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Literature summary extracted from

  • Kohn, G.; Delvaux, D.; Lakaye, B.; Servais, A.C.; Scholer, G.; Fillet, M.; Elias, B.; Derochette, J.M.; Crommen, J.; Wins, P.; Bettendorff, L.
    High inorganic triphosphatase activities in bacteria and mammalian cells: identification of the enzymes involved (2012), PLoS ONE, 7, e43879.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.1 0.00001
-
 diphosphate at pH 9.1 and 25°C Escherichia coli
3.6.1.1 0.91
-
 Triphosphate at pH 9.1 and 25°C Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.1 Mg2+ dependent on Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.6.1.1 20000
-
 x * 20000, calculated from amino acid sequence Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.1.1 diphosphate + H2O Escherichia coli
-
 2 phosphate
-
 ?
3.6.1.1 diphosphate + H2O Escherichia coli MG1655
-
 2 phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.1 Escherichia coli
-
-
-
3.6.1.1 Escherichia coli MG1655
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.6.1.1 0.0002
-
 with triphosphate as substrate, at pH 9.1 and 37°C Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.1 diphosphate + H2O
-
 Escherichia coli 2 phosphate
-
 ?
3.6.1.1 diphosphate + H2O
-
 Escherichia coli MG1655 2 phosphate
-
 ?
3.6.1.1 triphosphate + H2O the enzyme is less efficient for the hydrolysis of triphosphate than for diphosphate but is the main enzyme responsible for triphosphate hydrolysis in vivo Escherichia coli ?
-
 ?
3.6.1.1 triphosphate + H2O the enzyme is less efficient for the hydrolysis of triphosphate than for diphosphate but is the main enzyme responsible for triphosphate hydrolysis in vivo Escherichia coli MG1655 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.6.1.1 ? x * 20000, calculated from amino acid sequence Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.6.1.1 inorganic pyrophosphatase
-
 Escherichia coli
3.6.1.1 PPase
-
 Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.6.1.1 80
-
 the enzyme activity is remarkably heat-stable (up to 80°C) Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.6.1.1 16.7
-
 Triphosphate at pH 9.1 and 25°C Escherichia coli
3.6.1.1 42
-
 diphosphate at pH 9.1 and 25°C Escherichia coli