The Enzyme Database

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Accepted name: limulus clotting factor C
Reaction: Selective cleavage of -Arg103┼Ser- and -Ile124┼Ile- bonds in limulus clotting factor B to form factor B. Cleavage of -Pro-Arg┼ bonds in synthetic substrates
Other name(s): factor C; limulus factor C
Comments: From the hemocyte granules of the horseshoe crabs Limulus and Tachypleus. Factor C is activated by Gram-negative bacterial lipopolysaccharides and chymotrypsin. Inhibited by antithrombin III. In peptidase family S1 (trypsin family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 115743-27-6
1.  Nakamura, T., Morita, T. and Iwanaga, S. Lipopolysaccharide-sensitive serine-protease zymogen (factor C) found in Limulus hemocytes. Isolation and characterization. Eur. J. Biochem. 154 (1986) 511–521. [DOI] [PMID: 3512266]
2.  Muta, T., Miyata, T., Misumi, Y., Tokunaga, F., Nakamura, T., Toh, Y., Ikehara, Y. and Iwanaga, S. Limulus factor C. An endotoxin-sensitive serine protease zymogen with a mosaic structure of complement-like, epidermal growth factor-like, and lectin-like domains. J. Biol. Chem. 266 (1991) 6554–6561. [PMID: 2007602]
3.  Tokunaga, F., Nakajima, H. and Iwanaga, S. Further studies on lipopolysaccharide-sensitive serine protease zymogen (factor C): its isolation from Limulus polyphemus hemocytes and identification as an intracellular zymogen activated by α-chymotrypsin, not by trypsin. J. Biochem. (Tokyo) 109 (1991) 150–157. [PMID: 2016264]
[EC created 1993]

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