Protein Variants | Comment | Organism |
---|---|---|
A90S | pH-value, at which the acid-denaturation is half completed is 4.19, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 1.0 for the mutant enzyme compared to 1.8 for wild-type enzyme | Staphylococcus sp. |
G79S | pH-value, at which the acid-denaturation is half completed is 4.39, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 1.4 for the mutant enzyme compared to 1.8 for wild-type enzyme | Staphylococcus sp. |
G88V | pH-value, at which the acid-denaturation is half completed is 3.57, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 3.0 for the mutant enzyme compared to 1.8 for wild-type enzyme | Staphylococcus sp. |
H124L | pH-value, at which the acid-denaturation is half completed is 2.98, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 2.8 for the mutant enzyme compared to 1.8 for wild-type enzyme | Staphylococcus sp. |
L25A | pH-value, at which the acid-denaturation is half completed is 4.15, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 1.2 for the mutant enzyme compared to 1.8 for wild-type enzyme | Staphylococcus sp. |
V66L | pH-value, at which the acid-denaturation is half completed is 3.36, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 2.6 for the mutant enzyme compared to 1.8 for wild-type enzyme | Staphylococcus sp. |
V66L/G79S/G88V | pH-value, at which the acid-denaturation is half completed is 3.67, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 1.1 for the mutant enzyme compared to 1.8 for wild-type enzyme | Staphylococcus sp. |
V66L/G88V | pH-value, at which the acid-denaturation is half completed is 3.42, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 1.6 for the mutant enzyme compared to 1.8 for wild-type enzyme | Staphylococcus sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus sp. | - |
- |
- |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
4.15 | - |
pH-value, at which the acid-denaturation is half completed in wild-type enzyme | Staphylococcus sp. |