Limulus clotting factor C
From Wikipedia the free encyclopedia
| Limulus clotting factor overbar C | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.21.84 | ||||||||
| CAS no. | 115743-27-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
| Limulus clotting factor C | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | ? | ||||||
| UniProt | P28175 | ||||||
| |||||||
Limulus clotting factor overbar C (EC 3.4.21.84, factor C, limulus factor C) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- 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
This enzyme is isolated from the hemocyte granules of the horseshoe crabs Limulus and Tachypleus, where it serves as a LPS endotoxin-sensitive trypsin type serine protease to protect the organism from bacterial infection, initiating a cascade leading to coagulin formation.[4] From the N-terminus to the C-terminus, the domains are:
- EGF-like domain
- 3 Sushi domains
- one LCCL domain and one C-type lectin domain
- 2 more Sushi domains
- a trypsin domain
This enzyme is useful in Limulus amebocyte lysate as the endotoxin-detecting element. It can be produced recombinantly.[5]
References[edit]
- ^ Nakamura T, Morita T, Iwanaga S (February 1986). "Lipopolysaccharide-sensitive serine-protease zymogen (factor C) found in Limulus hemocytes. Isolation and characterization". European Journal of Biochemistry. 154 (3): 511–21. doi:10.1111/j.1432-1033.1986.tb09427.x. PMID 3512266.
- ^ Muta T, Miyata T, Misumi Y, Tokunaga F, Nakamura T, Toh Y, et al. (April 1991). "Limulus factor C. An endotoxin-sensitive serine protease zymogen with a mosaic structure of complement-like, epidermal growth factor-like, and lectin-like domains". The Journal of Biological Chemistry. 266 (10): 6554–61. doi:10.1016/S0021-9258(18)38153-5. PMID 2007602.
- ^ Tokunaga F, Nakajima H, Iwanaga S (January 1991). "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 of Biochemistry. 109 (1): 150–7. doi:10.1093/oxfordjournals.jbchem.a123337. PMID 2016264.
- ^ Iwanaga S (May 2007). "Biochemical principle of Limulus test for detecting bacterial endotoxins". Proceedings of the Japan Academy. Series B, Physical and Biological Sciences. 83 (4): 110–9. Bibcode:2007PJAB...83..110I. doi:10.2183/pjab.83.110. PMC 3756735. PMID 24019589.
- ^ Maloney T, Phelan R, Simmons N (October 2018). "Saving the horseshoe crab: A synthetic alternative to horseshoe crab blood for endotoxin detection". PLOS Biology. 16 (10): e2006607. doi:10.1371/journal.pbio.2006607. PMC 6200278. PMID 30312293.
External links[edit]
- Limulus+clotting+factor+_overbar_C_ at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
