The Enzyme Database

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EC 3.4.24.44     
Accepted name: atrolysin E
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 α1(IV) and at Gly7┼Leu in α2(IV)
Other name(s): Crotalus atrox metalloendopeptidase e; hemorrhagic toxin e
Comments: A 25.7 kDa hemorrhagic endopeptidase from the venom of the western diamondback rattlesnake (Crotalus atrox) that digests basement membrane components, including the triple helix of type IV collagen. Such action is believed to contribute to the hemorrhagic property by weakening capillary walls. In peptidase family M12 (astacin family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 172306-51-3
References:
1.  Bjarnason, J.B. and Tu, A.T. 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 (1978) 3395–3404. [PMID: 210790]
2.  Bjarnason, J.B. and Fox, J.W. 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 (1983) 3770–3778. [PMID: 6351911]
3.  Baramova, E.N., Shannon, J.D., Bjarnason, J.B. and Fox, J.W. Identification of the cleavave sites by a hemorrhagic metalloproteinase in type IV collagen. Matrix 10 (1990) 91–97. [PMID: 2374521]
[EC 3.4.24.44 created 1992]
 
 


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