Biology:Atrolysin E
From HandWiki
| Atrolysin E | |||||||||
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| Identifiers | |||||||||
| EC number | 3.4.24.44 | ||||||||
| CAS number | 172306-51-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Atrolysin E (EC 3.4.24.44, Crotalus atrox metalloendopeptidase e, hemorrhagic toxin e) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Cleavage of Asn3-Gln, Ser9-His and Ala14-Leu bonds in insulin B chain and Tyr14-Gln and Thr8-Ser in A chain. Cleaves type IV collagen at Ala73-Gln in alpha1(IV) and at Gly7-Leu in alpha2(IV)
This endopeptidase is present in the venom of the western diamondback rattlesnake (Crotalus atrox).
References
- ↑ "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 (16): 3395–404. August 1978. doi:10.1021/bi00609a033. PMID 210790.
- ↑ "Proteolytic specificity and cobalt exchange of hemorrhagic toxin e, a zinc protease isolated from the venom of the western diamondback rattlesnake (Crotalus atrox)". Biochemistry 22 (16): 3770–8. August 1983. doi:10.1021/bi00285a009. PMID 6351911.
- ↑ "Identification of the cleavage sites by a hemorrhagic metalloproteinase in type IV collagen". Matrix 10 (2): 91–7. May 1990. doi:10.1016/s0934-8832(11)80175-7. PMID 2374521.
External links
- Atrolysin+E at the US National Library of Medicine Medical Subject Headings (MeSH)
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