EC Number   |
Activating Compound |
Reference |
|---|
   3.4.24.87 | Rituximab |
a monoclonal anti-CD 20 antibody, Rituximab leads to a prompt reduction in IgG antibody levels, followed by an increase in ADAMTS 13 activity increases. However, in patients receiving Rituximab electively, normalisation of ADAMTS 13 enzyme activity may be delayed for up to 3 months |
711559 |
| 3.4.24.87 | Ristocetin |
activates |
650715 |
| 3.4.24.87 | Urea |
activates at 1 M |
652481 |
| 3.4.24.87 | Urea |
activation, substrate is degraded at 1 M |
650717, 650725 |
| 3.4.24.87 | more |
antibodies that recognize domains T67, T8, and CUB domains have additive effects. Binding activates ADAMTS13 up to 4.2fold at pH 7.4, but antibodies have markedly decreased effects on ADAMTS13 activity at pH 6 |
735184 |
| 3.4.24.87 | von Willebrand factor |
binding to substrate von Willebrand factor D4 allosterically activates ADAMTS13, increasing its catalytic activity. Binding also positions ADAMTS13 on the substrate where it can act rapidly when shear stress exposes the scissile bond in the adjacent A2 domain |
735184 |
| 3.4.24.87 | more |
CCl4 at concentration of 6.5 mM does not directly enhance the activity of ADAMTS-13 |
670063 |
| 3.4.24.87 | more |
cleavage of von Willebrand factor A2 requires the force-induced A2 unfolding |
711576 |
| 3.4.24.87 | more |
coagulation factor VIII, platelet glycoprotein 1balpha, and heparin sulfate accelerate the cleavage of von Willebrand factor |
720833 |
| 3.4.24.87 | more |
in the absence of factor VIII, lyophilized platelets increase the formation of cleavage product by 2-3fold under fluid shear stresses. However, in the presence of physiological concentration of factor VIII (1 nM), the formation of von Willebrand factor cleavage product increases dramatically as a function of increasing platelets (150000 per microliter) with the maximal rate enhancement of about 8fold |
719881 |
