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Literature summary extracted from

  • Abate, W.; Sattar, A.A.; Liu, J.; Conway, M.E.; Jackson, S.K.
    Evaluation of recombinant factor C assay for the detection of divergent lipopolysaccharide structural species and comparison with Limulus amebocyte lysate-based assays and a human monocyte activity assay (2017), J. Med. Microbiol., 66, 888-897 .
    View publication on PubMed

Activating Compound

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

Natural Substrates/ Products (Substrates)

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
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.84 Limulus polyphemus
-
-
-
3.4.21.86 Limulus polyphemus
-
-
-

Posttranslational Modification

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.21.84 amoebocyte
-
Limulus polyphemus
-
3.4.21.86 amebocyte
-
Limulus polyphemus
-

Substrates and Products (Substrate)

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
-
?

Synonyms

EC Number Synonyms Comment Organism
3.4.21.84 Factor C
-
Limulus polyphemus
3.4.21.86 Clotting enzyme
-
Limulus polyphemus

General Information

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