Sociedad Americana de Hirudoterapia

Determinants of specificity in coagulation proteases.

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

Última actualización: June 18, 2026Revisado por: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Narrative reviewDesarrollo de fármacosFarmacología salivalPage 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

Resumen

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...

Por qué esto importa para la hirudoterapia

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.

Citación

Determinants of specificity in coagulation proteases.

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

DOI

Contexto clínico relacionado

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Añadido a la biblioteca ASH: May 28, 2026 · Última actualización del sitio: June 18, 2026

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