Sedolisin
The sedolisin (MEROPS S53) family of peptidases are a family of serine proteases structurally related to the subtilisin (S8) family. Well-known members of this family include sedolisin ("pseudomonalisin") found in Pseudomonas bacteria, xanthomonalisin ("sedolisin-B"), physarolisin as well as animal tripeptidyl peptidase I. It is also known as sedolysin or serine-carboxyl peptidase. This group of enzymes contains a variation on the catalytic triad: unlike S8 which uses Ser-His-Asp, this group runs on Ser-Glu-Asp, with an additional acidic residue Asp in the oxyanion hole.
| S8/S53 domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Peptidase_S8 | ||||||||
| Pfam | PF00082 | ||||||||
| InterPro | IPR000209 | ||||||||
| PROSITE | PDOC00125 | ||||||||
| CATH | 1GA6 | ||||||||
| SCOP2 | 1GA6 / SCOPe / SUPFAM | ||||||||
| CDD | cd07477 | ||||||||
| |||||||||
Their optimal pH is around 3. Most members of the family are produced as a precursor protein with N-terminal (InterPro: IPR015366) and sometimes C-terminal peptides that need to be cleaved off.