Activation of prothrombin by ASP, a serine protease released from Aeromonas sobria

FEBS Lett. 2007 Dec 22;581(30):5935-9. doi: 10.1016/j.febslet.2007.11.076. Epub 2007 Dec 5.


The effect of a serine protease (ASP) secreted from Aeromonas sobria on plasma coagulation was investigated. Proteolytically active ASP promoted human plasma coagulation in a dose-dependent manner. Consistent with the preference for a factor Xa-specific oligo-peptide substrate, ASP produced enzymatic activity from human prothrombin but not from factors IX and X. ASP cleaved prothrombin to produce enzymatically active 37 kDa-fragment displaying the same molecular mass as alpha-thrombin. ASP is the first bacterial serine protease that produces alpha-thrombin, through which ASP may contribute to the induction of thrombotic tendency in disseminated intravascular coagulation complicated with sepsis caused by A. sobria infections.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aeromonas / drug effects
  • Aeromonas / enzymology*
  • Amino Acid Sequence
  • Blood Coagulation / drug effects
  • Blood Coagulation Factors / chemistry
  • Blood Coagulation Factors / metabolism
  • Enzyme Precursors / metabolism
  • Humans
  • Molecular Sequence Data
  • Peptides / chemistry
  • Peptides / metabolism
  • Prothrombin / chemistry
  • Prothrombin / metabolism*
  • Serine Endopeptidases / pharmacology*
  • Substrate Specificity / drug effects


  • Blood Coagulation Factors
  • Enzyme Precursors
  • Peptides
  • Prothrombin
  • Serine Endopeptidases