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Literature summary for 4.2.2.2 extracted from
- The stability, structural organization, and denaturation of pectate lyase C, a parallel beta-helix protein (2000), Biochemistry, 39, 15932-15943.
General Stability
| General Stability | Organism |
|---|---|
| complete unfolding in 6 M guanidine-HCl | Dickeya chrysanthemi |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Dickeya chrysanthemi | - |
- |
- |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| after complete unfolding in 6 M guanidine-HCl and removal of the denaturant by dialysis, the enzymatic activity of pelC is regained and is identical to that of freshly purified enzyme. Thermal denaturation is not reversible | Dickeya chrysanthemi |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| pectate lyase C | - |
Dickeya chrysanthemi |
| pelC | - |
Dickeya chrysanthemi |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
thermal denaturation is not reversible. The enzyme has its maximal thermal stability at pH 5, CD-monitored thermal denaturation | Dickeya chrysanthemi |
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