Genes from the medicinal leech Hirudo medicinalis coding for unusual enzymes that specifically cleave endo-epsilon (gamma-Glu)-Lys isopeptide bonds and help to dissolve blood clots
Research article published in Molecular & general genetics (1996)
Abstract
We previously detected in salivary gland secretions of the medicinal leech (Hirudo medicinalis) a novel enzymatic activity, endo-epsilon(gamma-Glu)-Lys isopeptidase, which cleaves isopeptide bonds formed by transglutaminase (Factor XIIIa) between glutamine gamma-carboxamide and the epsilon-amino group of lysine. Such isopeptide bonds, either within or between protein polypeptide chains are formed in many biological processes. However, before we started our work no enzymes were known to be capable of specifically splitting isopeptide bonds in proteins. The isopeptidase activity we detected was specific for isopeptide bonds. The enzyme was termed destabilase. Here we report the first purification of destabilase, part of its amino acid sequence isolation and sequencing of two related cDNAs derived from the gene family that encodes destabilase proteins, and the detection of isopeptidase activity encoded by one of these cDNAs cloned in a baculovirus expression vector. The deduced mature protein products of these cDNAs contain 115 and 116 amino acid residues, including 14 highly conserved Cys residues, and are formed from precursors containing specific leader peptides. No homologous sequences were found in public databases.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Resumen
Genes from the medicinal leech Hirudo medicinalis coding for unusual enzymes that specifically cleave endo-epsilon (gamma-Glu)-Lys isopeptide bonds and help to dissolve blood clots.
Por qué esto importa para la hirudoterapia
This study reports the purification and molecular characterization of destabilase, a novel enzyme from Hirudo medicinalis salivary gland secretions that specifically cleaves endo-epsilon(gamma-Glu)-Lys isopeptide bonds formed by transglutaminase (Factor XIIIa). The authors purified the enzyme, determined partial amino acid sequence, isolated two related cDNAs encoding mature proteins of 115 and 116 residues with 14 conserved Cys residues, and confirmed isopeptidase activity from one cloned cDNA in a baculovirus expression system; no homologous sequences were found in public databases. This is directly relevant to ASH's domain as it characterizes a distinct enzyme from the medicinal leech that targets isopeptide bonds formed in biological processes. However, the work is biochemical in nature—purification and molecular cloning—and the abstract does not report in vivo efficacy, clinical data, or specify which biological processes are affected.
Citación
Genes from the medicinal leech Hirudo medicinalis coding for unusual enzymes that specifically cleave endo-epsilon (gamma-Glu)-Lys isopeptide bonds and help to dissolve blood clots
Zavalova LL et al. · Molecular & general genetics, 1996
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Añadido a la biblioteca ASH: May 27, 2026 · Última actualización del sitio: June 18, 2026