Snake venom serine proteinases: sequence homology vs. substrate specificity, a paradox to be solved

Toxicon. 2005 Jun 15;45(8):1115-32. doi: 10.1016/j.toxicon.2005.02.020. Epub 2005 Apr 19.

Abstract

Snake venom glands synthesize a variety of serine proteinases capable of affecting the haemostatic system. They act on macromolecular substrates of the coagulation, fibrinolytic, and kallikrein-kinin systems, and on platelets to cause an imbalance of the haemostatic system of the prey. In this review we describe their biochemical/biophysical characteristics, biological activities as well as aspects of their evolution and structure-activity relationship.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Blood Coagulation / physiology*
  • Evolution, Molecular*
  • Molecular Sequence Data
  • Phylogeny*
  • Sequence Homology, Amino Acid*
  • Serine Endopeptidases / genetics*
  • Serine Endopeptidases / metabolism*
  • Serine Proteinase Inhibitors / metabolism
  • Snake Venoms / enzymology*
  • Snakes*
  • Substrate Specificity / genetics

Substances

  • Serine Proteinase Inhibitors
  • Snake Venoms
  • Serine Endopeptidases