Activating Compound | Comment | Organism | Structure |
---|---|---|---|
potassium cyclic 2,3-diphosphoglycerate | required for activity at 1 M, can be substituted by other salts with strongly hydrated anions, especially by K+, the enzyme is inactive and thermolabile, and changes the oligomerization state at low salt concentrations | Methanopyrus kandleri |
General Stability | Organism |
---|---|
potassium cyclic 2,3-diphosphoglycerate and potassium phosphate stabilize the enzyme | Methanopyrus kandleri |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
K+ | potassium cyclic 2,3-diphosphoglycerate required for activity at 1 M, can be substituted by other salts with strongly hydrated anions, especially by K+, the enzyme is inactive and thermolabile, and changes the oligomerization state at low salt concentrations | Methanopyrus kandleri | |
potassium phosphate | required for activity at 1 M, can be substituted by other salts with strongly hydrated anions, especially by potassium cyclic 2,3-diphosphoglycerate, the enzyme is inactive and thermolabile, and changes the oligomerization state at low salt concentrations | Methanopyrus kandleri |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
32000 | - |
2 * 32000, crystal structure analysis, high potassium phosphate concentration of 1.0 M | Methanopyrus kandleri |
32000 | - |
4 * 32000, crystal structure analysis, high potassium phosphate concentration of 1.5 M | Methanopyrus kandleri |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methanopyrus kandleri | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
additional information | the hyperthermophilic methanogenic archaeon grows on H2 and CO2 as sole energy source best at 98°C | Methanopyrus kandleri | - |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 32000, crystal structure analysis, high potassium phosphate concentration of 1.0 M | Methanopyrus kandleri |
More | structure analysis, at low salt conditions the enzyme is in an equilibrium of dimer, trimer and tetramer, the latter being the active and most thermostable enzyme form, the dimer is also active, but the monomer is inactive | Methanopyrus kandleri |
tetramer | 4 * 32000, crystal structure analysis, high potassium phosphate concentration of 1.5 M | Methanopyrus kandleri |
Synonyms | Comment | Organism |
---|---|---|
formyltransferase | - |
Methanopyrus kandleri |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
the enzyme is thermostable | Methanopyrus kandleri |
90 | - |
30 min, wild-type enzyme, loss of 70% activity at 0.8-1.0 M potassium phosphate | Methanopyrus kandleri |