Activating Compound | Comment | Organism | Structure |
---|---|---|---|
lipopolysaccharide | factor C activation through lipopolysaccharide assay. Detection of various LPS structural species by rFC-based assay. Several bacterial species are used as sources for endotoxin/lipopolysaccharide, overview. Highest activity is obtained with Escherichia coli LPS O111:B4 and J5, lowest activity with LPS from Francisella tularensis or Salmonella lipid A. Induction of interleukin IL-6 by various LPS structural species | Limulus polyphemus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
pro-factor B + H2O | Limulus polyphemus | activation | factor B + ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Limulus polyphemus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
amoebocyte | - |
Limulus polyphemus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pro-factor B + H2O | activation | Limulus polyphemus | factor B + ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Factor C | - |
Limulus polyphemus |
General Information | Comment | Organism |
---|---|---|
metabolism | the enzyme is part of the clotting cascade of Limulus polyphemus. Factor C, the first component of the cascade, is a serine protease that is activated by endotoxin binding. The cascade, initiated by lipopolysaccharide, culminates in the activation of the pro-clotting enzyme to its active form, the clotting enzyme, which in turn acts on coagulogen to convert it into the coagulin clot | Limulus polyphemus |
physiological function | Factor C activates factor B in the clotting cascade in Limulus polyphemus | Limulus polyphemus |