Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.4.21.47: alternative-complement-pathway C3/C5 convertase

This is an abbreviated version!
For detailed information about alternative-complement-pathway C3/C5 convertase, go to the full flat file.

Word Map on EC 3.4.21.47

Reaction

Cleavage of Arg-/-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg-/- bond in complement component C5 alpha-chain to yield C5a and C5b =

Synonyms

(C3b)n,Bb, (CVF)-dependent glycine-rich-beta-glucoprotein, alternative C3 convertase, alternative C5 convertase, alternative complement pathway C3 convertase, alternative complement pathway C3(C5) convertase, alternative pathway C3 convertase, alternative pathway C3 convertase complex, alternative pathway C3-convertase, alternative pathway C3/C5 convertase, alternative pathway C5 convertase, alternative pathway of complement C3/C5 convertase, alternative-complement-pathway C3/C5 convertase, AP C3 convertase, AP C3-convertase, AP C3/C5 convertase, AP C5 convertase, APC C3/C5 convertase, C3 convertase, C3 proactivator, C3/C5 convertase, C3b,Bb, C3b2, C3bB complex, C3bBb, C3bBb convertase, C3bBb(C3b)n, C3bBb3b, C3bBbC3b, C5 convertase, cobra venom factor-dependent C3 convertase, complement alternative pathway C3 convertase, complement C 3(C 5) convertase (amplification), complement C5 convertase, complement component C3/C5 convertase (alternative), convertase, complement C3(C5) (amplification), CVF,Bb, CVFh,Bb, CVFn,Bb, GBG, Glycine-rich beta glycoprotein, heat-labile factor, PBF2, proenzyme factor B, properdin factor B

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.47 alternative-complement-pathway C3/C5 convertase

Crystallization

Crystallization on EC 3.4.21.47 - alternative-complement-pathway C3/C5 convertase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
C3 convertase formed by C3b and the protease fragment Bb in complex with staphylococcal complement inhibitor, hanging drop vapor diffusion method, using 75 mM sodium/potassium tartrate, 8.0% (w/v) PEG 3350, 50 mM Bis-Tris propane, pH 6.5
-
crystal structures of the pro-convertase C3bB at 4 A resolution and its complex with factor D at 3.5 A resolution. Factor B binding to C3b forms an open activation state of C3bB. Factor D specifically binds the open conformation of factor B through a site distant from the catalytic center and is activated by the substrate, which displaces factor D’s self-inhibitory loop. This concerted proteolytic mechanism, which is cofactordependent and substrate-induced, restricts complement amplification to C3b-tagged target cells
engineered subunit Bb with Cys-resiudes at positions 435 and 428, in complex with inhibitors 6-amidino-2-naphthyl-4-guanidinobenzoate or diisopropyl phosphate
in complex with factor H, hanging drop vapor diffusion method, using 7.0% (w/v) PEG 3350, 70 mM ammonium acetate, pH 7.1, at 18°C
-
structural analysis of complement component C3b in complex with the macrophage-expressed complement receptor CRIg, domain architecture of complement component C3 and the C3b/C3c-CRIg complexes shown, structural similarities between complement components C3b and C3c indicated, comparison between complement components C3b and C3 reveals that complement component C3 stimulation is accompanied by major strucural rearrangements