3.4.21.45: complement factor I
This is an abbreviated version!
For detailed information about complement factor I, go to the full flat file.
Word Map on EC 3.4.21.45
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3.4.21.45
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hemolytic
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convertase
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macular
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properdin
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uremic
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cell-bound
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c3d
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fluid-phase
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glomerulonephritis
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complement-mediated
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opsonization
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medicine
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i-mediated
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eculizumab
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alpha\'-chain
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c4-binding
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c4bp
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microangiopathic
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opsonin
- 3.4.21.45
-
hemolytic
-
convertase
-
macular
- properdin
-
uremic
-
cell-bound
- c3d
-
fluid-phase
- glomerulonephritis
-
complement-mediated
-
opsonization
- medicine
-
i-mediated
- eculizumab
-
alpha\'-chain
-
c4-binding
- c4bp
-
microangiopathic
-
opsonin
Reaction
Inactivates complement subcomponents C3b, iC3b and C4b by proteolytic cleavage =
Synonyms
C3b inactivator, C3b/C4b inactivator, C3bINA, CFI, complement C3b inactivator, complement C3b/C4b inactivator, complement C4b inactivator, complement C4bi, complement compoment C3b inactivator, complement factor I, complement inhibitor factor I, complement regulator factor I, conglutinogen-activating factor C, factor I, factor I-like activity, fI, GcIf-1, GcIf-2, GcIf-3, GcIf-4, IF, plasma protease factor I, serine protease Factor I
ECTree
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Inhibitors
Inhibitors on EC 3.4.21.45 - complement factor I
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4-(2-aminoethyl)benzenesulfonyl fluoride
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0.25 mM, inhibits SP domain form and fI
benzyloxycarbonyl-D-Phe-Pro-methoxypropylboroglycinepinanediol ester
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0.05 mM, 82% inhibition; inhibits amidolytic activity
Cr2+
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inhibition of proteolytic and amidolytic activity, 54% inhibition of amidolytic activity at 1 mM, 43% inhibition of proteolytic activity at 0.1 mM
Fe3+
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inhibition of proteolytic and amidolytic activity, 59% inhibition of amidolytic activity at 1 mM, 23% inhibition of proteolytic activity at 0.1 mM
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binds to complement factor I which inhibits the ability of factor I to cleave C3b to inactivated C3b. Addition of factor I restores inactivated C3b production in amyloid beta-treated RPE cells. Preincubation of factor I with amyloid beta in the presence of factor H abolishes the ability of factor I to cleave FGR-7-amino-4-methylcoumarin
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amyloid beta
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production of inactivated C3b is significantly decreased when C3b and factor H are incubated with eyes from neprilysin gene-disrupted mice, which leads to an increased deposition of amyloid beta, compared with when C3b and factor H are incubated with eyes from wild-type mice
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0.0005 mM, 23% inhibition of proteolytic activity. 0.0005 mM, 37% inhibition of amidolytic activity
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0.01 mM, 24% inhibition of amidolytic activity; 0.01 mM, 29% inhibition of proteolytic activity
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1 mM, 90% inhibition of proteolytic activity. 1 mM, 87% inhibition of amidolytic activity
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no inhibition by 0.1 mM 1,10-phenanthroline, 0.001 mM pepstatin A, 0.1 mM chymostatin, 0.0002 mM, C1 inhibitor and 0.1 mM bestatin
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additional information
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factor I is in a proteolytically inactive form, it circulates in a zymogen-like state despite being fully processed to the mature sequence. This inactive form is maintained by the noncatalytic heavy-chain allosterically modulating activity of the light chain. Once the ternary complex of factor I, a cofactor and a substrate is formed, the allosteric inhibition is released, and factor I is oriented for cleavage
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additional information
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the enzyme does not have any known physiological inhibitor, although synthetic inhibitors, such as suramin, are able to weakly inhibit it
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additional information
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phosphorylation of C3b inhibits the cleavage of the alpha'-chain of C3b
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