EC Number   |
Activating Compound |
Reference |
|---|
   3.4.21.43 | beta-amyloid peptide |
i.e. Abeta1-42, activates |
81410 |
| 3.4.21.43 | C3b |
both the soluble form of the enzyme, C4b,C2a and the surface-bound form of the enzyme EAC1,C4b,C2a exhibit a poor affinity for the substrate C5. Very high affinity C5 convertase is generated only when the low affinity C3/C5 convertases are allowed to deposit C3b by cleaving native C3 |
652460 |
| 3.4.21.43 | complement C2 |
provides catalytic activity for the C3 convertase C4bC2a |
695326 |
| 3.4.21.43 | complement component C2b |
essential for the interaction of C4b and C2a |
81407 |
| 3.4.21.43 | complement component C3b |
in inactive surface-fixed form essential for cleavage of C5 |
81408 |
| 3.4.21.43 | factor B |
the classical C5 convertase requires factor D, factor B, and properdin for activation and complex assembly |
732705 |
| 3.4.21.43 | factor D |
the classical C5 convertase requires factor D, factor B, and properdin for activation and complex assembly |
732705 |
| 3.4.21.43 | more |
complement activation via the lectin pathway on zymosan particles is at least 4times more efficient than via the classical pathway on sheep erythrocytes coated with antibody. Every C4b deposited via the lectin pathway is capable of forming a convertase in contrast to only one of four C4b molecules deposited via the classical pathway. Rate of formation of lectin pathway C3/C5 convertases depends on the activation of C4 and C2 by MASP-2 |
698871 |
| 3.4.21.43 | more |
cooperation of the enzyme with MBL-associated serine proteases MASP-1 and MASP-2 in C3 cleavage, the serine proteases generate active C3 convertase at high serum concentration, while MASP-3 inhibits it, overview |
680169 |
| 3.4.21.43 | more |
molecular interactions between MASP-2, C4, and C2 and their activation fragments leading to complement activation via the lectin pathway, overview |
683669 |
