EC Number   |
Protein Variants |
Reference |
|---|
    3.8.1.2 | D10N |
Asn10 of the mutant enzyme is spontaneously deaminated to yield Asp, though slowly, causing increasing activity of the mutant preparation |
-, 648317 |
| 3.8.1.2 | D11E |
totally inactive in catalysis |
-, 648308 |
| 3.8.1.2 | D11N |
totally inactive in catalysis |
-, 648308 |
| 3.8.1.2 | D11S |
totally inactive in catalysis |
-, 648308 |
| 3.8.1.2 | D13A |
significant decrease in the free energy of binding for the DehL-L-2-chloropropionic acid model complex, indicating the involvement of the residue in catalysis and/or structural integrity of the active site |
756515 |
| 3.8.1.2 | D180A |
site-directed mutagenesis of a residue that strongly interacts with the substrate |
-, 719121 |
| 3.8.1.2 | D181N |
totally inactive in catalysis |
-, 648308 |
| 3.8.1.2 | H184A |
significant decrease in the free energy of binding for the DehL-L-2-chloropropionic acid model complex, indicating the involvement of the residue in catalysis and/or structural integrity of the active site |
756515 |
| 3.8.1.2 | H184Y |
mutation significantly increases the binding strength of the enzyme towards D-2-chloropropionate |
757450 |
| 3.8.1.2 | I186Y |
mutation significantly increases the binding strength of the enzyme towards D-2-chloropropionate |
757450 |
