Amino acid sequence of a kinin-releasing enzyme, KR-E-1, from the venom of Agkistrodon caliginosus (Kankoku-mamushi).

The amino acid sequence of a bradykinin-releasing enzyme, named KR-E-1, isolated from the venom of Agkistrodon caliginosus (Kankoku-mamushi) was determined by Edman sequencing of the peptides which was derived from digests with cyanogen bromide, hydroxylamine, achromobacter protease I, trypsin, V8 protease, arginine endopeptidase, and endoproteinase Asp-N. KR-E-1 consisted of 235 amino acids and showed conservation of the catalytic amino acid residues (His(57), Asp(102), and Ser(195)) of the chymotrypsin family of serine protease in its amino acid sequence. The carboxy-terminal amino acid, Phe, was determined using carboxypeptidase Y. This enzyme contains glucosamine and an N-linked glycosylation site. KR-E-1 showed 32, 31, 65, 65, and 67% sequence homology to human kallikrein, bovine thrombin, KN-BJ 2, elegaxobin, and elegaxobin II, respectively. The characteristic of structure of KR-E-1 was found to involve hydrophobic amino acid residues abundantly localizing in positions 1-50, with lysine residues abundantly localizing in positions 73-101.