title: [Polyfunctionality of destabilase, a lysozyme from a medicinal leech].
abstract: Experimental data indicating the polyfunctionality of destabilase, a lysozyme from the salivary gland secretion of the medicinal leech, a unique representative of invertebrate lysozymes, were analyzed. The destabilase combines the properties of endo-s-lysyl-y-glutamyl isopeptidase (D-dimer monomerase), lysozyme, and chitinase and simultaneously is a nonenzymatic antimicrobial agent. The polypeptide sequence of lysozyme destabilase is encoded by a family of three genes (Ds1, Ds2, and Ds3). The ability of the enzyme to hydrolyze endoisopeptide bonds formed by transglutaminases, which are detected in many pathological conditions, including thrombosis, is considered from the viewpoint of its further application in practice.
authors.forename: I P
authors.initials: IP
authors.lastname: Baskova
authors.forename: L L
authors.initials: LL
authors.lastname: Zavalova
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D010450:Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D047709:Hirudo medicinalis / Q000201:enzymology*; D008969:Molecular Sequence Data
chemical_list: D010450:Endopeptidases; C045348:fibrin destabilase