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Literature summary for 3.6.1.1 extracted from

  • Volk, S.E.; Dudarenkov, V.Y.; Käpylä, J.; Kasho, V.N.; Voloshina, O. A.; Salminen, T.; Goldman, A.; Lahti, R.; Baykov, A.A.; Cooperman, B.S.
    Effect of E20D substitution in the active site of Escherichia coli inorganic pyrophosphatase in its quaternary structure and catalytic properties (1995), Biochemistry, 35, 4662-4669.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D97E decreased pH-independence rates of diphosphate hydrolysis and resynthesis, destabilized EMg2(Mgdiphosphate)2 complex, raised pKa, Mg2+ binding changed Escherichia coli
E20D lower specific activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0016
-
diphosphate pH 7.2, E20D Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
Escherichia coli
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ wild type: two Mg2+ ions per active site required for catalysis Escherichia coli
Mg2+ stabilization of the hexameric E20D 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
-
-
-

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
-
?

Subunits

Subunits Comment Organism
hexamer wild type Escherichia coli
trimer dissociated variant, SDS-PAGE Escherichia coli