Vibriolysin
From Wikipedia, the free encyclopedia
Vibriolysin (EC 3.4.24.25, Aeromonas proteolytica neutral proteinase, aeromonolysin) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical reaction
- Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1'. Phe at P1' is the most favoured residue, which distinguished this enzyme from thermolysin
| Vibriolysin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.25 | ||||||||
| CAS no. | 69598-88-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
This thermostable enzyme is isolated from Vibrio proteolyticus.
