EC Number   |
Protein Variants |
Reference |
|---|
    6.3.4.6 | D1321A |
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme |
-, 727941 |
| 6.3.4.6 | D1584N |
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme |
-, 727941 |
| 6.3.4.6 | E1792A |
the mutant shows reduced catalytic efficiency compared to the wild type enzyme |
727941 |
| 6.3.4.6 | G559E/G572E |
mutation renders the protein monomeric |
-, 744532 |
| 6.3.4.6 | K1605A |
mutation in active site of the carboxylyase. A mixture of mutants K1605A and S177A is as efficient as wild-type |
-, 744532 |
| 6.3.4.6 | K1605A |
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme |
-, 727941 |
| 6.3.4.6 | S177A |
mutation in the active site of the allophanate hydrolase. A mixture of mutants K1605A and S177A is as efficient as wild-type |
-, 744532 |
| 6.3.4.6 | Y1324F |
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme |
-, 727941 |
| 6.3.4.6 | Y1628F |
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme |
-, 727941 |
