Atrolysin B
| Atrolysin B | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.24.41 | ||||||||
| CAS number | 172306-48-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Atrolysin B (EC 3.4.24.41, Crotalus atrox metalloendopeptidase b, hemorrhagic toxin b, Ht-b) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Cleavage of His5-Leu, His10-Leu, Ala14-Leu, Tyr16-Leu and Gly23-Phe of insulin B chain; identical to the cleavage of insulin B chain by atrolysin C. Also cleaves -Ser bonds in glucagon
This enzyme is present in the western diamondback rattlesnake (Crotalus atrox).
References
- ↑ Bjarnason, J.B.; Tu, A.T. (1978). "Hemorrhagic toxins from western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin e". Biochemistry. 17: 3395–3404. doi:10.1021/bi00609a033. PMID 210790.
- ↑ Bjarnason, J.B.; Hamilton, D.; Fox, J.W. (1988). "Studies on the mechanism of hemorrhage production by five proteolytic hemorrhagic toxins from Crotalus atrox venom". Biol. Chem. Hoppe-Seyler. 369: 121–129. PMID 3060135.
External links
- Atrolysin B at the US National Library of Medicine Medical Subject Headings (MeSH)
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