Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Fabrichniy, I.P.; Lehtioe, L.; Tammenkoski, M.; Zyryanov, A.B.; Oksanen, E.; Baykov, A.A.; Lahti, R.; Goldman, A.
    A trimetal site and substrate distortion in a family II inorganic pyrophosphatase (2007), J. Biol. Chem., 282, 1422-1431.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.6.1.1 purified recombinant wild-type and mutant enzymes in complex with substrate analogue imidodiphosphate, PNP, and/or inhibitor fluoride, 35-40 mg/ml protein in 83mM TES/K+, pH 7.2, 17 mM KCl and 0.05 mM EGTA is mixed with 5 mM MgCl2 and 10 mM NaF, 1 mM PNP, sitting drop vapour diffusion method, 4°C, 3:2 ratio of protein to well solution, the latter containing 100 mM HEPES/K+, pH 7.5, 2.3-2.5 M ammonium sulfate, 3-4% PEG 400, 2-3 days, X-ray diffraction structure determination and anaylsis at 1.75-2.15 A resolution, the mutant H98Q crystals do not contain fluoride ions Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
3.6.1.1 H98Q the mutant shows highly reduced activity compared to the wild-type enzyme, crystal structure determination and comparison of substrate/inhibitor binding to the wild-type enzyme Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.1 fluoride inhibition of wild-type and mutant enzyme Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.1 0.012
-
 imidodiphosphoric acid pH 7.2, 25°C, wild-type enzyme Bacillus subtilis
3.6.1.1 0.06
-
 diphosphate pH 7.2, 25°C, wild-type enzyme Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.1 Fe3+ bound in in sites M1 and M2, the Fe3+:Mn2+ ratio is about 6:1 in site M1 and about 2:1 in site M2 Bacillus subtilis
3.6.1.1 Mn2+ bound in in sites M1 and M2, the Fe3+:Mn2+ ratio is about 6:1 in site M1 and about 2:1 in site M2 Bacillus subtilis
3.6.1.1 additional information the enzyme contains a unique trinuclear metal center, detailed structure analysis, overview. Mn2+ and Fe3+ do not exchange for Mg2+ even in the presence of a large excess of Mg2+ Bacillus subtilis

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 Bacillus subtilis
-
 2 phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.1 Bacillus subtilis P37487
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.1 diphosphate + H2O
-
 Bacillus subtilis 2 phosphate
-
 ?
3.6.1.1 imidodiphosphate + H2O active site and substrate binding structure determination and analysis, overview Bacillus subtilis phosphate + phosphoramidic acid
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.6.1.1 family II inorganic pyrophosphatase
-
 Bacillus subtilis
3.6.1.1 family II PPase
-
 Bacillus subtilis
3.6.1.1 PPase
-
 Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.6.1.1 0.014
-
 imidodiphosphoric acid pH 7.2, 25°C, wild-type enzyme Bacillus subtilis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.6.1.1 0.012
-
 fluoride pH 7.2, 25°C, wild-type enzyme, kinetics Bacillus subtilis