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Literature summary for 3.6.1.1 extracted from

  • Baykov, A.A.; Dudarenkov, V.Y.; Käpylä, J.; Salminen, T.; Hyytiä, T.; Kasho, V.N.; Husgafvel, S.; Cooperman, B.S.; Goldman, A.; Lahti, R.
    Dissociation of hexameric Escherichia coli inorganic pyrophosphatase into trimers on His-136 -> Gln or His-140 -> substitution and its effect on enzyme catalytic activities (1995), J. Biol. Chem., 270, 30804-30812.
    View publication on PubMed
Search for more literature for 3.6.1.1

Protein Variants

Protein Variants Comment Organism
H110Q catalytic activity unchanged compared to wild type enzyme Escherichia coli
H119Q catalytic activity unchanged compared to wild type enzyme Escherichia coli
H136Q variant can be dissociated in trimers, hydrolytic activity 225% of wild-type enzyme Escherichia coli
H140Q variant can be dissociated in trimers, hydrolytic activity 110% of wild-type enzyme Escherichia coli
H60Q catalytic activity unchanged compared to wild type enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0023
-
 Mg-diphosphate pH 7.2, hexameric, H136Q enzyme Escherichia coli
0.0027
-
 Mg-diphosphate pH 7.2, H140Q enzyme, hexameric Escherichia coli
0.0034
-
 Mg-diphosphate pH 8, wild type enzyme Escherichia coli
0.008
-
 Mg-diphosphate pH 8, hexameric, H136Q enzyme Escherichia coli
0.198
-
 Mg-diphosphate pH 7.2, H136Q enzyme, trimeric Escherichia coli
0.44
-
 Mg-diphosphate pH 8, H140Q enzyme, trimeric Escherichia coli
4.2
-
 Mg-diphosphate pH 7.2, H140Q enzyme, trimeric Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ four Mg2+ ions per active site required for catalysis Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
20000
-
 6 * 20000, homohexameric, 175 amino acid residues per subunit, wild type enzyme Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
diphosphate + H2O Escherichia coli
-
 2 phosphate
-
 r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diphosphate + H2O
-
 Escherichia coli 2 phosphate
-
 r
diphosphate + H2O diphosphate in form of Mg-diphosphate Escherichia coli 2 phosphate
-
 ?

Subunits

Subunits Comment Organism
hexamer 6 * 20000, homohexameric, 175 amino acid residues per subunit, wild type enzyme Escherichia coli
trimer dissociated variant, SDS-PAGE Escherichia coli