Destabilase Isopeptidase Activity
Isopeptidase domain of destabilase that cleaves cross-linked fibrin — distinct from lysozyme domain.
Preclinical / mechanisticLast updated: 2026-05-26 · Reviewed by ASH Editorial Board
Mechanistic Evidence Box
Preclinical / mechanistic- Page type
- Compound profile
- Evidence type
- Isopeptidase domain of destabilase that cleaves cross-linked fibrin — distinct from lysozyme domain.
- Evidence level
- In vitro
- Drug vs leech
- Purified natural compound
- Safety domains
- Bleeding
Clinical translation limit
Destabilase's isopeptidase activity against cross-linked fibrin is documented in vitro and in limited animal studies; this does NOT establish clinical efficacy as a thrombolytic. No FDA-approved derivative exists.
Molecular Profile
- Category
- Fibrinolytic
- Evidence tier
- Preclinical
- Molecular weight
- 12,500 Da
- Source species
- Hirudo medicinalis
- PDB structures
- 6OJ9
Biological Targets
- → ε-(γ-Glu)-Lys isopeptide bonds in cross-linked fibrin
Key Citations
- Kurdyumov AS et al. (2015), BMC Biochem · PMID 26589324
- Manuvera VA et al. (2015), Protein Expr Purif · PMID 26277552
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-2
Second isoform of destabilase — lysozyme / isopeptidase activity targeting cross-linked fibrin.