Limulus clotting enzyme
Limulus clotting enzyme (EC 3.4.21.86, clotting enzyme) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Selective cleavage of -Arg18- and -Arg47- bonds in coagulogen to form coagulin and fragments
| Limulus clotting enzyme | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.21.86 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
This enzyme is present in the hemocyte granules of horseshoe crabs Limulus and Tachypleus. In the immunity-related clotting pathways of these organisms, it is the final enzyme responsible for the activation of coagulin.[3]
References
- Muta T, Hashimoto R, Miyata T, Nishimura H, Toh Y, Iwanaga S (December 1990). "Proclotting enzyme from horseshoe crab hemocytes. cDNA cloning, disulfide locations, and subcellular localization". The Journal of Biological Chemistry. 265 (36): 22426–33. PMID 2266134.
- 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. 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. doi:10.2183/pjab.83.110. PMC 3756735. PMID 24019589.
External links
- Limulus+clotting+enzyme at the US National Library of Medicine Medical Subject Headings (MeSH)
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