inositol 1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
pH not specified in the publication, temperature not specified in the publication
0.000023
inositol 4-butyl-1-[(phosphorylmethyl)phosphonic acid]-2,3,5,6-tetraphosphate
pH not specified in the publication, temperature not specified in the publication
0.013
1,2,3,4-tetra(adenosine-5'-O-phosphorothio)erythritol
-
pH 7.6, 30°C
0.018
1,2,3,4-tetra(adenosine-5'-O-phosphorothio)erythritol
-
pH 7.6, 30°C
0.017
1,2,3-tri(adenosine-5'-O-phosphorothio)glycerol
-
pH 7.6, 30°C
0.037
1,2,3-tri(adenosine-5'-O-phosphorothio)glycerol
-
pH 7.6, 30°C
0.025
1,3-di(adenosine-5'-O-phospho)-2-phosphorothio-glycerol
-
pH 7.6, 30°C
0.032
1,3-di(adenosine-5'-O-phospho)-2-phosphorothio-glycerol
-
pH 7.6, 30°C
0.0085
1,4-di(adenosine-5'-O-phospho)erythritol
-
pH 7.6, 30°C
0.142
1,4-di(adenosine-5'-O-phospho)erythritol
-
pH 7.6, 30°C
0.00015
1,4-di(adenosine-5'-O-phosphorothio)erythritol
-
pH 7.6, 30°C
0.0015
1,4-di(adenosine-5'-O-phosphorothio)erythritol
-
pH 7.6, 30°C
0.0015
A-5'-p-alpha,beta,alpha',beta'-bis(oxymethylene)p-5'-A
-
-
0.0025
A-5'-p-alpha,beta,alpha',beta'-bis(oxymethylene)p-5'-A
-
-
0.0021
A-5'-p-beta,beta'-methyleneoxy-p-5'-A
-
-
0.0022
A-5'-p-beta,beta'-methyleneoxy-p-5'-A
-
-
0.025
Ca2+
-
-
0.003
F-
-
pH 8.0, 25°C, wild-type enzyme
0.006
F-
-
pH 8.0, 25°C, mutant enzyme E59D, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys
0.007
F-
-
pH 8.0, 25°C, mutant enzyme E122Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys
0.02
F-
-
pH 8.0, 25°C, mutant enzyme E58Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys
0.05
F-
-
pH 8.0, 25°C, mutant enzyme E58D fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys
0.25
F-
-
pH 8.0, 25°C, mutant enzyme E125Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser
1
F-
-
pH 8.0, 25°C, mutant enzyme R54Q fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys
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E103Q
-
turnover-number for hydrolysis of Ap4A is 3.2% of that of the wild-type enzyme, KM-value is 66% of the wild-type value
E52Q
-
turnover-number for hydrolysis of Ap4A is 0.02% of that of the wild-type enzyme, KM-value is 60% of the wild-type value
E56Q
-
turnover-number for hydrolysis of Ap4A is 0.001% of that of the wild-type enzyme, KM-value is 90% of the wild-type value
H31A
-
turnover-number for hydrolysis of Ap4A is 52% of that of the wild-type enzyme, KM-value is 8.3fold higher than the KM-value of the wild-type enzyme
H31V
-
turnover-number for hydrolysis of Ap4A is 61% of that of the wild-type enzyme, KM-value is 12.5fold higher than the KM-value of the wild-type enzyme
H38G
-
turnover-number for hydrolysis of Ap4A is 135% of that of the wild-type enzyme, KM-value is 66% of the wild-type value
H38K
-
turnover-number for hydrolysis of Ap4A is 135% of that of the wild-type enzyme, KM-value is 47% of the wild-type value
K36M
-
turnover-number for hydrolysis of Ap4A is 9% of that of the wild-type enzyme, KM-value is 1.5fold higher than the KM-value of the wild-type enzyme
K79M
-
turnover-number for hydrolysis of Ap4A is 0.7% of that of the wild-type enzyme, KM-value is 1.7fold higher than the KM-value of the wild-type enzyme
K81M
-
turnover-number for hydrolysis of Ap4A is 130% of that of the wild-type enzyme, KM-value is 2.3fold higher than the KM-value of the wild-type enzyme
K83M
-
turnover-number for hydrolysis of Ap4A is 2.6% of that of the wild-type enzyme, KM-value is 15.9fold higher than the KM-value of the wild-type enzyme
Y121A
-
turnover-number for hydrolysis of Ap4A is 61% of that of the wild-type enzyme, KM-value is 8.5fold higher than the KM-value of the wild-type enzyme
Y27A
-
turnover-number for hydrolysis of Ap4A is 113% of that of the wild-type enzyme, KM-value is 1.25fold higher than the KM-value of the wild-type enzyme
Y27D
-
turnover-number for hydrolysis of Ap4A is 126% of that of the wild-type enzyme, KM-value is 1.8fold higher than the KM-value of the wild-type enzyme
Y76A
-
turnover-number for hydrolysis of Ap4A is 8.7% of that of the wild-type enzyme, KM-value is 6.7fold higher than the KM-value of the wild-type enzyme
Y76A/Y121A
-
turnover-number for hydrolysis of Ap4A is 4.8% of that of the wild-type enzyme, KM-value is 3.75fold higher than the KM-value of the wild-type enzyme
E58A
crystallization data
T70A
active site mutant, has no effect on platelet aggregation and secretion
E122Q
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 20% of the wild-type value, turnover-number is 50% of the wild-type value. 2.3fold reduction in sensitivity to fluoride
E125Q
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser. KM-value is 0.7% of the wild-type value, turnover-number is 56% of the wild-type value. Cleavage of (2'-pdA)AppppA to produce ATP and 2'-deoxyadenylated AMP rather than 2'-deoxyadenylated ATP + AMP as with wild-type enzyme, the ratio of ATP released is increased compared to wild-type. 83fold reduction in sensitivity to fluoride
E55Q
-
fusion protein containing and N-terminal extension of Gly-Pro-Leu-Gly-Ser. KM-value is 4.8% of the wild-type value, turnover-number is 0.01% of the wild-type value. Activity with (2'-pdA)AppppA is to low to be detected. More than 330fold reduction in sensitivity to fluoride
E58D
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 38.4% of the wild-type value, turnover-number is 9% of the wild-type value. Cleavage of (2'-pdA)AppppA to produce ATP and 2'-deoxyadenylated AMP rather than 2'-deoxyadenylated ATP + AMP as with wild-type enzyme, the ratio of ATP released is increased compared to wild-type. 16.7fold reduction in sensitivity to fluoride
E58Q
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 80% of the wild-type value, turnover-number is 43.9% of the wild-type value. 6.7fold reduction in sensitivity to fluoride
E59D
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 4fold higher than the wild-type value, turnover-number is 0.02% of the wild-type value. Activity with (2'-pdA)AppppA is to low to be detected. 2fold reduction in sensitivity to fluoride
E59Q
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. KM-value is 2.4fold higher than the wild-type value, turnover-number is 0.00076% of the wild-type value. Activity with (2'-pdA)AppppA is to low to be detected
R54Q
-
fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys. Cleavage of (2'-pdA)AppppA to produce ATP and 2'-deoxyadenylated AMP rather than 2'-deoxyadenylated ATP + AMP as with wild-type enzyme, the ratio of ATP released is increased compared to wild-type. 330fold reduction in sensitivity to fluoride
P133A
5fold increase in Km value
P133F
3fold decrease in kcat value
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Warner, A.H.; Finamore, F.J.
Isolation, purification, and characterization of P1,P4-diguanosine 5'-tetraphosphate asymmetrical-pyrophosphohydrolase from brine shrimp eggs
Biochemistry
4
1568-1575
1965
Artemia salina
brenda
Vallejo, C.G.; Sillero, M.A.G.; Sillero, A.
Diguanosinetetraphosphate guanosylhydrolase in Artemia salina
Biochim. Biophys. Acta
358
117-125
1974
Artemia salina
brenda
Lobaton, C.D.; Vallejo, C.G.; Sillero, A.; Sillero, M.A.G.
Diguanosinetetraphosphatase from rat liver: Activity on diadenosine tetraphosphate and inhibition by adenosine tetraphosphate
Eur. J. Biochem.
50
495-501
1975
Rattus norvegicus
brenda
Vallejo, C.G.; Lobaton, C.D.; Quintanilla, M.; Sillero, A.; Sillero, M.A.G.
Dinucleosidasetetraphosphatase in rat liver and Artemia salina
Biochim. Biophys. Acta
438
304-309
1976
Artemia salina, Rattus norvegicus
brenda
Moreno, A.; Lobaton, C.D.; Sillero, M.A.G.; Sillero, A.
Dinucleosidetetraphosphatase from Ehrlich ascites tumour cells: inhibition by adenosine, guanosine and uridine 5-tetraphosphates
Int. J. Biochem.
14
629-634
1982
Mus musculus
brenda
Cameselle, J.C.; Costas, M.J.; Sillero, M.A.G.; Sillero, A.
Bis-(5-guanosyl) tetraphosphatase in rat tissues
Biochem. J.
201
405-410
1982
Rattus norvegicus
brenda
Costas, M.J.; Cameselle, J.C.; Sillero, A.
Mitochondrial location of rat liver dinucleoside triphosphatase
J. Biol. Chem.
261
2064-2067
1986
Rattus norvegicus
brenda
Cameselle, J.C.; Costas, M.J.; Sillero, M.A.G.; Sillero, A.
Dinucleosidetetraphosphatase inhibition by Zn(II)
Biochem. Biophys. Res. Commun.
113
717-722
1983
Rattus norvegicus
brenda
Cameselle, J.C.; Costas, M.J.; Sillero, M.A.G.; Sillero, A.
Two low Km hydrolytic activities on dinucleoside 5',5'''-P1,P4-tetraphosphates in rat liver. Characterization as the specific dinucleoside tetraphosphatase and a phosphodiesterase-I-like enzyme
J. Biol. Chem.
259
2879-2885
1984
Rattus norvegicus
brenda
Costas, M.J.; Cameselle, J.C.
Binding of zinc (II) to beta-D-fructose 2,6-bisphosphate
Biochem. Biophys. Res. Commun.
143
206-211
1987
Rattus norvegicus
brenda
Hause, B.; Feussner, K.; Wasternack, C.
Nuclear location of a diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) hydrolase in tomato cells grown in suspension cultures
Bot. Acta
110
452-457
1997
Solanum lycopersicum
-
brenda
Maksel, D.; Guranowski, A.; Ilgoutz, S.; Moir, A.; Blackburn, M.G.; Gayler, K.R.
Cloning and expression of diadenosine 5',5'''-P1,P4-tetraphosphate hydrolase from Lupinus angustifolius L
Biochem. J.
329
313-319
1998
Lupinus sp.
brenda
McLennan, A.G.; Mayers, E.; Walker-Smith, I.; Chen, H.
Lanterns of firefly Photinus pyralis contain abundant diadenosine 5',5'''-P1,P4-tetraphosphate pyrophosphohydrolase activity
J. Biol. Chem.
270
3706-3709
1995
Photinus pyralis
brenda
Pinto, R.M.; Costas, M.J.; Fernandez, A.; Canales, J.; Garcia-Agundez, J.A.; Camselle, J.C.
Dinucleoside tetraphosphatase from human blood cells: Purification and characterization as a high specific activity enzyme recognized by an anti-rat tetraphosphatase antibody
FEBS Lett.
287
85-88
1991
Homo sapiens, Rattus norvegicus
brenda
Guranowski, A.
Fluoride is a strong specific inhibitor of (asymmetrical) Ap4A hydrolases
FEBS Lett.
262
205-208
1990
Bos taurus, Saccharomyces cerevisiae, Cucurbita pepo, Helianthus sp., Lupinus sp.
brenda
Lazewska, D.; Starzynska, E.; Guranowski, A.
Human placental (asymmetrical) diadenosine 5',5'''-P1,P4-tetraphosphate hydrolase: Purification to homogenity and some properties
Protein Expr. Purif.
4
45-51
1993
Homo sapiens
brenda
McLennan, A.G.; Mayers, E.; Hankin, S.; Thorne, N.M.; Prescott, M.; Powls, R.
The green alga Scenedesmus obliquus contains both diadenosine 5',5'''-P1,P4-tetraphosphate (asymmetrical) pyrophosphohyrolase and phosphorylase activities
Biochem. J.
300
183-189
1994
Chlorella vulgaris, Scenedesmus sp.
brenda
Guranowski, A.; Brown, P.; Ashton, P.A.; Blackburn, G.M.
Regiospecificity of the hydrolysis of diadenosine polyphosphates catalyzed by three specific pyrophosphohydrolases
Biochemistry
33
235-240
1994
Lupinus sp.
brenda
Feussner, K.; Guranowski, A.; Kostka, S.; Wasternack, C.
Diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) hydrolase from tomato (Lycopersicon esculentum cv. Lukullus): Purification, biochemical properties and behaviour during stress
Z. Naturforsch. C
51
477-486
1996
Solanum lycopersicum
brenda
Swarbrick, J.D.; Bashtannyk, T.; Maksel, D.; Pau, R.N.; Gayler, K.R.; Gooley, P.R.
1H, 13C and 15N backbone of the 19000 kDa diadenosine 5',5'''-P1,P4-tetraphosphate hydrolase from Lupinus angustifolius L.
J. Biomol. NMR
16
269-270
2000
Lupinus sp.
brenda
Robinson, A.K.; de la Pena C.E.; Barnes, L.D.
Isolation and charcterization of diadenosine tetraphosphate (Ap4A) hydrolase from Schizosaccharomyces pombe
Biochim. Biophys. Acta
1161
139-148
1993
Saccharomyces cerevisiae
brenda
Guranowski, A.; Galbas, M.; Hartmann, R.; Justesen, J.
Selective degradation of 2'-adenylated diadenosine tri- and tetraphosphates, Ap3A and Ap4A, by two specific human dinucleoside polyphosphate hydrolases
Arch. Biochem. Biophys.
373
218-224
2000
Homo sapiens
brenda
Maksel, D.; Gooley, P.R.; Swarbrick, J.D.; Guranowski, A.; Gange, C.; Blackburn, G.M.; Gayler, K.R.
Characterization of active-site residues in diadenosine tetraphosphate hydrolase from Lupinus angustifolius
Biochem. J.
357
399-405
2001
Lupinus angustifolius
brenda
Guranowski, A.; Starzynska, E.; McLennan, A.G.; Baraniak, J.; Stec, W.J.
Adenosine-5'-O-phosphorylated and adenosine-5'-O-phosphorothioylated polyols as strong inhibitors of (symmetrical) and (asymmetrical) dinucleoside tetraphosphatases
Biochem. J.
373
635-640
2003
Homo sapiens, Lupinus angustifolius
brenda
Abdelghany, H.M.; Gasmi, L.; Cartwright, J.L.; Bailey, S.; Rafferty, J.B.; McLennan, A.G.
Cloning, characterisation and crystallization of a diadenosine 5',5'''-P1,P4-tetraphosphate pyrophosphohydrolase from Caenorhabditis elegans
Biochim. Biophys. Acta
1550
27-36
2001
Caenorhabditis elegans
brenda
Abdelghany, H.M.; Bailey, S.; Blackburn, G.M.; Rafferty, J.B.; McLennan, A.G.
Analysis of the catalytic and binding residues of the diadenosine tetraphosphate pyrophosphohydrolase from Caenorhabditis elegans by site-directed mutagenesis
J. Biol. Chem.
278
4435-4439
2003
Caenorhabditis elegans
brenda
Minelli, A.; Allegrucci, C.; Liguori, L.; Ronquist, G.
Ecto-diadenosine polyphosphate hydrolase activity on human prostasomes
Prostate
51
1-9
2002
Homo sapiens
brenda
Swarbrick, J.D.; Buyya, S.; Gunawardana, D.; Gayler, K.R.; McLennan, A.G.; Gooley, P.R.
Structure and substrate-binding mechanism of human Ap4A hydrolase
J. Biol. Chem.
280
8471-8481
2005
Homo sapiens (P50583), Homo sapiens
brenda
Winward, L.; Whitfield, W.G.; Woodman, T.J.; McLennan, A.G.; Safrany, S.T.
Characterisation of a bis(5-nucleosyl)-tetraphosphatase (asymmetrical) from Drosophila melanogaster
Int. J. Biochem. Cell Biol.
39
943-954
2007
Drosophila melanogaster (Q4V6M1), Drosophila melanogaster
brenda
Szurmak, B.; Wyslouch-Cieszyeska, A.; Wszelaka-Rylik, M.; Bal, W.; Dobrzanska, M.
A diadenosine 5',5''-P1P4 tetraphosphate (Ap4A) hydrolase from Arabidopsis thaliana that is activated preferentially by Mn2+ ions
Acta Biochim. Pol.
55
151-160
2008
Arabidopsis thaliana (Q9C6Z2), Arabidopsis thaliana
brenda
Guranowski, A.; Starzynska, E.; Pietrowska-Borek, M.; Rejman, D.; Blackburn, G.M.
Novel diadenosine polyphosphate analogs with oxymethylene bridges replacing oxygen in the polyphosphate chain: potential substrates and/or inhibitors of Ap4A hydrolases
FEBS J.
276
1546-1553
2009
Homo sapiens, Lupinus angustifolius
brenda
Jeyakanthan, J.; Kanaujia, S.P.; Nishida, Y.; Nakagawa, N.; Praveen, S.; Shinkai, A.; Kuramitsu, S.; Yokoyama, S.; Sekar, K.
Free and ATP-bound structures of Ap4A hydrolase from Aquifex aeolicus V5
Acta Crystallogr. Sect. D
66
116-124
2010
Aquifex aeolicus (O66548), Aquifex aeolicus
brenda
Branson, K.M.; Mertens, H.D.; Swarbrick, J.D.; Fletcher, J.I.; Kedzierski, L.; Gayler, K.R.; Gooley, P.R.; Smith, B.J.
Discovery of inhibitors of lupin diadenosine 5,5-P1,P4-tetraphosphate hydrolase by virtual screening
Biochemistry
48
7614-7620
2009
Lupinus angustifolius (O04841)
brenda
Vasilenko, N.; Moshynskyy, I.; Zakhartchouk, A.
SARS coronavirus protein 7a interacts with human Ap4A-hydrolase
Virol. J.
7
31
2010
Homo sapiens (P50583), Homo sapiens
brenda
Arczewska, K.D.; Baumeier, C.; Kassahun, H.; Sengupta, T.; Bjoras, M.; Kusmierek, J.T.; Nilsen, H.
Caenorhabditis elegans NDX-4 is a MutT-type enzyme that contributes to genomic stability
DNA Repair
10
176-187
2011
Caenorhabditis elegans (Q9U2M7), Caenorhabditis elegans, Caenorhabditis elegans Bristol N2 (Q9U2M7)
brenda
Wu, M.; Chong, L.S.; Capolicchio, S.; Jessen, H.J.; Resnick, A.C.; Fiedler, D.
Elucidating diphosphoinositol polyphosphate function with nonhydrolyzable analogues
Angew. Chem. Int. Ed. Engl.
53
7192-7197
2014
Homo sapiens (O95989)
brenda
Ge, H.; Chen, X.; Yang, W.; Niu, L.; Teng, M.
Crystal structure of wild-type and mutant human Ap4A hydrolase
Biochem. Biophys. Res. Commun.
432
16-21
2013
Homo sapiens (P50583), Homo sapiens
brenda
Barta, M.L.; Lovell, S.; Sinclair, A.N.; Battaile, K.P.; Hefty, P.S.
Chlamydia trachomatis CT771 (nudH) is an asymmetric Ap4A hydrolase
Biochemistry
53
214-224
2014
Chlamydia trachomatis
brenda
Osman, W.; Endo, S.; Oh-Hashi, K.; Kitamura, Y.; Kitade, Y.
Molecular characterization and mutational analysis of recombinant diadenosine 5',5''-P1,P4-tetraphosphate hydrolase from Plasmodium falciparum
Biol. Pharm. Bull.
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1191-1196
2012
Plasmodium falciparum (C0H4F3), Plasmodium falciparum
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Albright, R.A.; Chang, W.C.; Robert, D.; Ornstein, D.L.; Cao, W.; Liu, L.; Redick, M.E.; Young, J.I.; De La Cruz, E.M.; Braddock, D.T.
NPP4 is a procoagulant enzyme on the surface of vascular endothelium
Blood
120
4432-4440
2012
Homo sapiens (Q9Y6X5)
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Sasaki, M.; Takegawa, K.; Kimura, Y.
Enzymatic characteristics of an ApaH-like phosphatase, PrpA, and a diadenosine tetraphosphate hydrolase, ApaH, from Myxococcus xanthus
FEBS Lett.
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3395-3402
2014
Myxococcus xanthus (Q1DC62), Myxococcus xanthus DK 1622 (Q1DC62)
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