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 | 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 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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | dependent on, bound to the enzyme | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
diphosphate + H2O | Escherichia coli | - |
2 phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
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 | 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 | Comment | Organism |
---|---|---|
E-PPase | - |
Escherichia coli |
inorganic pyrophosphatase | - |
Escherichia coli |
PPase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | 7.5 | assay at | Escherichia coli |
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 |