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C3 zymogen + H2O
C3b + C3a
C5 zymogen + H2O
C5b + C5a
complement component C3 + H2O
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Substrates: classical pathway of the complement system
Products: -
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complement component C3 + H2O
complement component C3a + complement component C3b
complement component C3 + H2O
component C3b + anaphylatoxin C3a
complement component C5 + H2O
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Substrates: activity of enzyme bound to component C3b
Products: -
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complement component C5 + H2O
complement component C5a + complement component C5b
complement componentC3 + H2O
complement component C3a + complement component C3b
additional information
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C3 zymogen + H2O
C3b + C3a
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Substrates: -
Products: -
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C3 zymogen + H2O
C3b + C3a
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Substrates: activation
Products: -
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C5 zymogen + H2O
C5b + C5a
-
Substrates: -
Products: -
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C5 zymogen + H2O
C5b + C5a
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Substrates: activation
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complement component C3 + H2O
complement component C3a + complement component C3b
-
Substrates: -
Products: -
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complement component C3 + H2O
complement component C3a + complement component C3b
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Substrates: hydrolyzes peptide bond Arg77-Ser of the alpha-chain of C3
Products: -
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complement component C3 + H2O
complement component C3a + complement component C3b
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Substrates: complement component C3 is the preferred substrate. Cleavage of the preferred C3 substrate and deposition of C3b effectively switches the output of the enzyme from C3b to C5b, resulting in initiation of the cytosolic process of complement
Products: -
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complement component C3 + H2O
complement component C3a + complement component C3b
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Substrates: C3 complement cleavage is a central event in the activation of the complement system via the classical, the alternative, and the lectin pathway, overview
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complement component C3 + H2O
complement component C3a + complement component C3b
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Substrates: -
Products: -
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complement component C3 + H2O
complement component C3a + complement component C3b
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Substrates: -
Products: -
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complement component C3 + H2O
component C3b + anaphylatoxin C3a
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Substrates: -
Products: -
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complement component C3 + H2O
component C3b + anaphylatoxin C3a
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Substrates: -
Products: iC3b is generated by Factor I after formation of C3b. iC3b is a proteolytically inactive form of C3b that retains the ability to opsonize microbes, but cannot participate in convertase function
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complement component C5 + H2O
complement component C5a + complement component C5b
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Substrates: -
Products: -
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complement component C5 + H2O
complement component C5a + complement component C5b
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Substrates: hydrolyzes peptide bond Arg77 of the alpha-chain of complement component C5, cleavage of C5 requires complement fragment C3b which binds C5 and renders it susceptible to cleavage by the C4b,C2a complex
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complement component C5 + H2O
complement component C5a + complement component C5b
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Substrates: C5 convertases C4b2aC3b and C3b 2 Bb
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complement component C5 + H2O
complement component C5a + complement component C5b
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Substrates: C5 convertases, C4b2a3b and C3b2Bb, cleave C5 into the anaphylatoxin C5a and C5b followed by initiation of the terminal pathway, leading to formation of lytic C5b-9 membrane attack complexes, overview
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complement component C5 + H2O
complement component C5a + complement component C5b
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Substrates: C5 convertases, C4b2a3b and C3b2Bb, cleave C5 into the anaphylatoxin C5a and C5b, overview
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complement component C5 + H2O
complement component C5a + complement component C5b
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Substrates: -
Products: -
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complement component C5 + H2O
complement component C5a + complement component C5b
-
Substrates: -
Products: -
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complement component C5 + H2O
complement component C5a + complement component C5b
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Substrates: C5 convertases, C4b2a3b and C3b2Bb, cleave C5 into the anaphylatoxin C5a and C5b, overview
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complement componentC3 + H2O
complement component C3a + complement component C3b
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Substrates: C3 convertase C3bBb
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complement componentC3 + H2O
complement component C3a + complement component C3b
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Substrates: C3 convertases, C4b2a and C3bBb, cleave C3 into the anaphylatoxin C3a and C3b, overview
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complement componentC3 + H2O
complement component C3a + complement component C3b
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Substrates: C3 convertases, C4b2a and C3bBb, cleave C3 into the anaphylatoxin C3a and C3b, overview
Products: -
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additional information
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Substrates: dissociation of the classical-complement-pathway C3/C5 convertase by the regulators decay-accelerating factor, DAF, complement receptor 1, CR1, factor H and C4-binding protein C4BP, controls the function of the enzyme. Decay acceleration mediated by DAF, C4BP and CR1 requires interaction of the alpha4/5 region of C2a with a CCP2/CCP3 site of DAF or structurally homologous sites of CR1 and C4BP
Products: -
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additional information
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Substrates: the enzyme has a very short half-life. Dissociation of the two noncovalently bound subunits proceeds with a half_life of 1-3 min at 37°C under physiological conditions, and this rate increases greatly if regulatory proteins are present. Numerous decay-accelerating proteins are present in plasma and on host cells that bind to the noncatalytic subunit C4b and increase the rate at which the catalytic subunit C2a is released into the medium. C2a loses its enzymatic activity and its ability to bind to C4b upon release. Although C4b is able to rebind C2 and reform the enzyme, the interaction with most decay-accelerating factors also leads to permanent proteolytic interaction of the cell-bound subunit C4b by a fluid-phase protease Factor I. Theses regulatory events limit cleavage of C3, reduce release of the anaphylatoxin C3a and control the formation of more efficient C5 convertase enzymes
Products: -
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additional information
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Substrates: factor B associates with complement component C3b and after proteolysis yields the C3 convertase of the alternative pathway, complement component C2A provides the catalytic center to the convertase complexes of the classical and lectin-binding pathways of complement activation, structural basis of the substrate specificity of the complement complex, overview, attachment of C3b to either C4b2a or C3bBb yields the C5 convertases, C4b2a3b and C3b2Bb, respectively, that cleave complement component C5
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additional information
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Substrates: the alternative pathway lead via C3 convertase C3bBb and the C5 convertases C4b2aC3b and C3b 2 Bb
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additional information
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Substrates: the C3 convertases, bimolecular complexes C4b2a and C3bBb, of the classical and alternative pathways are the central enzymes of the complement cascade, focused complement activation on foreign targets depends on regulatory proteins that decay the bimolecular C3 convertases, activity and regulation of complement control proteins CCP1-CCP4 as modules of the cell surface regulator, decay-accelerating factor, i.e. DAF or CD55, interaction of DAF with the convertases is mediated predominantly by two patches, one centered around Arg69 and Arg96 on CCP2 and the other around Phe148 and Leu171 on CCP3, structure, overview
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additional information
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Substrates: the multi-domain serine protease C2 is the catalytic fragment of classical pathway C3 and C5 convertase of human complement of the classical and lectin pathways of complement activation, formation of these convertases requires the Mg2+-dependent binding of C2 to C4b and the subsequent cleavage of C2 by C1s or MASP2, respectively, the C-terminal fragment C2a consisting of a serine protease and a von Willebrand factor type A domain, remains attached to C4b, forming the C3 convertase, C4b2a, structure, overview
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additional information
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Substrates: the virion-associated Kaposis sarcoma-associated herpesvirus complement control protein is required for complement regulation and cell binding, involved structures, Kaposis sarcoma-associated herpesvirus, KSHV, encodes a lytic cycle protein called KSHV complement control protein, KCP, that inhibits activation of the complement cascade. It does so by regulating C3 convertases, accelerating their decay, and acting as a cofactor for factor I degradation of C4b and C3b, two components of the C3 and C5 convertases, KCP is expressed on the surface of human infected endothelial cells, mechanism, overview, K64Q/K65Q/K88Q KCP mutant lacks complement regulatory activity
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additional information
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Substrates: pharmacological complement inhibition at the C3 convertase level promotes neuronal survival, neuroprotective intracerebral gene expression, and neurological outcome after traumatic brain injury, overview
Products: -
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additional information
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Substrates: the enzyme catalyzes the central step of the complement cascade, overview, molecular interactions between MBL-associated serine protease-2, MASP-2, C4, and C2 and their activation fragments leading to complement activation via the lectin pathway, MASP-2 cleaves C4 releasing C4a and generating C4b, which attaches covalently to the pathogen surface upon exposure of its reactive thioester, C2 binds to C4b and is also cleaved by MASP-2 to form the C3 convertase C4b2a, overview
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C3 zymogen + H2O
C3b + C3a
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Substrates: activation
Products: -
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C5 zymogen + H2O
C5b + C5a
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Substrates: activation
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complement component C3 + H2O
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Substrates: classical pathway of the complement system
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complement component C3 + H2O
complement component C3a + complement component C3b
complement component C3 + H2O
component C3b + anaphylatoxin C3a
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Substrates: -
Products: iC3b is generated by Factor I after formation of C3b. iC3b is a proteolytically inactive form of C3b that retains the ability to opsonize microbes, but cannot participate in convertase function
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complement component C5 + H2O
complement component C5a + complement component C5b
complement componentC3 + H2O
complement component C3a + complement component C3b
additional information
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complement component C3 + H2O
complement component C3a + complement component C3b
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Substrates: -
Products: -
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complement component C3 + H2O
complement component C3a + complement component C3b
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Substrates: complement component C3 is the preferred substrate. Cleavage of the preferred C3 substrate and deposition of C3b effectively switches the output of the enzyme from C3b to C5b, resulting in initiation of the cytosolic process of complement
Products: -
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complement component C3 + H2O
complement component C3a + complement component C3b
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Substrates: C3 complement cleavage is a central event in the activation of the complement system via the classical, the alternative, and the lectin pathway, overview
Products: -
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complement component C5 + H2O
complement component C5a + complement component C5b
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Substrates: -
Products: -
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complement component C5 + H2O
complement component C5a + complement component C5b
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Substrates: C5 convertases C4b2aC3b and C3b 2 Bb
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complement component C5 + H2O
complement component C5a + complement component C5b
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Substrates: C5 convertases, C4b2a3b and C3b2Bb, cleave C5 into the anaphylatoxin C5a and C5b followed by initiation of the terminal pathway, leading to formation of lytic C5b-9 membrane attack complexes, overview
Products: -
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complement component C5 + H2O
complement component C5a + complement component C5b
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Substrates: C5 convertases, C4b2a3b and C3b2Bb, cleave C5 into the anaphylatoxin C5a and C5b, overview
Products: -
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complement component C5 + H2O
complement component C5a + complement component C5b
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Substrates: C5 convertases, C4b2a3b and C3b2Bb, cleave C5 into the anaphylatoxin C5a and C5b, overview
Products: -
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complement componentC3 + H2O
complement component C3a + complement component C3b
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Substrates: C3 convertase C3bBb
Products: -
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complement componentC3 + H2O
complement component C3a + complement component C3b
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Substrates: C3 convertases, C4b2a and C3bBb, cleave C3 into the anaphylatoxin C3a and C3b, overview
Products: -
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complement componentC3 + H2O
complement component C3a + complement component C3b
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Substrates: C3 convertases, C4b2a and C3bBb, cleave C3 into the anaphylatoxin C3a and C3b, overview
Products: -
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additional information
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Substrates: dissociation of the classical-complement-pathway C3/C5 convertase by the regulators decay-accelerating factor, DAF, complement receptor 1, CR1, factor H and C4-binding protein C4BP, controls the function of the enzyme. Decay acceleration mediated by DAF, C4BP and CR1 requires interaction of the alpha4/5 region of C2a with a CCP2/CCP3 site of DAF or structurally homologous sites of CR1 and C4BP
Products: -
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additional information
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Substrates: the enzyme has a very short half-life. Dissociation of the two noncovalently bound subunits proceeds with a half_life of 1-3 min at 37°C under physiological conditions, and this rate increases greatly if regulatory proteins are present. Numerous decay-accelerating proteins are present in plasma and on host cells that bind to the noncatalytic subunit C4b and increase the rate at which the catalytic subunit C2a is released into the medium. C2a loses its enzymatic activity and its ability to bind to C4b upon release. Although C4b is able to rebind C2 and reform the enzyme, the interaction with most decay-accelerating factors also leads to permanent proteolytic interaction of the cell-bound subunit C4b by a fluid-phase protease Factor I. Theses regulatory events limit cleavage of C3, reduce release of the anaphylatoxin C3a and control the formation of more efficient C5 convertase enzymes
Products: -
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additional information
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Substrates: factor B associates with complement component C3b and after proteolysis yields the C3 convertase of the alternative pathway, complement component C2A provides the catalytic center to the convertase complexes of the classical and lectin-binding pathways of complement activation, structural basis of the substrate specificity of the complement complex, overview, attachment of C3b to either C4b2a or C3bBb yields the C5 convertases, C4b2a3b and C3b2Bb, respectively, that cleave complement component C5
Products: -
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additional information
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Substrates: the alternative pathway lead via C3 convertase C3bBb and the C5 convertases C4b2aC3b and C3b 2 Bb
Products: -
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additional information
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Substrates: the C3 convertases, bimolecular complexes C4b2a and C3bBb, of the classical and alternative pathways are the central enzymes of the complement cascade, focused complement activation on foreign targets depends on regulatory proteins that decay the bimolecular C3 convertases, activity and regulation of complement control proteins CCP1-CCP4 as modules of the cell surface regulator, decay-accelerating factor, i.e. DAF or CD55, interaction of DAF with the convertases is mediated predominantly by two patches, one centered around Arg69 and Arg96 on CCP2 and the other around Phe148 and Leu171 on CCP3, structure, overview
Products: -
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additional information
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Substrates: the multi-domain serine protease C2 is the catalytic fragment of classical pathway C3 and C5 convertase of human complement of the classical and lectin pathways of complement activation, formation of these convertases requires the Mg2+-dependent binding of C2 to C4b and the subsequent cleavage of C2 by C1s or MASP2, respectively, the C-terminal fragment C2a consisting of a serine protease and a von Willebrand factor type A domain, remains attached to C4b, forming the C3 convertase, C4b2a, structure, overview
Products: -
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additional information
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Substrates: the virion-associated Kaposis sarcoma-associated herpesvirus complement control protein is required for complement regulation and cell binding, involved structures, Kaposis sarcoma-associated herpesvirus, KSHV, encodes a lytic cycle protein called KSHV complement control protein, KCP, that inhibits activation of the complement cascade. It does so by regulating C3 convertases, accelerating their decay, and acting as a cofactor for factor I degradation of C4b and C3b, two components of the C3 and C5 convertases, KCP is expressed on the surface of human infected endothelial cells, mechanism, overview, K64Q/K65Q/K88Q KCP mutant lacks complement regulatory activity
Products: -
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additional information
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Substrates: pharmacological complement inhibition at the C3 convertase level promotes neuronal survival, neuroprotective intracerebral gene expression, and neurological outcome after traumatic brain injury, overview
Products: -
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additional information
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Substrates: the enzyme catalyzes the central step of the complement cascade, overview, molecular interactions between MBL-associated serine protease-2, MASP-2, C4, and C2 and their activation fragments leading to complement activation via the lectin pathway, MASP-2 cleaves C4 releasing C4a and generating C4b, which attaches covalently to the pathogen surface upon exposure of its reactive thioester, C2 binds to C4b and is also cleaved by MASP-2 to form the C3 convertase C4b2a, overview
Products: -
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C1 inhibitor
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blocks the the classical pathway
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C4b-binding protein
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regulates assembly and decay of the classical pathway C3/C5 convertase 4times lower than the lectin pathway convertase
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C4BP
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effectively inhibits both C3 and C5 conversion
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C4d antibody
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blocks the the classical pathway
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CN-
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inhibits the aggregation of C4b and C2a and the activity of the active enzyme
complement receptor of immunoglobulin family
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inhibits C5 conversion specifically
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complement receptor type 1-related protein y
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i.e. Crry, a mouse-specific complement inhibitor, expressed in astrocytes, microglia, and neurons of murine brain, in vivo and in vitro inhibition of C3 convertase, overview
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Cp40
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the inhibitor shows potent inhibition of C3 conversion
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diisopropyl fluorophosphate
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eculizumab
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potently inhibits C5 conversion but leaves C3 conversion unaffected
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EDTA
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inhibits interaction between C4b and C2b
Efb-C
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does not inhibit C3 convertase activity but C5 convertase activity
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extracellular complement binding protein
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does not inhibit C3 convertase activity but C5 convertase activity
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extracellular complement-binding protein
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Ecb, a potent complement inhibitor from Staphylococcus aureus, with strong antiinflammatory properties, inhibitory mechanism for blocking C3b-containing convertases, Efb-C and Ecb act on the bacterial surface, overview
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extracellular fibrinogen-binding protein
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Efb, a potent complement inhibitor from Staphylococcus aureus, with strong antiinflammatory properties, inhibitory mechanism for blocking C3b-containing convertases, Efb-C and Ecb act on the bacterial surface, overview
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factor H
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inhibits C5 conversion specifically
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factor H related-protein 5
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inhibits C5 conversion in a concentration-dependent manner
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hepatitis virus C
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inhibition of C3 convertase activity and C3b deposition onto bacterial membrane by hepatitis C virus, impairment of both C3 convertase and Factor I activity
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mouse anti human factor B antibody
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N-terminal long homologous repeat A of complement receptor type 1
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responsible for dissociation of enzyme. Highest decay accelerating activity for mutant dimeric construct N-terminal long homologous repeat A (D109N/E116K)/N-terminal long homologous repeat A (D109N)
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NH2-CD59-DAF-GPI
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chimeric molecule, DAF: decay accelerating factor, GPI: glycosylphosphatidylinositol
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NH2DAF-CD59-GPI
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chimeric molecule, DAF: decay accelerating factor, GPI: glycosylphosphatidylinositol
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OmCI
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the inhibitor blocks C5 cleavage by interfering with convertase recognition far from C5a
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Ornithodoros moubata complement inhibitory protein
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potently inhibits C5 conversion but leaves C3 conversion unaffected
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Pra1
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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
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rosmarinic acid
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inhibition of C5 convertase by binding to component C3b
soluble complement receptor type 1
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SSL7
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the inhibitor blocks C5 cleavage by interfering with convertase recognition far from C5a
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staphylococcal complement inhibitor
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SCIN, a potent complement inhibitor from Staphylococcus aureus, with strong antiinflammatory properties, inhibitory mechanism for blocking C3b-containing convertases, overview
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staphylococcal superantigen-like protein 7
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inhibits C5 conversion
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thioredoxin 1
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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
TT32
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human complement receptor type 2 (CR2)/CR1 fusion protein
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additional information
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Kaposi's sarcoma-associated herpesvirus complement control protein inhibits complement through decay-accelerating activity of the classical C3 convertase and cofactor activity for factor I-mediated degradtion of C4b and C3b, as well as acting as an attachment factor for binding to heparan sulfate on permissive cells, overview
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additional information
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the C3b-specific antibody fragment S77 does not inhibit the classical pathway C5 convertase in human serum
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additional information
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addition of guinea pig serum in 40 mM EDTA initiates lysis of existing convertase complexes and excludes the possibility of de novo convertase formation
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Nagasawa, S.; Kobayashi, C.; Maki-Suzuki, T.; Yamashita, N.; Koyama, J.
Purification and characterization of the C3 convertase of the classical pathway of human complement system by size exclusion high-performance liquid chromatography
J. Biochem.
97
493-499
1985
Homo sapiens
brenda
Kerr, M.A.
The human complement system: assembly of the classical pathway C3 convertase
Biochem. J.
189
173-181
1980
Homo sapiens
brenda
Vogt, W.; Schmidt, G.; v.Buttlar, B.; Dieminger, L.
A new function of the activated third component of complement: binding to C5, an essential step for C5 activation
Immunology
34
29-40
1978
Homo sapiens
brenda
Porter, R.R.; Reid, K.B.M.
The biochemistry of complement
Nature
275
699-704
1978
Homo sapiens
brenda
Nicholson-Weller, A.; Burge, J.; Austen, F.
Purification from guinea pig erythrocyte stroma of a decay-accelerating factor for the classical C3 convertase, C4b2a
J. Immunol.
127
2035-2039
1978
Homo sapiens
brenda
Emmerling, M.R.; Spiegel, K.; Watson, M.D.
Inhibiting the formation of classical C3-convertase on the Alzheimer s beta-amyloid peptide
Immunopharmacology
38
101-109
1997
Homo sapiens
brenda
Sahu, A.; Rawal, N.; Pangburn, M.K.
Inhibition of complement by covalent attachment of rosmarinic acid to activated C3b
Biochem. Pharmacol.
57
1439-1446
1999
Homo sapiens
brenda
Bloch, E.F.; Rahbar, M.; Wright, A.K.; Patterson, A.M.; Souza, R.F.; Hammer, C.H.; Gaither, T.A.; Joiner, K.A.
Potassium cyanide protects Escherichia coli from complement killing by the inhibition of C3 convertase activity
Immunol. Invest.
22(2)
127-149
1993
Homo sapiens
-
brenda
Kerr, M.A.
The second component of human complement
Methods Enzymol.
80
54-64
1981
Homo sapiens
-
brenda
Fodor, W.L.; Rollins, S.A.; Guilmette, E.R.; Settler, E.; Squinto, S.P.
A novel bifunctional chimeric complement inhibitor that regulates C3 convertase and formation of the membrane attack complex
J. Immunol.
155
4135-4138
1995
Homo sapiens
brenda
Pangburn, M.K.; Rawal, N.
Structure and function of complement C5 convertase enzymes
Biochem. Soc. Trans.
30
1006-1010
2002
Homo sapiens
brenda
Rawal, N.; Pangburn, M.K.
Formation of high affinity C5 convertase of the classical pathway of complement
J. Biol. Chem.
278
38476-38483
2003
Homo sapiens
brenda
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Homo sapiens
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