EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
7.1.3.2 | K+ | enzyme exhibits an absolute requirement for Na+ but displays the highest activity in the presence of millimolar levels of both Na+ and K+. Two Na+ binding sites and one K+ binding site are involved in enzyme activation | Thermotoga maritima |
EC Number | Cloned (Comment) | Organism |
---|---|---|
3.6.1.1 | expression in Escherichia coli | Thermotoga maritima |
7.1.3.2 | expression in Escherichia coli | Thermotoga maritima |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.6.1.1 | D190A | the Na+ dose dependency of the D190A variant closely resembles that of the wild-type enzyme | Thermotoga maritima |
3.6.1.1 | D703N | the variant exhibits a much lower slope on the rate vs [Na+] plot than the wild-type enzyme at all of the K+ concentrations examined | Thermotoga maritima |
7.1.3.2 | D190A | the Na+ dose dependencies closely resemble those of the wild-type enzyme | Thermotoga maritima |
7.1.3.2 | D190A/D703N | activation by alkali cations is similar to the D703N variant, but the maximum is shifted to 2fold higher Na+ and K+ concentrations | Thermotoga maritima |
7.1.3.2 | D703N | only one Na+ binding site (K+-dependent) and one K+ binding site are involved in activation of the variant | Thermotoga maritima |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.6.1.1 | membrane | bound to | Thermotoga maritima | 16020 | - |
7.1.3.2 | membrane | - |
Thermotoga maritima | 16020 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.6.1.1 | K+ | the enzyme absolutely requires Na+ for activity, whereas both Na+ and K+ are needed for maximal activity | Thermotoga maritima | |
3.6.1.1 | Li+ | Li+ can substitute for Na+ as activator. In the presence of K+, Li+ iss a less potent activator than Na+ | Thermotoga maritima | |
3.6.1.1 | Na+ | the enzyme absolutely requires Na+ for activity, whereas both Na+ and K+ are needed for maximal activity | Thermotoga maritima |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.6.1.1 | Thermotoga maritima | Q9S5X0 | - |
- |
3.6.1.1 | Thermotoga maritima DSM 3109 | Q9S5X0 | - |
- |
7.1.3.2 | Thermotoga maritima | Q9S5X0 | - |
- |
7.1.3.2 | Thermotoga maritima DSM 3109 | Q9S5X0 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.6.1.1 | - |
Thermotoga maritima |
EC Number | Storage Stability | Organism |
---|---|---|
7.1.3.2 | 4°C, stable for at least 1 week | Thermotoga maritima |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.6.1.1 | diphosphate + H2O | - |
Thermotoga maritima | 2 phosphate | - |
? | |
3.6.1.1 | diphosphate + H2O | - |
Thermotoga maritima DSM 3109 | 2 phosphate | - |
? | |
7.1.3.2 | diphosphate + H2O + Na+(side1) | - |
Thermotoga maritima | H+ + Na+(side2) + 2 phosphate | - |
? | |
7.1.3.2 | diphosphate + H2O + Na+(side1) | - |
Thermotoga maritima DSM 3109 | H+ + Na+(side2) + 2 phosphate | - |
? | |
7.1.3.2 | additional information | enzyme does not catalyze oxygen exchange between phosphate and water. Solubilized HppA exhibits low but measurable PPi-synthesizing activity, which also requires Na+ but is inhibited by K+ | Thermotoga maritima | ? | - |
- |
|
7.1.3.2 | additional information | enzyme exhibits an absolute requirement for Na+ but displays the highest activity in the presence of millimolar levels of both Na+ and K+. Two Na+ binding sites and one K+ binding site are involved in enzyme activation. In the absence of K+, Li+ may substitute for Na+ | Thermotoga maritima | ? | - |
- |
|
7.1.3.2 | additional information | enzyme does not catalyze oxygen exchange between phosphate and water. Solubilized HppA exhibits low but measurable PPi-synthesizing activity, which also requires Na+ but is inhibited by K+ | Thermotoga maritima DSM 3109 | ? | - |
- |
|
7.1.3.2 | additional information | enzyme exhibits an absolute requirement for Na+ but displays the highest activity in the presence of millimolar levels of both Na+ and K+. Two Na+ binding sites and one K+ binding site are involved in enzyme activation. In the absence of K+, Li+ may substitute for Na+ | Thermotoga maritima DSM 3109 | ? | - |
- |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
7.1.3.2 | ? | x * 66000, SDS-PAGE, x * 73000, calculated from sequence | Thermotoga maritima |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.6.1.1 | Tm-PPase | - |
Thermotoga maritima |
7.1.3.2 | HppA | - |
Thermotoga maritima |
7.1.3.2 | K(+)-stimulated pyrophosphate-energized sodium pump | - |
Thermotoga maritima |
7.1.3.2 | TM_0174 | - |
Thermotoga maritima |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.6.1.1 | 40 | - |
assay at | Thermotoga maritima |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.6.1.1 | 7.2 | - |
assay at | Thermotoga maritima |