| Activity |
|---|
| Catalytic type | Cysteine |
| Peplist | Included in the Peplist with identifier PL00068 |
| NC-IUBMB | Subclass 3.4 (Peptidases) >> Sub-subclass 3.4.14 (Dipeptidyl-peptidase and tripeptidyl-peptidases) >> Peptidase 3.4.14.1
|
| Enzymology | BRENDA database |
| Activity status | human: active (Turk et al., 2004)
mouse: active (Adkison et al., 2002)
|
| Physiology | A function is the activation of granulocyte serine endopeptidases by removal of N-terminal dipeptides (e.g. Pham et al., 1999). |
| Knockout | Mutations in the gene for dipeptidyl-peptidase I lead to Papillon-Lefevre syndrome, an autosomal recessive disorder characterised by palmoplantar keratoderma and severe, early onset periodontitis (Hart et al., 1999; Toomes et al., 1999; Hart et al., 2000). Haim-Munk syndrome is also caused by mutations in dipeptidyl-peptidase I (Cury et al., 2005). |
| Pharmaceutical relevance | Mice lacking dipeptidyl-peptidase I showed improved survival of sepsis, suggesting that the peptidase may be a therapeutic target for treatment of sepsis (Mallen-St Clair et al., 2004). |
| Pathways |
KEGG | Lysosome |
|
Other databases
| WIKIPEDIA | http://en.wikipedia.org/wiki/Cathepsin_C |
| Cleavage site specificity |
Explanations of how to interpret the
following cleavage site sequence logo and specificity matrix can be found here. |
|---|
| Cleavage pattern | -/s/-/es -/-/-/gr (based on 33 cleavages) |
