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Molecular Cloning and Sequence Analysis of cDNA Encoding Acutolysin C, a Hemorrhagic Metalloproteinase, from
Qing-Du Liu1, Wei-Hua Xu, Xin Cheng
1School of Life Science, University of Science and Technology of China, Hefei 230027, China. jliu@ustc.edu.cn
Abstract:
A full-length cDNA of 1 650 bp was amplified from the snake venom gland cDNA library of Agkistrodon acutus. Analysis of the nucleotide sequence indicated that the amplified cDNA contained a complete open reading frame encoding 417 amino acid residues including signal peptide sequence, zymogen sequence and proteinase domain. The zymogen sequence contained CGVT motif that was highly conserved in almost all venom metalloproteinases. The metalloproteinase domain contained a conserved signature zinc-binding motif HEXXHXXGXXH in the catalytic region and the CIM turn. It shares high similarity with the sequence of acutolysin C deduced from crystallographic data, and with other class P-I snake venom hemorrhagic toxins.
