EC Number   |
Protein Variants |
Reference |
|---|
    4.2.1.1 | A23C/L203C/C206S |
mutant retains high catalytic efficiency, and differential scanning calorimetry shows acid stability and thermal stability that is enhanced compared with native enzyme |
728868 |
| 4.2.1.1 | A65L |
site-specific mutagenesis, enhancement of activity with all substrates, about 5fold increase in activity with 4-nitrophenyl acetate |
651052 |
| 4.2.1.1 | A65L/T200G |
site-specific mutagenesis, 5fold increase in activity with 4-nitrophenylacetate |
651052 |
| 4.2.1.1 | A65L/T200R |
site-specific mutagenesis, 4fold increase in activity with 4-nitrophenylacetate |
651052 |
| 4.2.1.1 | A65S |
the mutation can cause variations in binding affinity of small molecule inhibitors |
696308 |
| 4.2.1.1 | A65S/N67Q/E69T/I91L/F131V/K170E/L204A |
site-directed mutagenesis, active site mutant |
747545 |
| 4.2.1.1 | C148S |
the mutation eliminate potential problems with the oxidation of the single cysteine residue at position 148 |
728719 |
| 4.2.1.1 | C160S |
completely inactive |
33593 |
| 4.2.1.1 | C183S/C188S |
mutations at positions 183 and 188 are to enhance crystallization by removing oxidizable cysteine residues. The positions of residues 183 and 188 are solvent exposed on the side of the enzyme opposite to the active site. The mutations C183S and C188S do not affect catalysis |
664052 |
| 4.2.1.1 | C223S |
completely inactive |
33593 |
