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Literature summary for 2.4.2.1 extracted from
- Purine nucleoside phosphorylases from hyperthermophilic Archaea require a CXC motif for stability and folding (2009), FEBS J., 276, 5799-5805.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C254S/C256S | after denaturation using 6 M guadinium HCl, mutant achieves a recovery of catalytic activity of 46% | Pyrococcus furiosus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus furiosus | - |
- |
- |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| the CXC motif is necessary to obtain complete renaturation from the unfolded state. After denaturation using 6 M guadinium HCl, wild-type is able to achieve a recovery of catalytic activity of 90%. Sequence NH2-RRCGCKD-COOH acts as in vitro catalyst of oxidative protein folding | Pyrococcus furiosus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | enzyme is able to reactivate scrambled RNaseA | Pyrococcus furiosus | ? | - |
? |  |
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