Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ATP | ATP activates hydrolysis of MgPPi by E-PPase, molecular docking and kinetic analysis involving Lys112 and Lys115, activation mechanism, and regulatory function of ATP, modelling, overview | Escherichia coli | |
additional information | no activation by ADP and AMP | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ca2+-diphosphate | nonhydrolyzable substrate analogue | 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 |
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 | residues Arg43, Lys148, and Lys115 are involved in binding of diphosphate | Escherichia coli | 2 phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
E-PPase | - |
Escherichia coli |
inorganic pyrophosphatase | - |
Escherichia coli |
PPase | - |
Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | 7.5 | assay at | Escherichia coli |