Protein Variants | Comment | Organism |
---|---|---|
additional information | assembly of folded protein molecules into native-like aggregates is prevented by single-point mutations that introduce structural protections within one of the most flexible region of the protein, the peripheral edge beta-strand 4. The resulting mutants do not form native-like aggregates, but can still form thioflavin T-binding and beta-structured oligomers, albeit more slowly than the wild-type protein | Saccharolobus solfataricus |
V84D | site-directed mutagenesis | Saccharolobus solfataricus |
V84P | site-directed mutagenesis | Saccharolobus solfataricus |
Y86E | site-directed mutagenesis | Saccharolobus solfataricus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | hydrodynamic parameters by dynamic light scattering, kinetics, wild-type and mutant enzymes, overview | Saccharolobus solfataricus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharolobus solfataricus | Q97ZL0 | - |
- |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme has the ability to aggregate via the transient formation of oligomers in which the protein molecules retain native-like conformations, enzyme secondary and three-dimensional structure, topology, and comparison with acylphosphatases from other organisms, overview. beta-Structured oligomer formation proceeds via an alternative mechanism that is independent of the transient formation of native-like aggregates | Saccharolobus solfataricus |
Synonyms | Comment | Organism |
---|---|---|
ACP | - |
Saccharolobus solfataricus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Saccharolobus solfataricus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.5 | - |
assay at | Saccharolobus solfataricus |