KEGG   ENZYME: 3.4.21.84Help
Entry
EC 3.4.21.84                Enzyme                                 

Name
limulus clotting factor _overbar_C_;
factor C;
limulus factor C
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Selective cleavage of -Arg103!Ser- and -Ile124!Ile- bonds in limulus clotting factor B to form factor _overbar_B_. Cleavage of -Pro-Arg! bonds in synthetic substrates
Comment
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)
History
EC 3.4.21.84 created 1993
Orthology
K22079  limulus clotting factor C
Reference
1  [PMID:3512266]
  Authors
Nakamura T, Morita T, Iwanaga S.
  Title
Lipopolysaccharide-sensitive serine-protease zymogen (factor C) found in Limulus hemocytes. Isolation and characterization.
  Journal
Eur J Biochem 154:511-21 (1986)
DOI:10.1111/j.1432-1033.1986.tb09427.x
Reference
2  [PMID:2007602]
  Authors
Muta T, Miyata T, Misumi Y, Tokunaga F, Nakamura T, Toh Y, Ikehara Y, Iwanaga S.
  Title
Limulus factor C. An endotoxin-sensitive serine protease zymogen with a mosaic structure of complement-like, epidermal growth factor-like, and lectin-like domains.
  Journal
J Biol Chem 266:6554-61 (1991)
  Sequence
Reference
3  [PMID:2016264]
  Authors
Tokunaga F, Nakajima H, Iwanaga S.
  Title
Further studies on lipopolysaccharide-sensitive serine protease zymogen (factor C): its isolation from Limulus polyphemus hemocytes and identification as an intracellular zymogen activated by alpha-chymotrypsin, not by trypsin.
  Journal
J Biochem (Tokyo) 109:150-7 (1991)
Other DBs
ExplorEnz - The Enzyme Database: 3.4.21.84
IUBMB Enzyme Nomenclature: 3.4.21.84
ExPASy - ENZYME nomenclature database: 3.4.21.84
BRENDA, the Enzyme Database: 3.4.21.84
CAS: 115743-27-6

DBGET integrated database retrieval system