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

BRENDA support

Literature summary for 3.4.21.47 extracted from

  • Okroj, M.; Holmquist, E.; King, B.C.; Blom, A.M.
    Functional analyses of complement convertases using C3 and C5-depleted sera (2012), PLoS ONE, 7, e47245.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
factor B the classical C5 convertase requires factor D and factor B for activation and complex assembly Homo sapiens
factor D the classical C5 convertase requires factor D and factor B for activation and complex assembly Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information addition of guinea pig serum in 40 mM EDTA initiates lysis of existing convertase complexes and excludes the possibility of de novo convertase formation Homo sapiens
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 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface
-
Homo sapiens 9986
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
complement component C3 zymogen + H2O Homo sapiens activation complement component C3b + complement component C3a
-
?
complement component C5 zymogen + H2O Homo sapiens activation complement component C5b + complement component C5a
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P00751
-
-

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
complement component C3 zymogen + H2O
-
Homo sapiens complement component C3b + complement component C3a
-
?
complement component C3 zymogen + H2O activation Homo sapiens complement component C3b + complement component C3a
-
?
complement component C5 zymogen + H2O
-
Homo sapiens complement component C5b + complement component C5a
-
?
complement component C5 zymogen + H2O activation Homo sapiens complement component C5b + complement component C5a
-
?

Synonyms

Synonyms Comment Organism
alternative C3 convertase
-
Homo sapiens
alternative C5 convertase
-
Homo sapiens
C3 convertase
-
Homo sapiens
C3bBb
-
Homo sapiens
C3bBbC3b
-
Homo sapiens
C5 convertase
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
assay at Homo sapiens

General Information

General Information Comment Organism
metabolism all pathways converge at the level of the C3 molecule, where downstream events can be amplified by a mechanism of positive feedback supported by complement convertases: the classical/lectin pathway C3 convertase (C4b2a) or the alternative pathway C3 convertase (C3bBb). These convertases further cleave C3 to C3b and C3a, of which C3b binds to nearby surfaces, providing a convertase assembly platform, or to pre-assembled C3 convertases, switching them to C5 convertases (C4b2aC3b or C3bBbC3b, respectively). The C5 convertase cleaves C5 molecules to C5a and C5b and the latter initiates formation of the membrane attack complex (MAC, C5b678polyC9) and its insertion into a target membrane. Enzyme regulation, overview Homo sapiens
additional information the classical C5 convertase requires factor D and factor B for activation and complex assembly Homo sapiens