| Activity |
|---|
| Catalytic type | Serine |
| Peplist | Included in the Peplist with identifier PL00310 |
| NC-IUBMB | Subclass 3.4 (Peptidases) >> Sub-subclass 3.4.21 (Serine endopeptidases) >> Peptidase 3.4.21.6
|
| Enzymology | BRENDA database |
| Proteolytic events | CutDB database (14 cleavages) |
| Activity status | human: active (Brown et al., 2004)
mouse: active (Heidtmann et al., 1998)
|
| Biotechnology | Reagent for cleavage of recombinant fusion proteins (Jenny et al., 2003). |
| Physiology | Converts prothrombin to thrombin in blood coagulation, and can also activate factors V, VII and VIII. |
| Knockout | Knockout mice have been described by Dewerchin et al. (2000), and suggested to form an effective model for the bleeding disorders observed in severe factor X deficiency in humans. |
| Pharmaceutical relevance | Because of its role in converting prothrombin to thrombin in blood coagulation, activated factor X is a drug target for control of coagulation (Choi-Sledeski et al., 2003). It has been reported that synthetic inhibitors are effective antithrombotic agents in animal models, with a low risk of bleeding (Ieko et al., 2004). |
| Pathways |
KEGG | Complement and coagulation cascades |
|
Other databases
| WIKIPEDIA | http://en.wikipedia.org/wiki/Coagulation_factor_Xa |
| Cleavage site specificity |
Explanations of how to interpret the
following cleavage site sequence logo and specificity matrix can be found here. |
|---|
| Cleavage pattern | a/-/Gpfe/R tsi/v/-/g (based on 63 cleavages) |
FGGx