EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.4.21.84 | 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 |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.21.84 | pro-factor B + H2O | Limulus polyphemus | activation | factor B + ? | - |
? | |
3.4.21.86 | coagulogen + H2O | Limulus polyphemus | - |
coagulin + propeptide | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.21.84 | Limulus polyphemus | - |
- |
- |
3.4.21.86 | Limulus polyphemus | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.4.21.86 | proteolytic modification | the pro-clotting enzyme is activated by cleavage through factor B or factor G, the latter with less activity | Limulus polyphemus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.4.21.84 | amoebocyte | - |
Limulus polyphemus | - |
3.4.21.86 | amebocyte | - |
Limulus polyphemus | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.21.84 | pro-factor B + H2O | activation | Limulus polyphemus | factor B + ? | - |
? | |
3.4.21.86 | coagulogen + H2O | - |
Limulus polyphemus | coagulin + propeptide | - |
? | |
3.4.21.86 | coagulogen + H2O | chromogenic substrate | Limulus polyphemus | coagulin + propeptide | - |
? | |
3.4.21.86 | additional information | the clotting enzyme can be used in the Limulus amebocytelysate (LAL) assay. The kinetic chromogenic LAL assay uses a synthetic peptide-4-nitroanilide substrate that is cleaved by the clotting enzyme, resulting in a product that exhibits a yellow colour. The intensity of the yellow colour or the rate of colour formation correlates with the concentration of LPS in the assayed samples. The coagulation cascade of the LAL system can also be activated via activation of factor G by fungal glucans, although the activation of factor C, which then activates factor B, by LPS is many times more sensitive. Assay method development and evaluation, overview | Limulus polyphemus | ? | - |
? | |
3.4.21.86 | peptide-4-nitroanilide + H2O | - |
Limulus polyphemus | peptide + 4-nitroaniline | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.21.84 | Factor C | - |
Limulus polyphemus |
3.4.21.86 | Clotting enzyme | - |
Limulus polyphemus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.4.21.84 | 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 |
3.4.21.84 | physiological function | Factor C activates factor B in the clotting cascade in Limulus polyphemus | Limulus polyphemus |
3.4.21.86 | 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 |