EC Number   |
Protein Variants |
Reference |
|---|
   3.4.19.3 | A199P |
alpha6-helix region of A199P in the D1 state (initial denatured state) is partially unprotected, while some hydrophobic residues are protected against H/D exchange, although these hydrophobic residues are unprotected in the wild-type protein. Structure of A199P in the D1 state forms a temporary stable denatured structure with a non-native hydrophobic cluster and the unstructured alpha6-helix |
678264 |
| 3.4.19.3 | C142S |
complete loss of the activity |
722561 |
| 3.4.19.3 | C142S/C188S |
mutant enzyme loses its activity completely |
651099 |
| 3.4.19.3 | C142S/C188S |
small thermodynamic stability of the mutant enzyme C142S/C188S at low pH. The mutant enzyme is monomeric below pH 2.7, dimeric around pH 3 and tetrameric above pH 4.5. The heat-denaturation of the mutant enzyme is completely reversible at pH 2.3, although the unfolding-refolding reactions are characterized by extremely slow kinetics |
652880 |
| 3.4.19.3 | C142S/C188S |
the mutant enzyme is used in unfolding and refolding experiments to exclude the complexity in reaction due to oxidation of SH groups |
95297 |
| 3.4.19.3 | C142S/C188S/E192A |
at acidic pH the mutant enzyme is less stable than cysteine-free mutant C142S/C188S. At alkaline pH the mutant enzyme is more stable than cysteine-free mutant C142S/C188S. The thermal stability of the mutant enzyme at pH 2.15, pH 3.04 and pH 7.3 is less than that of the cysteine-free mutant enzyme C142S/C188S. At pH 8.7 and 9.6 the thermal stability of mutant enzyme is higher than that of the cysteine-free mutant C142S/C188S |
667733 |
| 3.4.19.3 | C142S/C188S/E192D |
at acidic pH the mutant enzyme is less stable than cysteine-free mutant C142S/C188S. The thermal stability of the mutant enzyme at pH 2.15, pH 3.04, pH 7.3, pH 8.7 and pH 9.6 is less than that of the cysteine-free mutant enzyme C142S/C188S |
667733 |
| 3.4.19.3 | C142S/C188S/E192I |
at acidic pH the mutant enzyme is less stable than cysteine-free mutant C142S/C188S. At alkaline pH the mutant enzyme is more stable than cysteine-free mutant C142S/C188S. The thermal stability of the mutant enzyme at pH 2.15, pH 3.04 and pH 7.3 is less than that of the cysteine-free mutant enzyme C142S/C188S. At pH 8.7 and 9.6 the thermal stability of mutant enzyme is higher than that of the cysteine-free mutant C142S/C188S |
667733 |
| 3.4.19.3 | C142S/C188S/E192Q |
at acidic pH the mutant enzyme is less stable than cysteine-free mutant C142S/C188S. At alkaline pH the mutant enzyme is more stable than cysteine-free mutant C142S/C188S. The thermal stability of the mutant enzyme at pH 2.15, pH 3.04 and pH 7.3 is less than that of the cysteine-free mutant enzyme C142S/C188S. At pH 8.7 and 9.6 the thermal stability of mutant enzyme is higher than that of the cysteine-free mutant C142S/C188S |
667733 |
| 3.4.19.3 | C142S/C188S/E192V |
at acidic pH the mutant enzyme is less stable than cysteine-free mutant C142S/C188S. At alkaline pH the mutant enzyme is more stable than cysteine-free mutant C142S/C188S. The thermal stability of the mutant enzyme at pH 2.15, pH 3.04 and pH 7.3 is less than that of the cysteine-free mutant enzyme C142S/C188S. At pH 8.7 and 9.6 the thermal stability of mutant enzyme is higher than that of the cysteine-free mutant C142S/C188S |
667733 |
