Identification of residues linked to the slow → fast transition of thrombin

Enriqueta R. Guinto, Alessandro Vindigni, Youhna M. Ayala, Quoc D. Dang, Enrico Di Cera

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Residues energetically linked to the allosteric transition of thrombin from its anticoagulant slow form to the procoagulant fast form have been identified by site-directed mutagenesis. The energetics of recognition by the two forms of the enzyme were probed by using a synthetic chromogenic substrate, fibrinogen, and hirudin. The thrombin residues E39, W60d, E192, D221, and D222 are linked to the slow → fast transition and are part of an 'allosteric core' through which events originating at the Na+ binding loop propagate to other regions of the enzyme. The thrombin residues Y76, W96, W148, and R173 lie at the periphery of the allosteric core, affect recognition of fibrinogen and hirudin to the same extent in both forms, and are not linked to the slow → fast transition.

Original languageEnglish
Pages (from-to)11185-11189
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number24
StatePublished - Nov 21 1995


  • allostery
  • fibrinogen
  • hirudin
  • molecular recognition
  • site-directed mutagenesis


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