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BRENDA support

Literature summary for 3.4.21.47 extracted from

  • Hourcade, D.E.; Mitchell, L.M.
    Access to the complement factor B scissile bond is facilitated by association of factor B with C3b protein (2011), J. Biol. Chem., 286, 35725-35732.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
E207A mutation in proenzyme factor B. Mutation disrupts salt bridge R234-E207, with little effects on the cleavage of proenzyme factor B Homo sapiens
E446V mutation in proenzyme factor B. Mutation disrupts salt bridge R234-E446 which partly stabilizes the complex C3bB(Mg2+) thereby inhibiting activation of the proenzyme Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

General Information

General Information Comment Organism
metabolism when factor B first associates with C3b, it bears two intact Arg234 salt bridges. The complex rapidly dissociates unless the Arg234-Glu446 salt bridge is released whereupon conformational changes occur that activate the metal ion-dependent adhesion site and partially stabilize the complex. The remaining salt bridge is then released, exposing the scissile bond and permitting factor D cleavage of proenzyme factor B Homo sapiens