EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.21.38 | proteolytic modification |
activation of the factor XII by proteolysis takes place in the presence of negatively charged materials. It is catalyzed by plasma enzymes, such as kallikrein, factor XIa and plasmin. Plasma kallikrein is probably the major activator under physiological conditions. High molecular weight kininogen stimulates the activation severalfold |
95422 |
| 3.4.21.38 | proteolytic modification |
activation of zymogen FXII to FXIIa by autoactivation |
707650 |
| 3.4.21.38 | proteolytic modification |
activation of zymogen FXII,i.e. Hageman factor, to FXIIa by autoactivation |
707649 |
| 3.4.21.38 | proteolytic modification |
amino acid substitutions around the cleavage site might explain the difference in sensitivity to activation between the human and guinea pig molecules |
95409 |
| 3.4.21.38 | proteolytic modification |
contains a C-terminal serine protease zymogen domain, which becomes activated upon contacting a negative surface |
653755 |
| 3.4.21.38 | proteolytic modification |
high molecular mass kininogen interferes with the binding of factor XII to sulfatides and its autoactivation |
670942 |
| 3.4.21.38 | proteolytic modification |
kallikrein mediates activation of the zymogen FXII. Although autohydrolysis of FXII by FXIIa may be a significant reaction in neat protein solutions, it is insignificant in plasma, autohydrolysis also is a negligible contributor to FXII activation in material-induced plasma coagulation |
709176 |
| 3.4.21.38 | proteolytic modification |
the conversion of factor XII to factor XIIa is due to the cleavage of a specific internal Arg-Val peptide bond |
95405, 95410 |
| 3.4.21.38 | proteolytic modification |
the zymogen is activated by Pseudomonas aeruginosa elastase. In this activation factor XII is cleaved in a limited fashion, liberating fragments with apparent molecular masses of 40000 Da and 30000 Da |
95425 |
| 3.4.21.38 | proteolytic modification |
when the contact phase of coagulation or fibrinolysis is initiated, factor XII is converted to factor XIIa by cleavage of a single internal Arg-Val peptide bond. This reaction occurs in the presence of kallikrein, an ionic surface, and high molecular weight kininogen |
95414 |
