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Toxicon. 2013 Dec 15;76:234-8. doi: 10.1016/j.toxicon.2013.10.006. Epub 2013 Oct 12.

Cloning and molecular characterization of BumaMPs1, a novel metalloproteinases from the venom of scorpion Buthus martensi Karsch.

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  • 1Basal Medical College of Nanyang Medical University, Nanyang 473041, Henan Province, China. Electronic address: xiaxichao8336@163.com.


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 44.53 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.

Copyright © 2013 Elsevier Ltd. All rights reserved.


Buthus martensi; Cloning and molecular characterization; Metalloproteinase; Phylogenetic tree

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