We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
triphosphatase, tripolyphosphatase, triphosphate phosphohydrolase, triphosphate tunnel metalloenzyme, inorganic triphosphatase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
triphosphate tunnel metalloenzyme
-
-
inorganic triphosphatase
-
-
-
-
inorganic triphosphatase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
triphosphate + H2O = diphosphate + phosphate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
phosphorous acid anhydride hydrolysis
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
triphosphate phosphohydrolase
-
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.
ATP + H2O
?
-
low affinity
-
-
?
triphosphate + H2O
diphosphate + phosphate
tripolyphosphate + H2O
diphosphate + phosphate
-
very good substrate with Mg2+ as activator. The enzyme has a strong preference for linear tripolyphosphate compared with cyclic trimetaphosphate and to the linear tetraphosphate
-
-
?
additional information
?
-
-
the enzyme has low affinity for CTP, ATP or thiamine triphosphate. Nucleoside triphosphatase activity is negligible in the presence of 5 mM Mg2+, but a small activity is observed in the presence of 1 mM Mn2+, in particular with GTP. Guanosine 5-tetraphosphate and long chain polyphosphate (containing about 65 phosphate residues) are not hydrolyzed. The enzyme has no adenylyl cyclase activity
-
-
?
triphosphate + H2O
diphosphate + phosphate
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
-
involved in phosphorous and energy exchange of mitochondria
-
?
triphosphate + H2O
diphosphate + phosphate
-
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
-
involved in transcription termination
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
triphosphate + H2O
diphosphate + phosphate
triphosphate + H2O
diphosphate + phosphate
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
-
involved in phosphorous and energy exchange of mitochondria
-
?
triphosphate + H2O
diphosphate + phosphate
-
involved in transcription termination
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Co2+
-
Co2+ is a better activator than Mn2+, although the maximum activity is less than 10% that measured in the presence of 5 mM Mg2+
Mg2+
-
the enzyme hydrolyzes tripolyphosphate with high catalytic efficiency in the presence of 5 mM Mg2+
Mn2+
-
very poor substituent for Mg2+ in the pH range 7.0-10, but there is a significant Mn2+-dependent activity at pH 10.0-10.5. Half-maximum activation is obtained at 0.4 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Zn2+
-
complete inhibition at 0.005 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.02 - 74
tripolyphosphate
additional information
additional information
-
no change in activity after nitrosylation of the enzyme with 250 microM nitrosylated glutathione
-
0.8
ATP
-
His-tagged wild type enzyme, at pH 8.1 and 50°C, in the presence of 10 mM Mn2+
1.2
ATP
-
His-tagged mutant enzyme K8A, at pH 10.1 and 50°C, in the presence of 10 mM Mn2+
0.02
tripolyphosphate
-
wildtype, 2 mM substrate
0.021
tripolyphosphate
-
His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
0.04
tripolyphosphate
-
His-tagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
0.058
tripolyphosphate
-
His-tagged wild type enzyme, at pH 7.1 and 37°C, in the presence of 5 mM Mg2+
0.078
tripolyphosphate
-
R265H mutant, 2 mM substrate in the presence of 5 mM ATP
0.083
tripolyphosphate
-
R265H mutant, 2 mM substrate
0.1
tripolyphosphate
-
untagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
0.122
tripolyphosphate
-
R265S mutant, 2 mM substrate
0.143
tripolyphosphate
-
R265H mutant, 2 mM substrate in the presence of 5 mM diphosphate
0.191
tripolyphosphate
-
His-tagged mutant enzyme K52R, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
0.39
tripolyphosphate
-
His-tagged mutant enzyme K8A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
0.72
tripolyphosphate
-
His-tagged mutant enzyme K85A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
2.6
tripolyphosphate
-
His-tagged mutant enzyme K85A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
74
tripolyphosphate
-
His-tagged mutant enzyme K8A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.28 - 7900
tripolyphosphate
0.36
ATP
-
His-tagged wild type enzyme, at pH 8.1 and 50°C, in the presence of 10 mM Mn2+
3.96
ATP
-
His-tagged mutant enzyme K8A, at pH 10.1 and 50°C, in the presence of 10 mM Mn2+
0.28
tripolyphosphate
-
His-tagged mutant enzyme K8A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
0.98
tripolyphosphate
-
His-tagged mutant enzyme K52R, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
10
tripolyphosphate
-
His-tagged mutant enzyme K85A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
21
tripolyphosphate
-
His-tagged mutant enzyme K85A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
60
tripolyphosphate
-
His-tagged wild type enzyme, at pH 7.1 and 37°C, in the presence of 5 mM Mg2+
76
tripolyphosphate
-
His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
288
tripolyphosphate
-
His-tagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
887
tripolyphosphate
-
His-tagged mutant enzyme K8A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
7900
tripolyphosphate
-
untagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4 - 79000
tripolyphosphate
0.45
ATP
-
His-tagged wild type enzyme, at pH 8.1 and 50°C, in the presence of 10 mM Mn2+
3.3
ATP
-
His-tagged mutant enzyme K8A, at pH 10.1 and 50°C, in the presence of 10 mM Mn2+
4
tripolyphosphate
-
His-tagged mutant enzyme K85A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
5.1
tripolyphosphate
-
His-tagged mutant enzyme K52R, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
29
tripolyphosphate
-
His-tagged mutant enzyme K85A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
190
tripolyphosphate
-
His-tagged mutant enzyme K8A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
2300
tripolyphosphate
-
His-tagged mutant enzyme K8A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
3300
tripolyphosphate
-
His-tagged wild type enzyme, at pH 7.1 and 37°C, in the presence of 5 mM Mg2+
3600
tripolyphosphate
-
His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
7200
tripolyphosphate
-
His-tagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
79000
tripolyphosphate
-
untagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.01
Cd2+
Nitrosomonas europaea
-
His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
0.02
Cu2+
Nitrosomonas europaea
-
His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
0.0015
Zn2+
Nitrosomonas europaea
-
His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.001
-
R265S mutant, 2 mM methionine and 2 mM ATP as substrate
0.0012
-
tripolyphosphatase activity of R265H mutant, 2 mM ATP as substrate
0.0019
-
tripolyphosphatase activity of R265H mutant, 2 mM pyrophosphate as substrate
0.002
-
R265H mutant, 2 mM methionine and 2 mM ATP as substrate
0.004
-
tripolyphosphatase activity of R265H mutant, 2 mM metatripolyphosphate as substrate
0.029
-
tripolyphosphatase activity of R265S mutant, 2 mM tripolyphosphate as substrate
0.067
-
tripolyphosphatase activity of R265H mutant, 2 mM tripolyphosphate as substrate in the presence of 5 mM pyrophosphate
0.128
-
tripolyphosphatase activity of R265H mutant, 2 mM tripolyphosphate as substrate
0.129
-
tripolyphosphatase activity of R265H mutant, 2 mM tripolyphosphate as substrate in the presence of 5 mM ATP
0.156
-
tripolyphosphatase activity of wildtype, 2 mM tripolyphosphate as substrate
0.588
-
wildtype, 2 mM methionine and 2 mM ATP as substrate
additional information
-
tripolyphosphate activity of R265H mutant is specific for tripolyphosphate and depends on magnesium ions, potassium is not required
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.
-
-
-
brenda
mold fungus
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
-
brenda
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.
19000
-
2 * 19000, SDS-PAGE
41600
-
R265H mutant, gel filtration, column equilibrated with 2 mM tripolyphosphate
60000
-
calculation from mRNA-sequence, subunit of D1 capping enzyme
90000
-
heterodimer of R265H mutant and wildtype enzyme, size exclusion chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
heterodimer
-
containing one R265H mutant subunit and one wildtype subunit, impaired AdoMet synthetase activity
homodimer
-
2 * 19000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hanging drop vapor diffusion method, selenomethionine-substituted protein, using 3.5 M sodium formate as a precipitation agent and 0.1 M Bis-Tris propane buffer, pH 7.0, at 20°C
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
K52R
-
the His-tagged mutant loses 90-99% of its activity (catalytic efficiency is at least 1000times lower) compared to the wild type enzyme. Mn2+ does not induce a significant activation of this mutant
K85A
-
the His-tagged mutant is about 10times less active than the wild type enzyme, but the optimal conditions for activity are essentially the same. The mutant is more strongly activated by Mn2+ than by Mg2+, and the inhibitory effects of Ca2+ and Zn2+ are less pronounced
K8A
-
the His-tagged mutant remains highly active with tripolyphosphate as substrate and Mg2+ as activator, with a catalytic efficiency close to that of the recombinant wild type enzyme
R265H
-
no AdoMet synthetase activity, normal tripolyphosphatase activity
R265S
-
no AdoMet synthetase activity, reduced tripolyphosphatase activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
His-tagged R265H mutant purified with Ni2+ Sepharose column chromatography and wildtype enzyme purified from liver
-
His-Trap column chromatography, gel filtration
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expressed in Escherichia coli BL21(DE3) cells
-
His-tagged R265H mutant, expressed in E. coli BL21
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Kulaev, I.S.; Konoshenko, G.I.; Umnov, A.M.
Localization of polyphosphatases hydrolyzing polyphosphates to orthophosphate in subcellular structures of Neurospora crassa
Biochemistry (Moscow)
37
190-194
1972
Neurospora crassa
-
brenda
Kulalev, A.M.; Egorov, S.N.; Mansurova, S.E.; Kulaev, I.S.
A comparative characterization of the polyphosphatases of Neurospora crassa and some other organisms
Biochemistry (Moscow)
39
309-312
1974
Neurospora crassa
-
brenda
Trilisenko, L.V.; Novotna, J.; Erban, V.; Behal, V.; Hostalek, Z.; Kulaev, I.S.
Subcellular localization of enzymes in Streptomyces aureofaciens and its alteration by benzyl thiocyanate
Folia Microbiol. (Praha)
32
402-410
1987
Kitasatospora aureofaciens
brenda
Yu, L.; Martins, A.; Deng, L.; Shuman, S.
Structure-function analysis of the triphosphatase component of vaccina virus mRNA capping enzyme
J. Virol.
71
9837-9843
1997
Vaccinia virus
brenda
Perez Mato, I.; Sanchez del Pino, M.M.; Chamberlin, M.E.; Mudd, S.H.; Mato, J.M.; Corrales, F.J.
Biochemical basis for the dominant inheritance of hypermethioninemia associated with the R264H mutation of the MAT1A gene. A monomeric methionine adenosyltransferase with tripolyphosphatase activity
J. Biol. Chem.
276
13803-13809
2001
Rattus norvegicus
brenda
Delvaux, D.; Murty, M.R.; Gabelica, V.; Lakaye, B.; Lunin, V.V.; Skarina, T.; Onopriyenko, O.; Kohn, G.; Wins, P.; De Pauw, E.; Bettendorff, L.
A specific inorganic triphosphatase from Nitrosomonas europaea: structure and catalytic mechanism
J. Biol. Chem.
286
34023-34035
2011
Nitrosomonas europaea
brenda
Select items on the left to see more content.
html completed