Ruberlysin
| Ruberlysin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.24.48 | ||||||||
| CAS number | 846020-01-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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).
References
- ↑ Mori, N.; Nikai, T.; Sugihara, H.; Tu, A.T. (1987). "Biochemical characterization of hemorrhagic toxins with fibrinogenase activity isolated from 'Crotalus ruber ruber venom". Arch. Biochem. Biophys. 253: 108–121. doi:10.1016/0003-9861(87)90643-6. PMID 2949699.
- ↑ Takeya, H.; Onikura, A.; Nikai, T.; Sugihara, H.; Iwanaga, S. (1990). "Primary structure of a hemorrhagic metalloproteinase, HT-2, isolated from the venom of Crotalus ruber ruber.". J. Biochem. (Tokyo). 108: 711–719. PMID 2081731.
External links
- Ruberlysin at the US National Library of Medicine Medical Subject Headings (MeSH)
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