Protein Variants | Comment | Organism |
---|---|---|
P117G/H124L/S128A | site-directed mutagenesis | Staphylococcus aureus |
General Stability | Organism |
---|---|
correlation between the magnitude of protein stabilization and the restriction of fast backbone motions, mannosylglycerate restricts local motions in addition to the global motions of the protein. Unfolding/folding pathway remain undisturbed in the presence of mannosylglycerate but the solute shows a specific effect on the local motions of beta-sheet residues | Staphylococcus aureus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | P117G/H124L/S128A mutant enzyme thermodynamics, overview | Staphylococcus aureus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus aureus | - |
- |
- |
Subunits | Comment | Organism |
---|---|---|
More | solution structure of the hyperstable P117G/H124L/S128A mutant enzyme variant, overview | Staphylococcus aureus |
Synonyms | Comment | Organism |
---|---|---|
SNase | - |
Staphylococcus aureus |
staphylococcal nuclease | - |
Staphylococcus aureus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
different concentrations of mannosylglycerate or presence of urea at 0.25M show no correlation with changes in the thermodynamic stability of the P117G/H124L/S128A mutant enzyme | Staphylococcus aureus |
General Information | Comment | Organism |
---|---|---|
additional information | mannosylglycerate preferentially affects specific structural elements of the P117G/H124L/S128A mutant enzyme, structure analysis, overview | Staphylococcus aureus |