Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.86 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
Search for more literature for 3.4.21.86

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
coagulogen + H2O Limulus polyphemus
-
 coagulin + propeptide
-
 ?

Organism

Organism UniProt Comment Textmining
Limulus polyphemus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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

Source Tissue Comment Organism Textmining
amebocyte
-
 Limulus polyphemus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
coagulogen + H2O
-
 Limulus polyphemus coagulin + propeptide
-
 ?
coagulogen + H2O chromogenic substrate Limulus polyphemus coagulin + propeptide
-
 ?
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 ?
-
 ?
peptide-4-nitroanilide + H2O
-
 Limulus polyphemus peptide + 4-nitroaniline
-
 ?

Synonyms

Synonyms Comment Organism
Clotting enzyme
-
 Limulus polyphemus

General Information

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