On the ancestral recruitment of metalloproteinases into the venom of snakes

Toxicon. 2012 Sep 15;60(4):449-54. doi: 10.1016/j.toxicon.2012.02.006. Epub 2012 Mar 3.

Abstract

Tracing the evolutionary history of proteins can reveal insights into gene alterations responsible for changes in structure and function. Here, the origin of snake venom metalloproteinases was rigorously reassessed using phylogenetics and the reconstruction of ancestral sequences. Basal SVMPs are most closely related to ADAM 7, 28 and decysin-1 proteins. Reconstructing the evolutionary history of these proteins and their hypothetical ancestors reveals progressive alterations in the amino acid composition and structural characteristics of ADAMs/SVMPs through evolutionary time.

MeSH terms

  • ADAM Proteins / chemistry
  • ADAM Proteins / genetics
  • ADAM Proteins / metabolism
  • Amino Acid Sequence
  • Animals
  • Evolution, Molecular*
  • Humans
  • Metalloendopeptidases / chemistry
  • Metalloendopeptidases / genetics
  • Metalloendopeptidases / metabolism
  • Metalloproteases / chemistry
  • Metalloproteases / genetics
  • Metalloproteases / metabolism*
  • Molecular Sequence Data
  • Phylogeny
  • Snake Venoms / chemistry
  • Snake Venoms / enzymology*
  • Snake Venoms / genetics

Substances

  • Snake Venoms
  • Metalloproteases
  • ADAM Proteins
  • Metalloendopeptidases
  • decysin