EC Number   |
Protein Variants |
Reference |
|---|
    3.6.1.1 | A226S |
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme |
667786 |
| 3.6.1.1 | A238S |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
667786 |
| 3.6.1.1 | C16S |
site-directed mutagenesis, the mutant shows a loss of 50% activity and a reduction in sensitivity to reductants and oxidized glutathione compared to the wild-type enzyme. In addition, the replacement causes a considerable disruption in thermostability, C16S substitution destabilizes PPase through impairing trimer-trimer interactions |
684755 |
| 3.6.1.1 | D102N |
site-directed mutagenesis, the active site residue mutation does only marginally influence the pH-dependence of fluoride inhibition |
688341 |
| 3.6.1.1 | D102V |
large decrease in metal binding affinity |
654598 |
| 3.6.1.1 | D103N |
site-directed mutagenesis |
756011 |
| 3.6.1.1 | D115E |
site-directed mutagenesis, the mutation affects metal binding and the hydrogen bonding network in the active, in contrary to the wild-type enzyme, the mutant shows an open conformation variant of the hitherto unobserved two-phosphate and two bridging water active site, crystal structure determination with bound phosphate and Mg2+, and comparison to the wild-type enzyme structure |
685100 |
| 3.6.1.1 | D117E |
site-directed mutagenesis, crystal structure determination with bound phosphate and Mg2+, and comparison to the wild-type enzyme structure |
685100 |
| 3.6.1.1 | D11N |
site-directed mutagenesis, inactive mutant |
718917 |
| 3.6.1.1 | D120E |
site-directed mutagenesis, crystal structure determination with bound phosphate and Mg2+, and comparison to the wild-type enzyme structure |
685100 |
