Any feedback?
No. of entries
Information on EC 3.6.1.25 - triphosphatase
for references in articles please use BRENDA:EC3.6.1.25
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 3 Hydrolases
3.6 Acting on acid anhydrides
3.6.1 In phosphorus-containing anhydrides
3.6.1.25 triphosphatase
The enzyme appears in viruses and cellular organisms
- 3.6.1.25
- atpase
- na+
- ouabain
-
k+-adenosine
-
ca2+-adenosine
- cardiac
-
sarcoplasmic
-
na+,k+-adenosine
-
k+-atpase
- ca2+-atpase
- myosin
-
parietal
-
guanylyltransferase
- na+,k+-atpase
-
contractile
- 5'-nucleotidase
- tripolyphosphate
-
ouabain-sensitive
- omeprazole
-
ecto-adenosine
-
inotropic
-
antisecretory
-
3.6.1.3
- digoxin
- diphosphatase
- phospholamban
- ecto-atpase
-
nak-atpase
- lansoprazole
showSynonyms
triphosphatase, tripolyphosphatase, triphosphate phosphohydrolase, triphosphate tunnel metalloenzyme, inorganic triphosphatase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
inorganic triphosphatase
Saci_0718
TTM
inorganic triphosphatase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
triphosphate + H2O = diphosphate + phosphate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
triphosphate phosphohydrolase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
62213-21-2
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
tripolyphosphate + H2O
diphosphate + phosphate
-
Substrates: 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
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Substrates: -
Products: -
Products: -
?
tetraphosphate + 2 H2O
diphosphate + 2 phosphate
Substrates: -
Products: -
Products: -
?
tetraphosphate + 2 H2O
diphosphate + 2 phosphate
Substrates: -
Products: -
Products: -
?
triphosphate + H2O
diphosphate + phosphate
Substrates: -
Products: -
Products: -
?
triphosphate + H2O
diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
triphosphate + H2O
diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
triphosphate + H2O
diphosphate + phosphate
-
Substrates: involved in phosphorous and energy exchange of mitochondria
Products: -
Products: -
?
triphosphate + H2O
diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
triphosphate + H2O
diphosphate + phosphate
-
Substrates: involved in transcription termination
Products: -
Products: -
?
triphosphate + H2O
diphosphate + phosphate
Substrates: -
Products: -
Products: -
?
triphosphate + H2O
diphosphate + phosphate
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: TTM3 is a protein with high triphosphatase activity (binding both tripolyphosphate and ATP) and low adenylyl cyclase activity
Products: -
Products: -
-
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: TTM dooes not produce any cyclic nucleotides. With substrate triphosphate, TTM is 19fold more reactive than with NTPs
Products: -
Products: -
-
additional information
?
-
Substrates: TTM dooes not produce any cyclic nucleotides. With substrate triphosphate, TTM is 19fold more reactive than with NTPs
Products: -
Products: -
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
triphosphate + H2O
diphosphate + phosphate
-
Substrates: -
Products: -
Products: -
?
triphosphate + H2O
diphosphate + phosphate
-
Substrates: involved in phosphorous and energy exchange of mitochondria
Products: -
Products: -
?
triphosphate + H2O
diphosphate + phosphate
-
Substrates: involved in transcription termination
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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+
Mn2+
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.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
enzyme shows feedback inhibition due to tunnel closure in the product state
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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+
0.021
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
0.1
tripolyphosphate
-
untagged wild type enzyme, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+
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.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000006
substrate ATP, formation of cAMP, presence of Mn2+, Mg2+, 30°C, pH 7.5
0.0012
-
tripolyphosphatase activity of R265H mutant, 2 mM ATP as substrate
0.0019
-
tripolyphosphatase activity of R265H mutant, 2 mM pyrophosphate as substrate
0.004
-
tripolyphosphatase activity of R265H mutant, 2 mM metatripolyphosphate as substrate
0.007
substrate ATP, release of ADP and phosphate, presence of Mn2+, Mg2+, 30°C, pH 7.5
0.0115
substrate triphosphate, presence of Mn2+, Mg2+, 30°C, pH 7.5
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
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.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
protein belongs to the CYTH-like phosphatase superfamily. The CYTH domain in BdTTM3 includes the characteristic EXEXK signature
additional information
enzyme shows a two-metal-ion reaction mechanism and feedback inhibition due to tunnel closure in the product state
additional information
-
enzyme shows a two-metal-ion reaction mechanism and feedback inhibition due to tunnel closure in the product state
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). 3PASE_ACET2
Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
156
0
18159
Swiss-Prot
-
3PASE_HAEIN
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
352
0
41315
Swiss-Prot
other Location (Reliability: 1)
3PASE_NITEU
Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298)
151
0
17314
Swiss-Prot
-
I1I2P2_BRADI
212
0
23037
TrEMBL
Mitochondrion (Reliability: 1)
Q4JAT2_SULAC
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
185
0
22174
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41600
-
R265H mutant, gel filtration, column equilibrated with 2 mM tripolyphosphate
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.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 23040, calculated from sequence, x * 55000, SDS-PAGE of recombinant GST-fusion protein
heterodimer
-
containing one R265H mutant subunit and one wildtype subunit, impaired AdoMet synthetase activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged R265H mutant purified with Ni2+ Sepharose column chromatography and wildtype enzyme purified from liver
-
recombinant protein, purified to homogeneity using an initial heat denaturation step followed by IMAC and subsequent size exclusion chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Orthopoxvirus vaccinia
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
Swiezawska, B.; Duszyn, M.; Kwiatkowski, M.; Jaworski, K.; Pawelek, A.; Szmidt-Jaworska, A.
Brachypodium distachyon triphosphate tunnel metalloenzyme 3 is both a triphosphatase and an adenylyl cyclase upregulated by mechanical wounding
FEBS Lett.
594
1101-1111
2020
Brachypodium distachyon (I1I2P2)
brenda
Vogt, M.S.; Ngouoko Nguepbeu, R.R.; Mohr, M.K.F.; Albers, S.V.; Essen, L.O.; Banerjee, A.
The archaeal triphosphate tunnel metalloenzyme SaTTM defines structural determinants for the diverse activities in the CYTH protein family
J. Biol. Chem.
297
100820
2021
Sulfolobus acidocaldarius (Q4JAT2), Sulfolobus acidocaldarius DSM 639 (Q4JAT2)
brenda
EXTERNAL LINKS (specific for EC-Number 3.6.1.25)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
