EC Number   |
Protein Variants |
Reference |
|---|
    2.8.1.1 | Arg |
one additional Arg residue at the 3'-end followed by a TAA stop codon, no significant changes to the wild-type enzyme |
645529 |
| 2.8.1.1 | C247S |
no activity to thiosulfate |
645528 |
| 2.8.1.1 | C254S |
more resistant than wild-type to inactivation by dithiothreitol, more readily reactivated following oxidative inactivation and increased exposure of hydrophobic surfaces following removal of the transferable sulfur |
645528 |
| 2.8.1.1 | C254S/C263S |
less stable in urea than wild type, more resistant than wild-type to inactivation by dithiothreitol, more readily reactivated following oxidative inactivation and increased exposure of hydrophobic surfaces following removal of the transferable sulfur |
645528 |
| 2.8.1.1 | C263S |
less stable in urea than wild type |
645528 |
| 2.8.1.1 | C266S |
activity is completely abolished, similar to wild-type, mutant is able to form high molecular weight oligomers (> 600 kDa) |
-, 760422 |
| 2.8.1.1 | C332S |
mutation leads to higher rigidity of the molecule |
672482 |
| 2.8.1.1 | C339V |
no conformational changes |
672482 |
| 2.8.1.1 | C33S |
about 3fold increase in sulfurtransferase activity, mutation destabilizes the quaternary structure |
-, 760422 |
| 2.8.1.1 | C3S |
mutant enzyme is fully active but less stable than wild-type enzyme, mutant enzyme has more easily exposed apparent hydrophobic surfaces than wild-type enzyme |
663321 |
