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

Inhibitors

Inhibitors 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.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-amidino-2-naphthyl-4-guanidinobenzoate
-
Ab (2B7)
inhibits the deposition of C3b on Escherichia coli in hemolymph plasma, whereas it exhibits no inhibitory effect on the deposition of C3b on Staphylococcus aureus
-
Aurin tricarboxylic acid
blocks the alternative pathway at a downstream step from C3b attachment. It prevents formation of C3 convertase at the stage where Factor B, attached to the membrane-bound properdin-C3b-Factor B (PC3bB) complex, is cleaved by the protease action of Factor D to form the active C3 convertase enzyme PC3bBb. Activity is restored by the addition of excess Factor D to the serum. But membrane attack complex formation is still blocked by ATA at the stage of C9 addition to C5b678. It has no effect on the classical pathway activation. Binding of aurin tricarboxylic acid to the QPDTIDHDLLLLQLS site blocks the ability of aurin tricarboxylic acid to bind to Factor D protein
C3b-specific antibody fragment S77
-
inhibits the alternative pathway C5 convertase in human serum
-
C4BP
-
the inhibitor blocks both C3 and C5 conversion
-
complement factor H-related protein 1
-
0.005-0.16 mg/ml inhibits C5 convertase activity
-
complement receptor 1
CR1, mediates decay acceleration of the C3bBb complex
-
complement receptor of immunoglobulin family
-
the inhibitor blocks both C3 and C5 conversion
-
Cp40
-
the inhibitor blocks both C3 and C5 conversion
-
CRIg
phagocytic receptor, binds to the beta-chain of complement components C3b and C3c and inhibits the AP C3 and C5 convertases, structure-activity relationship of CRIg mutants indicated
-
decay accelerating factor
DAF, mediates decay acceleration of the C3bBb complex
-
decay-accelerating factor
DAF, CD55, major site of interaction with the larger cleavage subunit complement component factor B (Bb), interaction pathway dissected, second short consensus repeat (SCR) domain of DAF (SCR2) interacts only with fragment Bb, whereas SCR4 interacts with complement component C3b, SCR3 does not directly interact with either subunit
-
diisopropyl phosphate
-
eculizumab
-
EDTA
-
-
Efb-C
-
C-terminal region of extracellular fibrinogen binding protein. The inhibitor specifically blocks C5 conversion, while leaving C3 conversion unaffected
-
extracellular complement binding protein
-
the inhibitor specifically blocks C5 conversion, while leaving C3 conversion unaffected
-
factor H
-
factor H related-protein 5
-
inhibits C5 conversion in a concentration-dependent manner
-
hemocyanin-depleted plasma
preincubation of hemocyanin-depleted plasma with the anti-factor C Ab (2B7) dose-dependently inhibits the proteolytic conversion of C3 to C3b in the presence of LPS
-
hydroxylamine
inactivates the thioester bond on C3, dramatically decreases the deposition of C3b on microbes
Leu-Gly-Leu-Ala-Arg-sarcosine
-
inhibits C5 cleavage
OmCI
-
the inhibitor blocks C5 cleavage by interfering with convertase recognition far from C5a
-
Ornithodoros moubata complement inhibitory protein
-
the inhibitor specifically interfers with C5 conversion but not C3 conversion
-
Pra1
-
i. e. Candida albicans complement regulator acquiring surface protein 2 or pH-regulated Ag 1. In the direct surrounding of the pathogen, inhibitor binds to fluid-phase C3, blocks cleavage of C3 to C3a and C3b and inhibits complement activation via the alternative and classical pathways. In addition, the release of the anaphylatoxins C3a and C5a, as well as C3b/iC3b surface deposition, is reduced. By reducing C3b/iC3b levels at the yeast surface, Pra1 decreases complement-mediated adhesion, as well as uptake of Candida albicans by human macrophages
-
soluble complement receptor type 1
-
-
-
SSL7
-
the inhibitor blocks C5 cleavage by interfering with convertase recognition far from C5a
-
staphylococcal complement inhibitor
-
thioredoxin 1
Trx-1, causes significant inhibition of alternative convertases, mechanism, overview. Trx-1 is capable of inhibiting all classical and alternative convertases but its effect is more pronounced in inhibition of alternative ones
TT30
-
TT32
-
human complement receptor type 2 (CR2)/CR1 fusion protein
-
additional information
-