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

BRENDA support

Literature summary 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

EC Number Activating Compound Comment Organism Structure
3.4.21.43 factor B the classical C5 convertase requires factor D, factor B, and properdin for activation and complex assembly Homo sapiens
3.4.21.43 factor D the classical C5 convertase requires factor D, factor B, and properdin for activation and complex assembly Homo sapiens
3.4.21.43 properdin the classical C5 convertase requires factor D, factor B, and properdin for activation and complex assembly Homo sapiens
3.4.21.47 factor B the classical C5 convertase requires factor D and factor B for activation and complex assembly Homo sapiens
3.4.21.47 factor D the classical C5 convertase requires factor D and factor B for activation and complex assembly Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.43 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
3.4.21.43 mouse anti human factor B antibody
-
Homo sapiens
3.4.21.43 thioredoxin 1 Trx-1, but not an active site mutated form, inhibits both C3 and C5 classical convertase formation, 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
3.4.21.47 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
3.4.21.47 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

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.43 cell surface
-
Homo sapiens 9986
-
3.4.21.47 cell surface
-
Homo sapiens 9986
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.43 Ca2+ dependent on Homo sapiens
3.4.21.43 Mg2+ required Homo sapiens
3.4.21.47 Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.43 Homo sapiens
-
-
-
3.4.21.47 Homo sapiens P00751
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.21.43 erythrocyte
-
Homo sapiens
-
3.4.21.47 erythrocyte
-
Homo sapiens
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
3.4.21.43 C3 convertase
-
Homo sapiens
3.4.21.43 C4b2a
-
Homo sapiens
3.4.21.43 C4b2aC3b
-
Homo sapiens
3.4.21.43 C5 convertase
-
Homo sapiens
3.4.21.43 classical C3 convertase
-
Homo sapiens
3.4.21.43 classical C5 convertase
-
Homo sapiens
3.4.21.47 alternative C3 convertase
-
Homo sapiens
3.4.21.47 alternative C5 convertase
-
Homo sapiens
3.4.21.47 C3 convertase
-
Homo sapiens
3.4.21.47 C3bBb
-
Homo sapiens
3.4.21.47 C3bBbC3b
-
Homo sapiens
3.4.21.47 C5 convertase
-
Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.21.43 37
-
assay at Homo sapiens
3.4.21.47 37
-
assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.21.43 7.3
-
assay at Homo sapiens
3.4.21.47 7.3
-
assay at Homo sapiens

General Information

EC Number General Information Comment Organism
3.4.21.43 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
3.4.21.43 additional information the classical C5 convertase requires factor D, factor B, and properdin for activation and complex assembly Homo sapiens
3.4.21.47 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
3.4.21.47 additional information the classical C5 convertase requires factor D and factor B for activation and complex assembly Homo sapiens