Destabilase-3
Paralog variant of destabilase identified in Hirudo medicinalis sialotranscriptome — isopeptidase/lysozyme bifunctional family member.
Preclínico / mecanísticoLast updated: 2026-05-26 · Reviewed by ASH Editorial Board
Mechanistic Evidence Box
Preclinical / mechanistic- Page type
- Compound profile
- Evidence type
- Paralog variant of destabilase identified in Hirudo medicinalis sialotranscriptome — isopeptidase/lysozyme bifunctional family member.
- Evidence level
- In vitro
- Drug vs leech
- Purified natural compound
- Safety domains
- Bleeding
Clinical translation limit
Destabilase-3's predicted bifunctional activity (isopeptidase + lysozyme) does NOT establish clinical efficacy as a thrombolytic or antimicrobial agent. No FDA-approved derivative exists.
Molecular Profile
- Category
- Fibrinolytic
- Evidence tier
- Preclinical
- Molecular weight
- 12,500 Da
- Source species
- Hirudo medicinalis
- Discovered
- 2018
Biological Targets
- → ε-(γ-Glu)-Lys isopeptide bonds in cross-linked fibrin
- → bacterial peptidoglycan
Key Citations
- Zavalova LL et al. (2014), Biomed Khim · PMID 25019395
External Resources
Related Fibrinolytic Compounds
Destabilase
Lysozyme with isopeptidase activity that dissolves stabilized fibrin clots — including aged thrombi resistant to tPA.
Hementerin
Direct fibrinogenolytic enzyme — degrades fibrinogen independently of plasmin.
Hementin
Direct fibrinogenolytic enzyme cleaving fibrinogen alpha-chain at unique sites — independent of plasmin.
Destabilase Isopeptidase Activity
Isopeptidase domain of destabilase that cleaves cross-linked fibrin — distinct from lysozyme domain.