Amino acid sequence of a neurotoxic phospholipase A2 enzyme from common death adder (Acanthophis antracticus) venom.
The amino acid sequence of the first neurotoxic phospholipase A2, acanthoxin A1, purified from the venom of the Common death adder (Acanthophis antarcticus) was determined. Acanthoxin A1 shows high homology with other Australian elapid PLA2 neurotoxins, in particular Acanthin-I and -II, also from Death adder, Pseudexin A from the Red-bellied black snake (Pseudechis porphyriacus), and Pa-12a and Pa-9c from the King brown snake (Pseudechis australis). Acanthoxin A1 is a single-chain 118 amino acid residue PLA2, including 14 half cystine residues and the essential residues forming the ubiquitous calcium binding pocket and catalytic site. Critical analysis of the residues hypothesized to be important for neurotoxicity is presented.
van der Weyden
L
L
Department of Cell and Molecular Biology, University of Technology, Sydney, Gore Hill, Australia.
Hains
P
P
Broady
K
K
Shaw
D
D
Milburn
P
P
D000595:Amino Acid Sequence; D000818:Animals; D004546:Elapid Venoms / Q000235:genetics; D017815:Elapidae / Q000235:genetics*; D008297:Male; D008969:Molecular Sequence Data; D010741:Phospholipases A / Q000235:genetics* / Q000302:isolation & purification; D054467:Phospholipases A2; D017386:Sequence Homology, Amino Acid
D004546:Elapid Venoms; C026235:Pseudechis venom; D010741:Phospholipases A; D054467:Phospholipases A2; C108584:acanthoxin