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Literature summary for 3.6.1.1 extracted from

  • Rodina, E.V.; Vorobyeva, N.N.; Kurilova, S.A.; Sitnik, T.S.; Nazarova, T.I.
    ATP as effector of inorganic pyrophosphatase of Escherichia coli. The role of residue Lys112 in binding effectors (2007), Biochemistry (Moscow), 72, 100-108.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
K112Q site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
K112Q/K115A site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
K112Q/K148Q site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type enzyme Escherichia coli
K115A site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme Escherichia coli
K148Q site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme Escherichia coli
additional information construction of a modified variant of wild type PPase with a derivative of ATP chemically attached to the amino group of Lys146 Escherichia coli
R43Q site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
ATP competes with methylenediphosphonate and diphosphate for binding at the allosteric regulatory site involving Lys112 Escherichia coli
diphosphate competes with ATP and methylenediphosphonate for binding at the allosteric regulatory site involving Lys112 Escherichia coli
Methylenediphosphonate competes with ATP and diphosphate for binding at the allosteric regulatory site involving Lys112 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic analysis of wild-type and mutant enzymes, Mg2+ binding kinetics, overview Escherichia coli
0.0027
-
diphosphate pH 7.5, 25°C, mutant K112Q/K148Q Escherichia coli
0.0032
-
diphosphate pH 7.5, 25°C, wild-type enzyme and mutant K112Q/K115A Escherichia coli
0.0045
-
diphosphate pH 7.5, 25°C, mutant K112Q Escherichia coli
0.0053
-
diphosphate pH 7.5, 25°C, trimeric mutant K112Q Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on, bound to the 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
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diphosphate + H2O
-
Escherichia coli 2 phosphate
-
?
diphosphate + H2O Lys112 is supposed to play a key role in forming contacts with the phosphate groups of the three studied effectors, overview Escherichia coli 2 phosphate
-
?

Subunits

Subunits Comment Organism
hexamer two trimers, preparation of wild-type trimers by incubation of enzyme in 0.1 M MES-NaOH, pH 5.3, for 20 h at 25°C, and of the mutant K112Q in 0.1 M Na-citrate buffer, pH 4.5, for 20 h at 25°C Escherichia coli

Synonyms

Synonyms Comment Organism
E-PPase
-
Escherichia coli
inorganic pyrophosphatase
-
Escherichia coli
PPase
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2 7.5 assay at Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information inhibition kinetics Escherichia coli
0.33
-
Methylenediphosphonate pH 7.5, 25°C, wild-type mutant Escherichia coli