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Limulus clotting enzyme

From Wikipedia, the free encyclopedia

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

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]

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References

  1. ^ 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. doi:10.1016/S0021-9258(18)45722-5. PMID 2266134.
  2. ^ 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.
  3. ^ 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.

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This page was last edited on 24 January 2024, at 17:53
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