American Society of Hirudotherapy

Determinants of specificity in coagulation proteases.

Review published in Journal of thrombosis and haemostasis : JTH (2005)

Last Updated: June 18, 2026Reviewed by: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Narrative reviewDrug DevelopmentSalivary PharmacologyPage et al. · Journal of thrombosis and haemostasis : JTH, 2005

Abstract

Proteases play diverse roles in a variety of essential biological processes, both as non-specific catalysts of protein degradation and as highly specific agents that control physiologic events. Here, we review the mechanisms of substrate specificity employed by serine proteases and focus our discussion on coagulation proteases. We dissect the interplay between active site and exosite specificity and how substrate recognition is regulated allosterically by Na+ binding. We also draw attention to a functional polarity that exists in the serine protease fold, which sheds light on the structural linkages between the active site and exosites.

Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.

Publication typeJournal ArticleResearch Support, N.I.H., ExtramuralResearch Support, Non-U.S. Gov'tReview
Indexed MeSH termsAllosteric RegulationAmino Acid SequenceAnimalsBinding SitesBlood CoagulationCatalytic DomainEnzyme ActivationHumansMolecular Sequence DataProtein ConformationProtein FoldingSerine Endopeptidases

Summary

Proteases play diverse roles in a variety of essential biological processes, both as non-specific catalysts of protein degradation and as highly specific agents that control physiologic events. Here, we review the mechanisms of substrate specificity employed by serine proteases and focus our...

Why This Matters for Hirudotherapy

This review examines mechanisms of substrate specificity employed by serine proteases, focusing on coagulation proteases and dissecting the interplay between active-site and exosite specificity, how substrate recognition is regulated allosterically by Na+ binding, and functional polarity in the protease fold that links the active site to exosites. The work provides a conceptual framework for understanding how coagulation enzymes achieve substrate selectivity through coordinated structural features. CAVEAT: The abstract does not mention hirudin, leeches, or any leech-derived anticoagulant, nor does it single out thrombin by name; this is a general review of coagulation protease biology with no defensible leech link to ASH's domain.

Citation

Determinants of specificity in coagulation proteases.

Page et al. · Journal of thrombosis and haemostasis : JTH, 2005

DOI

Added to ASH library: May 28, 2026 · Site last updated: June 18, 2026

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