Crystallization (Comment) | Organism |
---|---|
hanging-drop vapor diffusion method at 20°C. Crystal structures of the enzyme, in the apo-form and in complex with substrates | Thermococcus kodakarensis |
Protein Variants | Comment | Organism |
---|---|---|
DELTAN1-84 | mutant enzyme lacking the N-terminal 22 residues aggregates at 75°C | Thermococcus kodakarensis |
additional information | all the mutants, forming smaller assemblies, display a decrease in thermostability compared to the wild-type enzyme. Tk-AMPpaseDELTAC10 aggregates at temperatures of 80°C or higher, while aggregation of Tk-AMPpaseDELTAN84 is observed at 75°C and that of Tk-AMPpase?N84DELTAC10 is observed at 70°C | Thermococcus kodakarensis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermococcus kodakarensis | Q5JCX3 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Thermococcus kodakarensis |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
2.94 | - |
60°C, pH not specified in the publication | Thermococcus kodakarensis |
14.69 | - |
85°C, pH not specified in the publication | Thermococcus kodakarensis |
Subunits | Comment | Organism |
---|---|---|
multimer | forms a large macromolecular structure of more than 40 subunits in solution. Structures of two truncated forms of Tk-AMPpase (Tk-AMPpaseDELTAN84 and Tk-AMPpaseDELTAC10) clarify that the multimerization is achieved by two dimer interfaces within a single molecule: one by the central domain and the other by the C-terminal domain, which consists of an unexpected domain-swapping interaction. The N-terminal domain, characteristic of archaeal enzymes, is essential for enzymatic activity, participating in multimerization as well as domain closure of the active site upon substrate binding. Biochemical analysis demonstrates that the macromolecular assembly of the enzyme contributes to its high thermostability | Thermococcus kodakarensis |
Synonyms | Comment | Organism |
---|---|---|
AMPpase | - |
Thermococcus kodakarensis |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
the macromolecular assembly of the enzyme contributes to its high thermostability | Thermococcus kodakarensis |