Ruberlysin
From Wikipedia the free encyclopedia
| Ruberlysin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.48 | ||||||||
| CAS no. | 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[edit]
- ^ 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.
- ^ 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.
External links[edit]
- Ruberlysin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
