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Literature summary 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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.6.1.1 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

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

Inhibitors

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

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.6.1.1 soluble
-
 Escherichia coli
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.1 Mg2+ binding depends highly on the pH, binds to the active site, binding structure, overview Escherichia coli
3.6.1.1 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)

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

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.1 Escherichia coli P0A7A9
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.1 diphosphate + H2O
-
 Escherichia coli 2 phosphate
-
 r
3.6.1.1 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

EC Number Synonyms Comment Organism
3.6.1.1 PPase
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.1.1 25
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.1.1 7.4
-
 assay at, the pH heavily influences the metal binding of the enzyme, hydrolysis Escherichia coli
3.6.1.1 8
-
 assay at, synthesis Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.6.1.1 0.0028
-
 fluoride pH 7.4, 25°C, with 0.05 mM Mn2+ Escherichia coli
3.6.1.1 0.0358
-
 fluoride pH 7.4, 25°C, with 5 mM Mn2+ Escherichia coli