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Literature summary for 3.6.1.1 extracted from

  • Samygina, V.R.; Moiseev, V.M.; Rodina, E.V.; Vorobyeva, N.N.; Popov, A.N.; Kurilova, S.A.; Nazarova, T.I.; Avaeva, S.M.; Bartunik, H.D.
    Reversible inhibition of Escherichia coli inorganic pyrophosphatase by fluoride: trapped catalytic intermediates in cryo-crystallographic studies (2007), J. Mol. Biol., 366, 1305-1317.
    View publication on PubMed
Search for more literature for 3.6.1.1

Crystallization (Commentary)

Crystallization (Comment) Organism
wild-type enzyme with bound fluoride trapped in an intermediate conformation, and mutant R43Q with one phosphate and four Mn2+ bound, 7-8 mg/ml protein, with 0.2 M sodium acetate, pH 5.5, using 1.5 M-1.7 M NaCl as precipitant, X-ray diffraction structure determination and analysis at 1.05-1.68 A resolution Escherichia coli

Protein Variants

Protein Variants Comment Organism
D102N site-directed mutagenesis, the active site residue mutation does only marginally influence the pH-dependence of fluoride inhibition Escherichia coli
D65N site-directed mutagenesis, the active site residue mutation does only marginally influence the pH-dependence of fluoride inhibition Escherichia coli
D67N site-directed mutagenesis, the active site residue mutation does only marginally influence the pH-dependence of fluoride inhibition Escherichia coli
D70N site-directed mutagenesis, the active site residue mutation does only marginally influence the pH-dependence of fluoride inhibition Escherichia coli
R43Q site-directed mutagenesis, crystal structure determination and analysis and comparison to the wild-type structure Escherichia coli
Y55F site-directed mutagenesis, the active site residue mutation does only marginally influence the pH-dependence of fluoride inhibition Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
fluoride reversible inhibition, binds to the active site, binding structure, overview Escherichia coli

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ binding depends highly on the pH, binds to the active site, binding structure, overview Escherichia coli
Mn2+ binding depends highly on the pH, four ions bound per enzyme molecule, binds to the active site, binding structure, overview 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 P0A7A9
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diphosphate + H2O
-
 Escherichia coli 2 phosphate
-
 r
diphosphate + H2O the rate-limiting step of Mn2+-supported hydrolysis of the phosphoanhydride bond is followed by a fast release of the leaving phosphate from the P1 site, overview Escherichia coli 2 phosphate Mg- or Mn-bound substrate for the synthesis reaction r

Synonyms

Synonyms Comment Organism
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
7.4
-
 assay at, the pH heavily influences the metal binding of the enzyme, hydrolysis Escherichia coli
8
-
 assay at, synthesis Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0028
-
 fluoride pH 7.4, 25°C, with 0.05 mM Mn2+ Escherichia coli
0.0358
-
 fluoride pH 7.4, 25°C, with 5 mM Mn2+ Escherichia coli