Any feedback?
Literature summary extracted from
- Purine nucleoside phosphorylases from hyperthermophilic Archaea require a CXC motif for stability and folding (2009), FEBS J., 276, 5799-5805.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 2.4.2.1 | C254S/C256S | after denaturation using 6 M guadinium HCl, mutant achieves a recovery of catalytic activity of 46% | Pyrococcus furiosus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 2.4.2.1 | Pyrococcus furiosus | - |
- |
- |
Renatured (Commentary)
| EC Number | Renatured (Comment) | Organism |
|---|---|---|
| 2.4.2.1 | 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)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.4.2.1 | additional information | enzyme is able to reactivate scrambled RNaseA | Pyrococcus furiosus | ? | - |
? |  |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
