General Stability | Organism |
---|---|
the enzyme is stable and functional under hypersaline conditions | Pyrococcus horikoshii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
KCl | the enzyme is optimally active at salt concentration between 0.075 and 0.25 M KCl. More than 70% of the activity is maintained at 2 M KCl | Pyrococcus horikoshii | |
Zinc | the purified enzyme contains two equivalent of zinc per monomer. When zinc is removed by EDTA treatment, the complex dissociates into dimeric species | Pyrococcus horikoshii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus horikoshii | O59485 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Lys-4-nitroanilide + H2O | - |
Pyrococcus horikoshii | Lys + 4-nitroaniline | - |
? |
Subunits | Comment | Organism |
---|---|---|
dodecamer | studies on the parameters controlling the stability of the TET peptidase superstructure from Pyrococcus horikoshii reveal a crucial role of pH and catalytic metals in the oligomerization process. The dodecameric edifice of the enzyme remains intact under acidic pH. Basic pH leads to a significant deoligomerization. At pH 11 over 50% of the protein is still in its dodecameric form, revealing a great resistance of the edifice against deoligomerization. No unfolded or aggregated protein is found throughout the whole range of pH tested, indicating that the dimer is soluble and stable. Oligomerization is a metal dependent process | Pyrococcus horikoshii |
Synonyms | Comment | Organism |
---|---|---|
PhTET3 | - |
Pyrococcus horikoshii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
85 | - |
assay at | Pyrococcus horikoshii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Pyrococcus horikoshii |