Sociedad Americana de Hirudoterapia

Rational engineering of activity and specificity in a serine protease.

Research article published in Nature biotechnology (1997)

Última actualización: June 18, 2026Revisado por: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Research reportDesarrollo de fármacosFarmacología salivalDang et al. · Nature biotechnology, 1997

Abstract

The discovery of the Na(+)-dependent allosteric regulation in serine proteases makes it possible to control catalytic activity and specificity in this class of enzymes in a way never considered before. We demonstrate that rational site-directed mutagenesis of residues controlling Na+ binding can profoundly after the properties of a serine protease. By suppressing Na+ binding to thrombin, we shift the balance between procoagulant and anticoagulant activities of the enzyme. Those mutants, compared to wild-type, have reduced specificity toward fibrinogen, but enhanced or slightly reduced specificity toward protein C. Because this engineering strategy targets a fundamental regulatory mechanism, it is amenable of extension to other enzymes of biological and pharmacological importance.

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

Publication typeJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.
Indexed MeSH termsAmino Acid SequenceAnticoagulantsBinding SitesCoagulantsFibrinogenHumansKineticsModels, MolecularMutagenesis, Site-DirectedPoint MutationPolymerase Chain ReactionProtein C

Resumen

The discovery of the Na(+)-dependent allosteric regulation in serine proteases makes it possible to control catalytic activity and specificity in this class of enzymes in a way never considered before. We demonstrate that rational site-directed mutagenesis of residues controlling Na+ binding can...

Por qué esto importa para la hirudoterapia

This study demonstrated that site-directed mutagenesis of residues controlling Na+ binding to thrombin can profoundly alter the enzyme's properties, shifting the balance between procoagulant and anticoagulant activities by reducing specificity toward fibrinogen while enhancing or slightly reducing specificity toward protein C. The relevance to ASH's domain is indirect at best: thrombin is the target of leech-derived hirudin, and engineering thrombin's allosteric properties conceptually parallels the anticoagulant goals of leech therapy, but the study involves no leeches, no hirudin, and no leech-derived substances. It is a protein engineering study of a human enzyme with no direct hirudotherapy content.

Citación

Rational engineering of activity and specificity in a serine protease.

Dang et al. · Nature biotechnology, 1997

Contexto clínico relacionado

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

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