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Literature summary for 3.6.1.1 extracted from
- Binding of substrate at the effector site of pyrophosphatase increases the rate of its hydrolysis at the active site (2007), Biochemistry (Moscow), 72, 68-76.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| magnesium methylenediphosphonate | a non-hydrolyzable analogue, the enzyme contains an extra binding site for the substrate magnesium diphosphate or its non-hydrolyzable analogue magnesium methylenediphosphonate, binding of substrate at the effector site of pyrophosphatase increases the rate of its hydrolysis at the active site, overview | Escherichia coli |  |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D26A | site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation | Escherichia coli |
| D42E | site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation | Escherichia coli |
| E31A | site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation | Escherichia coli |
| K112Q | site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation | Escherichia coli |
| K115A | site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation | Escherichia coli |
| K148Q | site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation | Escherichia coli |
| R43Q | site-directed mutagenesis, the mutant shows a decrease in affinity to the effector site and, as a consequence, kinetics of substrate hydrolysis that do not obey the Michaelis-Menten equation | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic analysis of wild-type and mutant enzymes with different substrates, detailed overview | Escherichia coli |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| soluble | - |
Escherichia coli | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| lanthanum | results in a slow substrate binding to diphosphate | Escherichia coli | |
| Mg2+ | dependent on, activates, bound to the substrate as magnesium diphosphate | 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 | - |
- |
- |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 82 | - |
0.0025 mM substrate Mg-diphosphate, in absence of magnesium methylenediphosphonate | Escherichia coli |
| 142 | - |
0.0025 mM substrate Mg-diphosphate, in presence of 0.0075 mM magnesium methylenediphosphonate | Escherichia coli |
| 360 | - |
0.015 mM substrate Mg-diphosphate, in presence or absence of 0.0075 mM magnesium methylenediphosphonate | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| diphosphate + H2O | - |
Escherichia coli | 2 phosphate | - |
? | |
| diphosphate + H2O | high activity with magnesium diphosphate, low activity with lanthanum diphosphate | Escherichia coli | 2 phosphate | - |
? | |
| additional information | the enzyme contains an extra binding site for the substrate magnesium diphosphate or its non-hydrolyzable analogue magnesium methylenediphosphonate, binding of substrate at the effector site of pyrophosphatase increases the rate of its hydrolysis at the active site, overview | Escherichia coli | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | - |
Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| inorganic pyrophosphatase | - |
Escherichia coli |
| PPase | - |
Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Escherichia coli |
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