Snake venom thrombin-like enzymes: from reptilase to now

Cell Mol Life Sci. 2004 Apr;61(7-8):843-56. doi: 10.1007/s00018-003-3325-z.

Abstract

The snake venom thrombin-like enzymes (SVTLEs) comprise a number of serine proteases functionally and structurally related to thrombin. Until recently, only nine complete sequences of this subgroup of the serine protease family were known. Over the past 5 years, the primary structure of several SVTLEs has been characterized, and now this family includes several members. Of particular interest is their possible use in pathologies such as thrombosis. The aim of the present review is to summarize the state of the art concerning the evolutionary, structural and biological features of the SVTLEs.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Batroxobin* / chemistry
  • Batroxobin* / classification
  • Batroxobin* / physiology
  • Batroxobin* / therapeutic use
  • Binding Sites
  • Catalytic Domain
  • Enzyme Inhibitors / metabolism
  • Hemostatics / chemistry
  • Hemostatics / metabolism
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Sequence Alignment
  • Serine Endopeptidases* / chemistry
  • Serine Endopeptidases* / classification
  • Serine Endopeptidases* / physiology
  • Serine Endopeptidases* / therapeutic use
  • Snake Venoms / chemistry*
  • Thrombin* / chemistry
  • Thrombin* / genetics
  • Thrombin* / metabolism

Substances

  • Enzyme Inhibitors
  • Hemostatics
  • Snake Venoms
  • Batroxobin
  • Serine Endopeptidases
  • Thrombin