| Activity |
|---|
| Catalytic type | Serine |
| Peplist | Included in the Peplist with identifier PL00308 |
| NC-IUBMB | Subclass 3.4 (Peptidases) >> Sub-subclass 3.4.21 (Serine endopeptidases) >> Peptidase 3.4.21.22
|
| Enzymology | BRENDA database |
| Proteolytic events | CutDB database (3 cleavages) |
| Activity status | human: active (Schmidt & Bajaj, 2004)
mouse: active (Kundu et al., 1998)
|
| Physiology | Formed from coagulation factor IX by the action of factor XIa or factor VIIa. Factor IXa then proteolytically activates coagulation factor X, and may act on factor VII also (Bajaj et al., 2004). |
| Knockout | Hereditary deficiency is the cause of hemophila B, which is X-linked. A variety of different mutations are known (Giannelli et al., 1996). Knockout mice also have a severe bleeding disorder (Kundu et al., 1998). |
| Pharmaceutical relevance | A possible target for gene therapy of hemophilia B (Kundu et al., 1998). In a rat model of thromboembolic stroke, an inhibitory monoclonal antibody gave promising results, and within four hours of stroke produced a more favorable outcome than tissue-type plasminogen activator (Toomey et al., 2002). Administration of recombinant factor IX is reportedly a safe and effective treatment for hemophilia B (Shapiro et al., 2004). |
| Pathways |
KEGG | Complement and coagulation cascades |
|
Other databases
| WIKIPEDIA | http://en.wikipedia.org/wiki/Coagulation_factor_Ixa |
| Cleavage site specificity |
Explanations of how to interpret the
following cleavage site sequence logo and specificity matrix can be found here. |
|---|
| Cleavage pattern | -/-/g/R -/-/-/- (based on 12 cleavages) |
