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Literature summary for 3.6.1.1 extracted from

  • Kuhn, N.J.; Ward, S.
    Purification, properties, and multiple forma of a manganese-activated inorganic pyrophosphatase from Bacillus subtilis (1998), Arch. Biochem. Biophys., 354, 47-56.
    View publication on PubMed
Search for more literature for 3.6.1.1

Inhibitors

Inhibitors Comment Organism Structure
EDTA Na2SO4, Li2SO4 enhance deactivation, Mn2+ is protective Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activating Bacillus subtilis
Mg2+ free Mg2+ ions are not required Bacillus subtilis
Mn2+ activating Bacillus subtilis
Mn2+ conversion of the enzyme from inactive dimer to active trimer Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34000
-
 mass spectrometry Bacillus subtilis
36000
-
 SDS-PAGE Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
diphosphate + H2O Bacillus subtilis actual substrate is magnesium diphosphate or dimagnesium diphosphate 2 phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5375
-
-
 Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diphosphate + H2O actual substrate is magnesium diphosphate or dimagnesium diphosphate Bacillus subtilis 2 phosphate
-
 ?
diphosphate + H2O high specificity Bacillus subtilis 2 phosphate
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 34000, dimer when inactive Bacillus subtilis
trimer 3 * 34000, trimer when active Bacillus subtilis