EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
    3.6.1.1 | more |
no hydrolysis of ATP in the presence of Mg2+ |
Escherichia coli MRE 600 |
? |
- |
? |
| 3.6.1.1 | diphosphate + H2O |
no other substrates |
Geobacillus stearothermophilus |
2 phosphate |
- |
? |
| 3.6.1.1 | diphosphate + H2O |
no significant proton-translocation activity can be assayed in the total membrane fractions of pTVP-transformed yeast cells. This is probably due to the fact that the activity of the hyperthermophilic enzyme is negligible below 50-55°C. Above 50°C the high passive conductance of yeast membranes to protons makes it impossible to establish a reasonable pH gradient as demonstrated with V-PPases that hydrolyze PPi at these temperatures |
Thermotoga maritima |
2 phosphate |
- |
? |
| 3.6.1.1 | diphosphate + H2O |
no significant proton-translocation activity can be assayed in the total membrane fractions of pTVP-transformed yeast cells. This is probably due to the fact that the activity of the hyperthermophilic enzyme is negligible below 50-55°C. Above 50°C the high passive conductance of yeast membranes to protons makes it impossible to establish a reasonable pH gradient as demonstrated with V-PPases that hydrolyze PPi at these temperatures |
Thermotoga maritima DSM 3109 |
2 phosphate |
- |
? |
| 3.6.1.1 | more |
PfPPase is capable of utilizing PPi, polyP3, and ATP as substrates |
Plasmodium falciparum |
? |
- |
- |
| 3.6.1.1 | more |
polyphosphates and ATP are not hydrolyzed |
Leishmania major |
? |
- |
? |
| 3.6.1.1 | more |
polyphosphates and ATP are not hydrolyzed |
Leishmania major 252 |
? |
- |
? |
| 3.6.1.1 | diphosphate + H2O |
PPase plays an essential role in energy conservation and provides the energy for many biosynthetic pathways controlling the intracellular diphosphate levels |
Helicobacter pylori |
2 phosphate |
- |
? |
| 3.6.1.1 | diphosphate + H2O |
pronounced specificity for diphosphate |
Thermoplasma acidophilum |
2 phosphate |
- |
? |
| 3.6.1.1 | diphosphate + H2O |
reaction may be reversed by coupling to glucose-6-phosphate to 6-phospho-gluconate |
Escherichia coli |
2 phosphate |
- |
? |
