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Information on EC 3.4.21.47 - alternative-complement-pathway C3/C5 convertase and Organism(s) Homo sapiens and UniProt Accession P00751

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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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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
c3bbb, c5 convertase, properdin factor b, alternative pathway c3 convertase, c3b,bb, heat-labile factor, c3/c5 convertase, c3 proactivator, cvf,bb, ap c3 convertase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alternative C3 convertase
-
alternative C5 convertase
-
alternative pathway C3 convertase
-
alternative pathway C3-convertase
-
alternative-complement-pathway C3/C5 convertase
-
AP C3-convertase
-
C3bB complex
-
C3bBb convertase
-
C5 convertase
-
complement alternative pathway C3 convertase
-
(C3b)n,Bb
-
-
-
-
(CVF)-dependent glycine-rich-beta-glucoprotein
-
-
-
-
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
-
-
AP C3 convertase
-
-
AP C3/C5 convertase
-
-
AP C5 convertase
-
-
APC C3/C5 convertase
-
-
C3 convertase
C3 proactivator
-
-
-
-
C3/C5 convertase
C3b,Bb
C3b2
-
-
C3bBb
C3bBb convertase
-
-
C3bBb(C3b)n
-
C5 convertase
C3bBb3b
-
-
C3bBbC3b
-
-
C5 convertase
cobra venom factor-dependent 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
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
show the reaction diagram
CAS REGISTRY NUMBER
COMMENTARY hide
80295-67-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
complement component C3 + H2O
complement component C3a + complement component C3b
show the reaction diagram
complement component C3 zymogen + H2O
complement component C3b + complement component C3a
show the reaction diagram
complement component C5 + H2O
complement component C5a + complement component C5b
show the reaction diagram
complement component C5 zymogen + H2O
complement component C5b + complement component C5a
show the reaction diagram
t-butyloxycarbonyl-Gly-L-Leu-L-Ala-L-Arg-thiobenzyl ester
?
show the reaction diagram
substrate of enzyme subunit Bb
-
-
?
C2 fragment + H2O
?
show the reaction diagram
-
C-terminal fragment originating from the processing of meningococcal proteases
-
-
?
complement component C3 + H2O
complement component C3a + complement component C3b
show the reaction diagram
complement component C5 + H2O
complement component C5a + complement component C5b
show the reaction diagram
neisserial heparin binding antigen + H2O
?
show the reaction diagram
-
also known as GNA2132 (genome-derived Neisseria antigen 2132)
-
-
?
tert-butoxycarbonyl-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
tert-butoxycarbonyl-norleucine-Gln-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
tert-butoxycarbonyl-norleucine-Gln-Leu-Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
complement component C3 + H2O
complement component C3a + complement component C3b
show the reaction diagram
complement component C3 zymogen + H2O
complement component C3b + complement component C3a
show the reaction diagram
activation
-
-
?
complement component C5 + H2O
complement component C5a + complement component C5b
show the reaction diagram
complement component C5 zymogen + H2O
complement component C5b + complement component C5a
show the reaction diagram
activation
-
-
?
C2 fragment + H2O
?
show the reaction diagram
-
C-terminal fragment originating from the processing of meningococcal proteases
-
-
?
complement component C3 + H2O
complement component C3a + complement component C3b
show the reaction diagram
complement component C5 + H2O
complement component C5a + complement component C5b
show the reaction diagram
neisserial heparin binding antigen + H2O
?
show the reaction diagram
-
also known as GNA2132 (genome-derived Neisseria antigen 2132)
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required
Ni2+
promotes a stable C3bB complex
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-amidino-2-naphthyl-4-guanidinobenzoate
-
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
complement receptor 1
CR1, mediates decay acceleration of the C3bBb complex
-
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
-
factor H
-
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
C3b-specific antibody fragment S77
-
inhibits the alternative pathway C5 convertase in human serum
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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 of immunoglobulin family
-
the inhibitor blocks both C3 and C5 conversion
-
Cp40
-
the inhibitor blocks both C3 and C5 conversion
-
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
-
the inhibitor blocks both C3 and C5 conversion
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factor H related-protein 5
-
inhibits C5 conversion in a concentration-dependent manner
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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
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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
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soluble complement receptor type 1
-
-
-
SSL7
-
the inhibitor blocks C5 cleavage by interfering with convertase recognition far from C5a
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staphylococcal complement inhibitor
-
TT30
-
TT32
-
human complement receptor type 2 (CR2)/CR1 fusion protein
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
factor B
-
factor D
-
human complement factor H-related protein 4
CFHR 4, two isozymes A and B of 86 and 45 kDa from plasma, domain structure, overview. The protein belongs to the factor H family of plasma glycoproteins that are composed of short consensus repeat (SCR) domains. It activates complement by serving as a platform for the assembly of alternative pathway C3 convertase via its interaction with C3b protein. CFHR4 binds C3b via its C-terminus, and it lacks SCRs homologous to the complement inhibitory domains of factor H and has no significant complement regulatory activities. In contrast to the complement inhibitor factor H, CFHR4 acts as an enhancer of opsonization by promoting complement activation
-
mannan-binding lectin
mannan-binding lectin (MBL) promotes activation of complement component C3 through the combined action of MBL-associated serine proteases MASP-1 and MASP-2 without appreciable involvement of the alternative pathway, experimental conditions described
-
properdin
-
zymosan
it is capable of activating the classical pathway as well as the alternative pathway, when the classical pathway is blocked, mechanism, overview
-
formyl-methionyl-leucylphenylalanine
-
treatment of whole blood leads to stimulation of neutrophils resulting in activation of the alternative complement pathway and release of C5 fragments, which further amplify proinflammatory responses
mannan-binding lectin
-
binding to O antigen-specific oligosaccharides derived from Salmonella sp. corresponding to serogroup C, and efficient support of component C3 deposition in the absence of C2, C4, or the associated serine protease 2
-
phorbol myristate acetate
-
treatment of whole blood leads to stimulation of neutrophils resulting in activation of the alternative complement pathway and release of C5 fragments, which further amplify proinflammatory responses
properdin
-
surface plasmon resonance assays, properdin promotes the association of C3b with factor B and provides a focal point for the assembly of enzyme on a surface. Properdin can use its unoccupied C3b-binding sites as receptors and form a lattice of properdin-C3b, -C3bB and C3bBb complexes leading to in situ assembly of enzyme
-
tumor necrosis factor-alpha
-
treatment of whole blood leads to stimulation of neutrophils resulting in activation of the alternative complement pathway and release of C5 fragments, which further amplify proinflammatory responses
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.75 - 5.63
t-butyloxycarbonyl-Gly-L-Leu-L-Ala-L-Arg-thiobenzyl ester
0.00586 - 0.0264
complement component C3
-
0.0000075 - 0.0688
complement component C5
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.28 - 0.65
t-butyloxycarbonyl-Gly-L-Leu-L-Ala-L-Arg-thiobenzyl ester
0.107 - 1.78
complement component C3
-
0.0038 - 0.026
complement component C5
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00002
soluble complement receptor type 1
Homo sapiens
-
at 37°C, pH not specified in the publication
-
0.00013
TT30
Homo sapiens
-
at 37°C, pH not specified in the publication
-
0.000046
TT32
Homo sapiens
-
at 37°C, pH not specified in the publication
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
assay at
7.4
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
trauma patients, clinical characteristics shown
Manually annotated by BRENDA team
-
contains factor B
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
malfunction
-
enzyme inhibition with eculizumab blunts terminal complementxa0activation in patients with immunexa0complex-mediated primary membranoproliferative glomerulonephritis or C3 glomerulonephritis and nephrotic syndrome
metabolism
-
when factor B first associates with C3b, it bears two intact Arg234 salt bridges. The complex rapidly dissociates unless the Arg234-Glu446 salt bridge is released whereupon conformational changes occur that activate the metal ion-dependent adhesion site and partially stabilize the complex. The remaining salt bridge is then released, exposing the scissile bond and permitting factor D cleavage of proenzyme factor B
physiological function
-
both the in situ conversion of complement component C5 by the enzyme and immediate association of C5b with C6 and C7 are needed to guide proper insertion of bactericidal MAC pores
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CFAB_HUMAN
764
0
85533
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
-
x * 200000, enzyme component C3, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 200000, enzyme component C3, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
association of factor B with C3b in the presence of Mg2+ results in the formation of a bimolecular zymogen C3b,B, which is activated by the serine proteinase factor D, generating the C3 convertase, C3b,Bb
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
engineered subunit Bb with Cys-resiudes at positions 435 and 428, in complex with inhibitors 6-amidino-2-naphthyl-4-guanidinobenzoate or diisopropyl phosphate
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
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
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
923DELTADG
-
mutation in complement factor 3 gene identified in patients with dense deposit disease. Mutant C3923DELTADG, which lacks 2 amino acids, cannot be cleaved to C3b by the alternative pathway C3-convertase and is therefore the predominant circulating C3 protein in the patients. Upon activation to C3b by proteases, or to C3(H2O) by spontaneous thioester hydrolysis, mutant C3 generates an active C3-convertase that is regulated normally by decay accelerating factor but is resistant to decay by factor H. Activated C3b923DELTADG and C3(H2O)923DELTADG are resistant to proteolysis by factor I in the presence of factor H, but are efficiently inactivated in the presence of membrane cofactor protein, causing a fluid phase-restricted alternative pathway dysregulation in the patients that continuously activates and consumes C3 produced by the normal C3 allele
D254G
-
mutation in the Bb component decreases sensitivity to DAF to 9% of the wild-type value, sensitivity to CR1 to 4% of the wild-type value and sensitivity to Factor H to 48% of the wild-type value
D382A
-
mutation in the Bb component decreases sensitivity to DAF to 36% of the wild-type value, sensitivity to CR1 to 41% of the wild-type value
D382N
-
mutation in the Bb component decreases sensitivity to DAF to 54% of the wild-type value
D445A
-
mutation in the Bb component decreases sensitivity to CR1 to 71% of the wild-type value
D715A
-
factor B mutation, severly reduces hemolytic activity, in complex with C3b no cleavage of C3
D715E
-
factor B mutation, severly reduces hemolytic activity, in complex with C3b no cleavage of C3
D715N
-
factor B mutation, severly reduces hemolytic activity, in complex with C3b no cleavage of C3
D715S
-
factor B mutation, severly reduces hemolytic activity
D715Y
-
factor B mutation, severly reduces hemolytic activity
E207A
-
mutation in proenzyme factor B. Mutation disrupts salt bridge R234-E207, with little effects on the cleavage of proenzyme factor B
E301A
-
mutation in the Bb component decreases sensitivity to DAF to 75% of the wild-type value
E316A
-
mutation in the Bb component decreases sensitivity to DAF to 71% of the wild-type value
E379A
-
mutation in the Bb component decreases sensitivity to DAF to 52% of the wild-type value, sensitivity to CR1 to 50% of the wild-type value
E434A
-
mutation in the Bb component decreases sensitivity to CR1 to 65% of the wild-type value
E446V
-
mutation in proenzyme factor B. Mutation disrupts salt bridge R234-E446 which partly stabilizes the complex C3bB(Mg2+) thereby inhibiting activation of the proenzyme
F716A
-
factor B mutation, severly reduces hemolytic activity
K265A/K266A
-
Mutation in the Bb component decreases sensitivity to DAF to 18% of the wild-type value, sensitivity to CR1 to 18% of the wild-type value and sensitivity to Factor H to 19% of the wild-type value
K294A
-
mutation in the Bb component decreases sensitivity to CR1 to 44% of the wild-type value
M341A
-
mutation in the Bb component decreases sensitivity to Factor H to 75% of the wild-type value
N260D
-
mutation in the Bb component decreases sensitivity to DAF to 32% of the wild-type value, sensitivity to CR1 to 31% of the wild-type value and sensitivity to Factor H to 24% of the wild-type value
Q335A
-
mutation in the Bb component decreases sensitivity to DAF to 20% of the wild-type value
S339A
-
mutation in the Bb component decreases sensitivity to DAF to 32% of the wild-type value, sensitivity to CR1 to 50% of the wild-type value
W343A
-
mutation in the Bb component decreases sensitivity to DAF to 55% of the wild-type value, sensitivity to CR1 to 56% of the wild-type value
Y338A
-
mutation in the Bb component decreases sensitivity to DAF to 9% of the wild-type value, sensitivity to CR1 to 4% of the wild-type value and sensitivity to Factor H to 48% of the wild-type value
Y338F
-
mutation in the Bb component decreases sensitivity to DAF to 18% of the wild-type value, sensitivity to CR1 to 20% of the wild-type value and sensitivity to Factor H to 61% of the wild-type value
Y338S
-
mutation in the Bb component decreases sensitivity to DAF to 5% of the wild-type value, sensitivity to CR1 to 24% of the wild-type value
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
marked stabilization of enzyme by naturally occuring IgG directed against the enzyme. Antibody prevents convertase decay in the presence of factor H. In addition, the antibody stabilizes enzyme precursors and promotes enzyme assembly
-
properdin stabilizes enzyme-IgG complexes before any other complement protein has bound to them. The alternative pathway of convertase generation may depend on whether properdin is bound to its precursor, a C3b or a C3b2-IgG complex
-
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 C3b and increase the rate at which the catalytic subunit Bb is released into the medium. Bb loses its enzymatic activity and its ability to bind to C3b upon release. Although C3b is able to rebind Bb and reform the enzyme, the interaction with most decay-accelerating factors also leads to permanent proteolytic interaction of the cell-bound subunit C3b by a fluid-phase protease Factor I. These regulatory events limit cleavage of C3, reduce release of the anaphylatoxin C3a and control the formation of more efficient C5 convertase enzymes
-
the enzyme is subject to irreversible dissociation by three proteins: DAF, CR1 and factor H
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
C3bB(Ni2+) complex or C3bBb(factor B-D279G mutant) purified by gel filtration
affinity purification of factor B
-
complement proteins purified by gel filtration, to homogeneity
-
magnetic cobalt beads chromatography and analytical ultracentrifugation
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293E cells
-
factor B, expression in COS cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pangburn, M.K.; Muller-Eberhard, H.J.
The C3 convertase of the alternative pathway of human complement. Enzymic properties of the bimolecular proteinase
Biochem. J.
235
723-730
1986
Homo sapiens
Manually annotated by BRENDA team
DiScipio, R.G.; Smith, C.A.; Muller-Eberhard, H.J.; Hugli, T.E.
The activation of human complement component C5 by a fluid phase C5 convertase
J. Biol. Chem.
258
10629-10636
1983
Homo sapiens
Manually annotated by BRENDA team
Gutierrez, J.C.; Gtze, O.; Caporale, L.H.
An improved fluorogenic substrate for the alternative complement pathway C3/5 converting enzyme CVFBb
Biochim. Biophys. Acta
744
276-280
1983
Homo sapiens
Manually annotated by BRENDA team
Vogel, C.W.; Muller-Eberhard, H.J.
The cobra venom factor-dependent C3 convertase of human complement. A kinetic and thermodynamic analysis of a protease acting on its natural high molecular weight substrate
J. Biol. Chem.
257
8292-8299
1982
Homo sapiens
Manually annotated by BRENDA team
Kerr, M.A.
Human factor B
Methods Enzymol.
80
102-112
1981
Homo sapiens
Manually annotated by BRENDA team
Schwaeble, W.; Luttig, B.; Sokolowski, T.; Estaller, C.; Weiss, E.H.; Meyer zum Bschenfelde, K.H.; Whaley, K.; Dippold, W.
Human complement factor B: functional properties of a recombinant zymogen of the alternative activation pathway convertase
Immunobiology
188
221-232
1993
Homo sapiens
Manually annotated by BRENDA team
Williams, S.C.; Sim, R.B.
Dye-ligand affinity purification of human complement factor B and beta 2 glycoprotein I
J. Immunol. Methods
157
25-30
1993
Homo sapiens
Manually annotated by BRENDA team
Hourcade, D.E.; Mitchell, L.M.; Oglesby, T.J.
A conserved element in the serine protease domain of complement factor B
J. Biol. Chem.
273
25996-26000
1998
Homo sapiens
Manually annotated by BRENDA team
Sumiyoshi, K.; Andoh, A.; Fujiyama, Y.; Sakumoto, H.; Bamba, T.
Characterization of complement C3, C4, and factor B molecules in human bile
J. Gastroenterol.
32
230-235
1997
Homo sapiens
Manually annotated by BRENDA team
Fu, Q.; McPhie, P.; Gowda, D.C.
Methionine modification impairs the C5-cleavage function of cobra venom factor-dependent C3/C5 convertase
Biochem. Mol. Biol. Int.
45
133-144
1998
Homo sapiens
Manually annotated by BRENDA team
Berkovich, SA.; O'Keefe, M.C.; Hensley, P.; Caporale, L.
Effect of N-methylation on the modulation by synthetic peptides of the activity of the complement-factor-B-derived serine proteinase CVFBb
Biochem. J.
270
531-537
1990
Homo sapiens
Manually annotated by BRENDA team
Jelezarova, E.; Vogt, A.; Lutz, H.U.
Interaction of C3b(2)-IgG complexes with complement proteins properdin, factor B and factor H: implications for amplification
Biochem. J.
349
217-223
2000
Homo sapiens
Manually annotated by BRENDA team
Pangburn, M.K.; Rawal, N.
Structure and function of complement C5 convertase enzymes
Biochem. Soc. Trans.
30
1006-1010
2002
Homo sapiens
Manually annotated by BRENDA team
Hourcade, D.E.; Mitchell, L.; Kuttner-Kondo, L.A.; Atkinson, J.P.; Medof, M.E.
Decay-accelerating factor (DAF), complement receptor 1 (CR1), and factor H dissociate the complement AP C3 convertase (C3bBb) via sites on the type A domain of Bb
J. Biol. Chem.
277
1107-1112
2002
Homo sapiens
Manually annotated by BRENDA team
Rawal, N.; Pangburn, M.K.
Functional role of the noncatalytic subunit of complement C5 convertase
J. Immunol.
164
1379-1385
2000
Homo sapiens
Manually annotated by BRENDA team
Koelln, J.; Bredehorst, R.; Spillner, E.
Engineering of human complement component C3 for catalytic inhibition of complement
Immunol. Lett.
98
49-56
2005
Homo sapiens
Manually annotated by BRENDA team
Hourcade, D.E.
The role of properdin in the assembly of the alternative pathway C3 convertases of complement
J. Biol. Chem.
281
2128-2132
2006
Homo sapiens
Manually annotated by BRENDA team
Selander, B.; Martensson, U.; Weintraub, A.; Holmstroem, E.; Matsushita, M.; Thiel, S.; Jensenius, J.C.; Truedsson, L.; Sjoeholm, A.G.
Mannan-binding lectin activates C3 and the alternative complement pathway without involvement of C2
J. Clin. Invest.
116
1425-1434
2006
Homo sapiens
Manually annotated by BRENDA team
Koelln, J.; Spillner, E.; Andrae, J.; Klensang, K.; Bredehorst, R.
Complement inactivation by recombinant human C3 derivatives
J. Immunol.
173
5540-5545
2004
Homo sapiens
Manually annotated by BRENDA team
Ponnuraj, K.; Xu, Y.; Macon, K.; Moore, D.; Volanakis, J.E.; Narayana, S.V.
Structural analysis of engineered Bb fragment of complement factor B: insights into the activation mechanism of the alternative pathway C3-convertase
Mol. Cell
14
17-28
2004
Homo sapiens (P00751)
Manually annotated by BRENDA team
Jelezarova, E.; Lutz, H.U.
IgG naturally occurring antibodies stabilize and promote the generation of the alternative complement pathway C3 convertase
Mol. Immunol.
42
1393-1403
2005
Homo sapiens
Manually annotated by BRENDA team
Moller-Kristensen, M.; Thiel, S.; Sjoeholm, A.; Matsushita, M.; Jensenius, J.C.
Cooperation between MASP-1 and MASP-2 in the generation of C3 convertase through the MBL pathway
Int. Immunol.
19
141-149
2007
Homo sapiens (P00751), Mus musculus (P04186)
Manually annotated by BRENDA team
Kimura, Y.; Miwa, T.; Zhou, L.; Song, W.C.
Activator-specific requirement of properdin in the initiation and amplification of the alternative pathway complement
Blood
111
732-740
2008
Homo sapiens (P00751), Homo sapiens, Mus musculus (P04186), Mus musculus
Manually annotated by BRENDA team
Harris, C.L.; Pettigrew, D.M.; Lea, S.M.; Morgan, B.P.
Decay-accelerating factor must bind both components of the complement alternative pathway C3 convertase to mediate efficient decay
J. Immunol.
178
352-359
2007
Homo sapiens (P00751)
Manually annotated by BRENDA team
Lutz, H.U.; Fumia, S.; Schurtenberger, C.; Alaia, V.
Opinion paper: Stimulation of complement amplification or activation of the alternative pathway of complement?
Mol. Immunol.
44
3862-3865
2007
Homo sapiens (P00751)
Manually annotated by BRENDA team
Bexborn, F.; Andersson, P.O.; Chen, H.; Nilsson, B.; Ekdahl, K.N.
The tick-over theory revisited: Formation and regulation of the soluble alternative complement C3 convertase (C3(H(2)O)Bb)
Mol. Immunol.
45
2370-2379
2008
Homo sapiens (P00751)
Manually annotated by BRENDA team
Wiesmann, C.; Katschke, K.J.; Yin, J.; Helmy, K.Y.; Steffek, M.; Fairbrother, W.J.; McCallum, S.A.; Embuscado, L.; DeForge, L.; Hass, P.E.; van Lookeren Campagne, M.
Structure of C3b in complex with CRIg gives insights into regulation of complement activation
Nature
444
217-220
2006
Homo sapiens (P00751)
Manually annotated by BRENDA team
Ganter, M.T.; Brohi, K.; Cohen, M.J.; Shaffer, L.A.; Walsh, M.C.; Stahl, G.L.; Pittet, J.F.
Role of the alternative pathway in the early complement activation following major trauma
Shock
28
29-34
2007
Homo sapiens (P00751)
Manually annotated by BRENDA team
Rawal, N.; Rajagopalan, R.; Salvi, V.P.
Activation of complement component C5: comparison of C5 convertases of the lectin pathway and the classical pathway of complement
J. Biol. Chem.
283
7853-7863
2008
Homo sapiens
Manually annotated by BRENDA team
Torreira, E.; Tortajada, A.; Montes, T.; Rodriguez de Cordoba, S.; Llorca, O.
3D structure of the C3bB complex provides insights into the activation and regulation of the complement alternative pathway convertase
Proc. Natl. Acad. Sci. USA
106
882-887
2009
Homo sapiens (P00751)
Manually annotated by BRENDA team
Heinen, S.; Hartmann, A.; Lauer, N.; Wiehl, U.; Dahse, H.M.; Schirmer, S.; Gropp, K.; Enghardt, T.; Wallich, R.; Haelbich, S.; Mihlan, M.; Schloetzer-Schrehardt, U.; Zipfel, P.F.; Skerka, C.
Factor H-related protein 1 (CFHR-1) inhibits complement C5 convertase activity and terminal complex formation
Blood
114
2439-2447
2009
Homo sapiens
Manually annotated by BRENDA team
Lindorfer, M.A.; Pawluczkowycz, A.W.; Peek, E.M.; Hickman, K.; Taylor, R.P.; Parker, C.J.
A novel approach to preventing the hemolysis of paroxysmal nocturnal hemoglobinuria: both complement-mediated cytolysis and C3 deposition are blocked by a monoclonal antibody specific for the alternative pathway of complement
Blood
115
2283-2291
2010
Homo sapiens
Manually annotated by BRENDA team
Katschke, K.J.; Stawicki, S.; Yin, J.; Steffek, M.; Xi, H.; Sturgeon, L.; Hass, P.E.; Loyet, K.M.; Deforge, L.; Wu, Y.; van Lookeren Campagne, M.; Wiesmann, C.
Structural and functional analysis of a C3b-specific antibody that selectively inhibits the alternative pathway of complement
J. Biol. Chem.
284
10473-10479
2009
Homo sapiens
Manually annotated by BRENDA team
Torreira, E.; Tortajada, A.; Montes, T.; Rodriguez de Cordoba, S.; Llorca, O.
Coexistence of closed and open conformations of complement factor B in the alternative pathway C3bB(Mg2+) proconvertase
J. Immunol.
183
7347-7351
2009
Homo sapiens
Manually annotated by BRENDA team
Strobel, S.; Zimmering, M.; Papp, K.; Prechl, J.; Jozsi, M.
Anti-factor B autoantibody in dense deposit disease
Mol. Immunol.
47
1476-1483
2010
Homo sapiens
Manually annotated by BRENDA team
Rooijakkers, S.H.; Wu, J.; Ruyken, M.; van Domselaar, R.; Planken, K.L.; Tzekou, A.; Ricklin, D.; Lambris, J.D.; Janssen, B.J.; van Strijp, J.A.; Gros, P.
Structural and functional implications of the alternative complement pathway C3 convertase stabilized by a staphylococcal inhibitor
Nat. Immunol.
10
721-727
2009
Homo sapiens
Manually annotated by BRENDA team
Wu, J.; Wu, Y.Q.; Ricklin, D.; Janssen, B.J.; Lambris, J.D.; Gros, P.
Structure of complement fragment C3b-factor H and implications for host protection by complement regulators
Nat. Immunol.
10
728-733
2009
Homo sapiens
Manually annotated by BRENDA team
Laursen, N.S.; Gordon, N.; Hermans, S.; Lorenz, N.; Jackson, N.; Wines, B.; Spillner, E.; Christensen, J.B.; Jensen, M.; Fredslund, F.; Bjerre, M.; Sottrup-Jensen, L.; Fraser, J.D.; Andersen, G.R.
Structural basis for inhibition of complement C5 by the SSL7 protein from Staphylococcus aureus
Proc. Natl. Acad. Sci. USA
107
3681-3686
2010
Homo sapiens
Manually annotated by BRENDA team
Camous, L.; Roumenina, L.; Bigot, S.; Brachemi, S.; Fremeaux-Bacchi, V.; Lesavre, P.; Halbwachs-Mecarelli, L.
Complement alternative pathway acts as a positive feedback amplification of neutrophil activation
Blood
117
1340-1349
2011
Homo sapiens
Manually annotated by BRENDA team
Fridkis-Hareli, M.; Storek, M.; Mazsaroff, I.; Risitano, A.M.; Lundberg, A.S.; Horvath, C.J.; Holers, V.M.
Design and development of TT30, a novel C3d-targeted C3/C5 convertase inhibitor for treatment of human complement alternative pathway-mediated diseases
Blood
118
4705-4713
2011
Homo sapiens
Manually annotated by BRENDA team
Hourcade, D.E.; Mitchell, L.M.
Access to the complement factor B scissile bond is facilitated by association of factor B with C3b protein
J. Biol. Chem.
286
35725-35732
2011
Homo sapiens
Manually annotated by BRENDA team
Martinez-Barricarte, R.; Heurich, M.; Valdes-Canedo, F.; Vazquez-Martul, E.; Torreira, E.; Montes, T.; Tortajada, A.; Pinto, S.; Lopez-Trascasa, M.; Morgan, B.P.; Llorca, O.; Harris, C.L.; Rodriguez de Cordoba, S.
Human C3 mutation reveals a mechanism of dense deposit disease pathogenesis and provides insights into complement activation and regulation
J. Clin. Invest.
120
3702-3712
2010
Homo sapiens
Manually annotated by BRENDA team
Luo, S.; Hartmann, A.; Dahse, H.; Skerka, C.; Zipfel, P.
Secreted pH-regulated antigen 1 of Candida albicans blocks activation and conversion of complement C3
J. Immunol.
185
2164-2173
2010
Homo sapiens
Manually annotated by BRENDA team
Forneris, F.; Ricklin, D.; Wu, J.; Tzekou, A.; Wallace, R.; Lambris, J.; Gros, P.
Structures of C3b in complex with factors B and D give insight into complement convertase formation
Science
330
1816-1820
2010
Homo sapiens (P01024)
Manually annotated by BRENDA team
Hebecker, M.; Jozsi, M.
Factor H-related protein 4 activates complement by serving as a platform for the assembly of alternative pathway C3 convertase via its interaction with C3b protein
J. Biol. Chem.
287
19528-19536
2012
Homo sapiens (P00751), Homo sapiens
Manually annotated by BRENDA team
Lee, M.; Guo, J.P.; McGeer, E.G.; McGeer, P.L.
Aurin tricarboxylic acid self-protects by inhibiting aberrant complement activation at the C3 convertase and C9 binding stages
Neurobiol. Aging
34
1451-1461
2013
Homo sapiens (P00751)
Manually annotated by BRENDA team
Okroj, M.; Holmquist, E.; King, B.C.; Blom, A.M.
Functional analyses of complement convertases using C3 and C5-depleted sera
PLoS ONE
7
e47245
2012
Homo sapiens (P00751)
Manually annotated by BRENDA team
Alcorlo, M.; Tortajada, A.; Rodriguez de Cordoba, S.; Llorca, O.
Structural basis for the stabilization of the complement alternative pathway C3 convertase by properdin
Proc. Natl. Acad. Sci. USA
110
13504-13509
2013
Homo sapiens (P00751)
Manually annotated by BRENDA team
Ruggenenti, P.; Daina, E.; Gennarini, A.; Carrara, C.; Gamba, S.; Noris, M.; Rubis, N.; Peraro, F.; Gaspari, F.; Pasini, A.; Rigotti, A.; Lerchner, R.M.; Santoro, D.; Pisani, A.; Pasi, A.; Remuzzi, G.; Remuzzi, G.
C5 convertase blockade in membranoproliferative glomerulonephritis a single-arm clinical trial
Am. J. Kidney Dis.
74
224-238
2019
Homo sapiens
Manually annotated by BRENDA team
Berends, E.T.; Gorham, R.D.; Ruyken, M.; Soppe, J.A.; Orhan, H.; Aerts, P.C.; de Haas, C.J.; Gros, P.; Rooijakkers, S.H.
Molecular insights into the surface-specific arrangement of complement C5 convertase enzymes
BMC Biol.
13
93
2015
Homo sapiens
Manually annotated by BRENDA team
Heesterbeek, D.; Bardoel, B.; Parsons, E.; Bennett, I.; Ruyken, M.; Doorduijn, D.; Gorham, R.J.; Berends, E.; Pyne, A.; Hoogenboom, B.; Rooijakkers, S.
Bacterial killing by complement requires membrane attack complex formation via surface-bound C5 convertases
EMBO J.
38
e99852
2019
Homo sapiens
Manually annotated by BRENDA team
Zwarthoff, S.A.; Berends, E.T.M.; Mol, S.; Ruyken, M.; Aerts, P.C.; Jozsi, M.; de Haas, C.J.C.; Rooijakkers, S.H.M.; Gorham, R.D.
Functional characterization of alternative and classical pathway C3/C5 convertase activity and inhibition using purified models
Front. Immunol.
9
1691
2018
Homo sapiens
Manually annotated by BRENDA team
Fridkis-Hareli, M.; Storek, M.; Or, E.; Altman, R.; Katti, S.; Sun, F.; Peng, T.; Hunter, J.; Johnson, K.; Wang, Y.; Lundberg, A.S.; Mehta, G.; Banda, N.K.; Michael Holers, V.
The human complement receptor type 2 (CR2)/CR1 fusion protein TT32, a novel targeted inhibitor of the classical and alternative pathway C3 convertases, prevents arthritis in active immunization and passive transfer mouse models
Mol. Immunol.
105
150-164
2019
Homo sapiens
Manually annotated by BRENDA team
Di Fede, M.; Biagini, M.; Cartocci, E.; Parillo, C.; Greco, A.; Martinelli, M.; Marchi, S.; Pezzicoli, A.; Delany, I.; Rossi Paccani, S.
Neisseria heparin binding antigen is targeted by the human alternative pathway C3-convertase
PLoS ONE
13
e0194662
2018
Homo sapiens
Manually annotated by BRENDA team