Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Thermococcus kodakarensis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | preferable divalent cation for ATPase activity | Thermococcus kodakarensis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
28000 | - |
2 * 28000, SDS-PAGE | Thermococcus kodakarensis |
49000 | - |
gel filtration | Thermococcus kodakarensis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermococcus kodakarensis | P95547 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Thermococcus kodakarensis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | the enzyme shows DNase activity on both single- and double-stranded DNAs along with the ATPase activity. ATPase activity is independent of both single-stranded and double-stranded DNAs | Thermococcus kodakarensis | AMP + diphosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 28000, SDS-PAGE | Thermococcus kodakarensis |
Synonyms | Comment | Organism |
---|---|---|
Pk-rec | - |
Thermococcus kodakarensis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
assay at | Thermococcus kodakarensis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Thermococcus kodakarensis |