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Literature summary for 3.4.21.86 extracted from

  • Muta, T.; Hashimoto, R.; Miyata, T.; Nishimura, H.; Toh, Y.; Iwanaga, S.
    Proclotting enzyme from horseshoe crab hemocytes. cDNA cloning, disulfide locations, and subcellular localization (1990), J. Biol. Chem., 265, 22426-22433.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information activated by limulus clotting factor B Limulus sp.

Cloned(Commentary)

Cloned (Comment) Organism
of proclotting enzyme, the zymogen of clotting enzyme Limulus sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
intracellular zymogen Limulus sp. 5622
-
zymogen granule
-
Limulus sp. 42588
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38190
-
Limulus sp., calculation from nucleotide sequence, mature protein Limulus sp.

Organism

Organism UniProt Comment Textmining
Limulus sp.
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein 3 potential glycosylation sites for N-linked carbohydrate chains. Moreover the zymogen contains 6 O-linked carbohydrate chains in the amino-terminal light chain generated after activation Limulus sp.

Source Tissue

Source Tissue Comment Organism Textmining
hemocyte
-
Limulus sp.
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Coagulogen + H2O
-
Limulus sp. Coagulin + fragments
-
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