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Literature summary for 3.4.22.8 extracted from
- Clostripain linker deletion variants yield active enzyme in Escherichia coli: a possible function of the linker peptide as intramolecular inhibitor of clostripain automaturation (1996), Curr. Microbiol., 33, 281-286.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Hathewaya histolytica |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C231S | heterodimer formation is largely impaired | Hathewaya histolytica |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Hathewaya histolytica | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | the clostripain core protein is composed of the light and the heavy chain subunits linked by a nonapeptide into a single polypeptide chain. Linker removal is due to autocatalytic processing yielding active heterodimeric enzyme. The linker nonapeptide serves as an important transient intramolecular inhibitor in the cellular self-defense program evolved by the natural host Clostridium histolyticum | Hathewaya histolytica |
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