Ruberlysin

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Ruberlysin
Identifiers
EC no. 3.4.24.48
CAS no. 846020-01-7
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Ruberlysin (EC 3.4.24.48, Crotalus ruber metalloendopeptidase II, hemorrhagic toxin II) is an enzyme. [1] [2] This enzyme catalyses the following chemical reaction

Cleavage of His10-Leu, Ala14-Leu, Tyr16-Leu and Gly23-Phe bonds in the B chain of insulin; His-Pro, Pro-Phe, and Trp-Ser of angiotensin I; and Gly-Phe of Met enkephalin

This endopeptidase is present in the venom of the red rattlesnake ( Crotalus ruber ruber ).

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Atrolysin A is an enzyme that is one of six hemorrhagic toxins found in the venom of western diamondback rattlesnake. This endopeptidase has a length of 419 amino acid residues. The metalloproteinase disintegrin-like domain and the cysteine-rich domain of the enzyme are responsible for the enzyme's hemorrhagic effects on organisms via inhibition of platelet aggregation.

Atrolysin B is an enzyme. This enzyme catalyses the following chemical reaction

Atrolysin C is an enzyme. This enzyme catalyses the following chemical reaction

Atrolysin E is an enzyme. This enzyme catalyses the following chemical reaction

Atrolysin F is an enzyme. This enzyme catalyses the following chemical reaction

Horrilysin is an enzyme. This enzyme catalyses the following chemical reaction

Trimerelysin I is an enzyme. This enzyme catalyses the following chemical reaction

Trimerelysin II is an enzyme. This enzyme catalyses the following chemical reaction

Mucrolysin is an enzyme. This enzyme catalyses the following chemical reaction

Fibrolase is an enzyme. This enzyme catalyses the following chemical reaction

Jararhagin is an enzyme. This enzyme catalyses the following chemical reaction

Agelenin, also called U1-agatoxin-Aop1a, is an antagonist of the presynaptic P-type calcium channel in insects. This neurotoxic peptide consists of 35 amino acids and can be isolated from the venom of the spider Allagelena opulenta.

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References

  1. Mori N, Nikai T, Sugihara H, Tu AT (February 1987). "Biochemical characterization of hemorrhagic toxins with fibrinogenase activity isolated from Crotalus ruber ruber venom". Archives of Biochemistry and Biophysics. 253 (1): 108–21. doi:10.1016/0003-9861(87)90643-6. PMID   2949699.
  2. Takeya H, Onikura A, Nikai T, Sugihara H, Iwanaga S (November 1990). "Primary structure of a hemorrhagic metalloproteinase, HT-2, isolated from the venom of Crotalus ruber ruber". Journal of Biochemistry. 108 (5): 711–9. PMID   2081731.