EC Number   |
Protein Variants |
Reference |
|---|
   3.4.14.4 | C518S |
mutation of the cysteine residue |
707596 |
| 3.4.14.4 | C519A |
activity similar to wild type |
649555 |
| 3.4.14.4 | C626S |
mutation of the cysteine residue |
707596 |
| 3.4.14.4 | C639S |
mutant, resistance against p-hydroxy-mercuribenzoate |
707596 |
| 3.4.14.4 | C654A |
activity similar to wild type |
649555 |
| 3.4.14.4 | C701A |
activity similar to wild type |
649555 |
| 3.4.14.4 | D372A |
residue Asp372 plays a crucial role in the large scale interdomain closure. During the MD simulation time, the variant remains more open than the wild type protein. Apparently, Ala is not as efficient as Asp in establishing the interdomain interactions |
732223 |
| 3.4.14.4 | D496G |
mutation in S2 subsite, mutant has lost selectivity due to the increase of the Km value. Mutant shows significantly decreased binding of peptides with N-terminal arginine, and of tynorphin |
731407 |
| 3.4.14.4 | G313A |
mutation detected in human cancer, strong decrease in activity. Mutation significantly increases the enzyme flexibility, particularly that of the binding site including the H450ELLGH455 motif, and influences the substrate interactions with the catalytic His568 |
755384 |
| 3.4.14.4 | G313W |
mutation detected in human cancer, almost abolishes activity |
755384 |
