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Literature summary for 3.4.19.3 extracted from
- Structural characterization of a trapped folding intermediate of pyrrolidone carboxyl peptidase from a hyperthermophile (2012), Biochemistry, 51, 6089-6096.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| Cys144Ser/Cys188Ser | cysteine-free variant. The 114-208 segment of the mutant folds into a stable compact structure with non-native helix-helix association in the D1 state. In the folding process from the D1 state to the native state, the alpha4- and alpha6-helices become separated and the central beta-sheet is folded between these helices. The non-native interaction between the alpha4- and alpha6-helices may be responsible for the unusually slow folding of the mutant | Pyrococcus furiosus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus furiosus | O73944 | - |
- |
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Release 2023.1 (January 2023)
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