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J. Biochem, 1988, Vol. 103, No. 4 596-605
© 1988 Japanese Biochemical Society

research-article

Amino Acid Sequence of a Coagulant Enzyme, Flavoxobin, from Trimeresurus flavoviridis Venom1

Tiee-Cherng Shieh, Faculty of Medicine*, Shun-ichiro Kawabata**, Hiroshi Kihara***, Motonori Ohno, Faculty of Science*,2 and Sadaaki Iwanaga**

*Department of Chemistry, Kyushu University Higashi-ku, Fukuoka, Fukuoka 812
**Department of Biology,Kyushu University Higashi-ku, Fukuoka, Fukuoka 812
***Department of Physiology,Kagoshima University Kagoshima, Kagoshima 890

2To whom correspondence should be addressed.

The amino acid sequence of a coagulant enzyme, named flavoxobin, isolated from the venom of Trimeresurus flavoviridis (the habu snake) was determined by sequencing the S-pyridylethylated derivative of the protein and its peptides generated by chemical (cyanogen bromide and hydroxylamine) and enzymatic (clostripain, Staphylococcus aureus V8 protease, Achromobacter protease I, and elastase) cleavages. Hydrazinolysis was also employed to determine the C-terminal amino acid. The enzyme consisted of 236 amino acids and had a calculated molecular weight of 25, 744. Flavoxobin was found to be highly (69%) homologous in sequence to batroxobin, a coagulant enzyme from the venom of Bothrops atrox, and 27, 39, and 31% homologous to bovine thrombin, bovine trypsin, and human kallikrein, respectively. The sequence around the active site serine residue deduced from the homology relationship was Phe-Asp-Ser-Gly-Thr, which is different from the common sequence, Gly-Asp-Ser-Gly-Gly, for most serine proteases. Flavoxobin appears to be similar in secondary structure composition to batroxobin.

1This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.


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