EC Number   |
Protein Variants |
Reference |
|---|
    4.1.1.11 | A128E |
naturally occuring mutation after treatment with pyrazinoic acid |
746598 |
| 4.1.1.11 | A128S |
naturally occuring mutation after treatment with pyrazinoic acid |
746598 |
| 4.1.1.11 | C17R |
naturally occuring mutation after treatment with pyrazinoic acid |
746598 |
| 4.1.1.11 | D116Y |
naturally occuring mutation after treatment with pyrazinoic acid |
746598 |
| 4.1.1.11 | D41G |
site-directed mutagenesis, the mutation improves the enzyme activity compared to wild-type |
-, 749207 |
| 4.1.1.11 | E130G |
naturally occuring mutation after treatment with pyrazinoic acid |
746598 |
| 4.1.1.11 | E56S |
site-directed mutagenesis, the Glu56Ser mutation improves the enzymatic activity and catalytic stability of L-aspartate alpha-decarboxylase for an efficient beta-alanine production, but no significant effect on the cell growth properties or the molecular weight of BsADC. The E56S mutant shows a 1.6fold higher activity and an approximately 1.4fold increased residual activity compared with the wild-type during 2 h reaction at 37°C, suggesting that the E56S mutation attenuates the mechanism-based inactivation of the enzyme. The mutant enzyme catalyzes the beta-alanine synthesis with a very high product yield of 215.3 g per liter culture. In BsADC, Glu56 corresponds to Ser56 in the center channel of the homotetramer ADC from Escherichia coli. Due to the shorter side chain of Ser56, the Glu56-to-Ser56 mutation may enhance the import of the Asp substrate and export of the beta-alanine product in the tetramer channel |
-, 749207 |
| 4.1.1.11 | F107L |
naturally occuring mutation after treatment with pyrazinoic acid |
746598 |
| 4.1.1.11 | G24S |
study of the structure and processing activity |
650998 |
| 4.1.1.11 | H11A |
study of the structure and processing activity |
650998 |
