EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.17.20 | glycoprotein |
- |
668290, 707597 |
| 3.4.17.20 | glycoprotein |
5 N-glycosylation sites at Asn22, Asn51, Asn63, Asn86, and Asn219, detailed carbohydrate analysis, overview, no O-glycosylation |
667710 |
| 3.4.17.20 | glycoprotein |
different glycosylation patterns dependent on the enzyme source |
670940 |
| 3.4.17.20 | glycoprotein |
the activation peptide contains four potential N-linked glycosylation sites at Asn22, Asn51, Asn63 and Asn96. The 36000 catalytic unit of 309 amino acids is not glycosylated. The glycosylation of the activation peptide may act to stabilize and increase the half-life of circulating TAFI |
653977 |
| 3.4.17.20 | glycoprotein |
the enzyme contains 4 potential N-glycosylation sites at Asn22, Asn51, Asn63, and Asn96, carbohydrates account for 20% of total mass of TAFI and are responsable for stabilization |
668341 |
| 3.4.17.20 | proteolytic modification |
activation of TAFI to TAFIa by cleavage through thrombin, activation reaction kinetics with wild-type isozymes and mutant enzymes at 37°C and pH 7.4 |
669459 |
| 3.4.17.20 | proteolytic modification |
activation pathways overview, cleavage of the activation peptide from proCPU, in vitro catalyzed through thrombin, meizothrombin, plasmin, trypsin, or neutrophil elastase, only the thrombin cleaved enzyme is active, in vivo by the thrombin/thrombomodulin complex in a Ca2+-dependent manner, kinetics, overview, the plasminogen activation system, overview |
670940 |
| 3.4.17.20 | proteolytic modification |
Ca2+-dependent activation by thrombin at room temperature |
670945 |
| 3.4.17.20 | proteolytic modification |
Ca2+-dependent activation by thrombin/thrombumodulin or plasmin by cleavage of the activation peptide |
670059 |
| 3.4.17.20 | proteolytic modification |
Ca2+-dependent activation by thrombin/thrombumodulin or plasmin by cleavage of the activation peptide, in vitro activation by trypsin at 37°C and pH 7.5 |
667710 |
