Abstract
This chapter examines the activity, specificity and structural chemistry of acutolysin. Acutolysin is the name given to the hemorrhagic toxin Acl-proteinase classified as a zinc metalloproteinase isolated from the venom of Agkistrodon acutus. Acutolysin is composed of 202 amino acid residues and is a single-chain protein of 22,944 Da with a pi of 4.7. This enzyme contains lmol of zinc per mol of toxin and a drastic change is observed in the low-frequency region of the Raman spectrum if zinc is removed from acutolysin. Metalloproteinases in snake venoms are classified into four groups and acutolysin belongs to class I. The crystal structure of acutolysin A and the location of the catalytic zinc ion are elaborated. Acutolysin is isolated from Agkistrodon acutus venom by a combination of gel-filtration and ion-exchange column chromatographies. A hemorrhagic metalloprotease, hemorrhagin IV, with a molecular weight of 44 kDa and a pi of 5.0 was also isolated from A. acutus venom, and it had lethal and caseinolytic activities. By cloning and sequence analysis for pro-metalloprotease-disintegrin variants from A. acutus venom, a total of seven cDNA clones encoding the multidomain precursors of six acidic and one alkaline low molecular mass metalloproteases were identified in venom gland cDNA .
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