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Literature summary for 3.4.21.47 extracted from
- Factor C acts as a lipopolysaccharide-responsive C3 convertase in horseshoe crab complement activation (2008), J. Immunol., 181, 7994-8001.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| factor C | acts as an LPS-responsive C3 convertase on the surface of invading Gram-negative bacteria in the initial phase of horseshoe crab complement activation. The proteolytic activity of factor C on the surface of Escherichia coli is essential for the deposition of C3b | Tachypleus tridentatus | |
| LPS | proteolytic conversion of C3 to C3b in hemocyanin-depleted plasma is strongly induced by LPS | Tachypleus tridentatus | |
| additional information | proteolytic conversion of C3 to C3b in hemocyanin-depleted plasma is not induced by zymosan, peptidoglycan, or laminarin | Tachypleus tridentatus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ab (2B7) | inhibits the deposition of C3b on Escherichia coli in hemolymph plasma, whereas it exhibits no inhibitory effect on the deposition of C3b on Staphylococcus aureus | Tachypleus tridentatus | |
| hemocyanin-depleted plasma | preincubation of hemocyanin-depleted plasma with the anti-factor C Ab (2B7) dose-dependently inhibits the proteolytic conversion of C3 to C3b in the presence of LPS | Tachypleus tridentatus | |
| hydroxylamine | inactivates the thioester bond on C3, dramatically decreases the deposition of C3b on microbes | Tachypleus tridentatus |  |
| additional information | the anticoagulogen Ab (14E7) has no effect on the conversion of C3. Abs against coagulation factor G (monoclonal) and the proclotting enzyme (polyclonal) do not inhibit the deposition of C3b on Escherichia coli | Tachypleus tridentatus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 185000 | - |
x * 185000, SDS-PAGE | Tachypleus tridentatus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Tachypleus tridentatus | B6ZH52 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| by ion-exchange chromatography | Tachypleus tridentatus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| hemolymph | - |
Tachypleus tridentatus | - |
| plasma | - |
Tachypleus tridentatus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | C3b binds uniformly to substances on the surface of Escherichia coli K12, whereas it shows a bimodal distribution on the surface of Staphylococcus aureus P209. Autoactivation activity of C3 | Tachypleus tridentatus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 185000, SDS-PAGE | Tachypleus tridentatus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| C3 convertase | - |
Tachypleus tridentatus |
| C3bBb | - |
Tachypleus tridentatus |
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