Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8397078 | Toxicon | 2013 | 5 Pages |
Abstract
Scorpion venoms metalloproteinase is involved in a number of important biological, physiological and pathophysiological processes. In this work, a complete sequence of metalloproteinase was first obtained from venom of scorpion Buthus martensi and named as BumaMPs1. BumaMPs1 has 393 amino acid residues containing with a molecular mass of 44.53Â kDa, showing an isoelectric point of 5.66. The primary sequence analysis indicated that the BumaMPs1 contains a zinc-binding motif (HELGHNLGISH), methionine-turn motif (YIM), disintegrin-like domain (ETCD) and N-glycosylation site. The multiple alignment of its deduced amino acid sequence and those of other metalloproteinase showed a high structural similarly, mainly among class reprolysin proteases. The phylogenetic analysis showed early divergence and independent evolution of BumaMPs1 from other metalloproteinase.
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Authors
Xichao Xia, Yuhong Ma, Shipeng Xue, Aimei Wang, Junliang Tao, Yan Zhao, Qingyuan Zhang, Rongzhi Liu, Shaoe Lu,