ExplorEnz: EC 3.4.21.84

Your query returned 1 entry. Printable version

3.4.21.84

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, Gene, KEGG, MetaCyc, MEROPS, CAS registry number: 115743-27-6

References:

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 3.4.21.84 created 1993]