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Polyfunctionality of lysozyme destabilase from the medicinal leech

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An Erratum to this article was published on 01 November 2009

Abstract

Experimental data indicating the polyfunctionality of lysozyme destabilase from the salivary gland secretion of the medicinal leech, a unique representative of invertebrate lysozymes, were analyzed. The destabilase combines the properties of endo-ɛ-lysyl-γ-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 under many pathological conditions, including thrombosis, is considered from the viewpoint of its further application in practice.

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Abbreviations

SGS:

the salivary gland secretion

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Authors and Affiliations

  1. Faculty of Biology, Moscow State University, Vorob’evy gory, Moscow, 119992, Russia

    I. P. Baskova

  2. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 117997, Russia

    L. L. Zavalova

Authors
  1. I. P. Baskova
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  2. L. L. Zavalova
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Correspondence to I. P. Baskova.

Additional information

Original Russian Text © I.P. Baskova, L.L. Zavalova, 2008, published in Bioorganicheskaya Khimiya, 2008, Vol. 34, No. 3, pp. 337–343.

An erratum to this article can be found online at http://dx.doi.org/10.1134/S1068162009060156

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Baskova, I.P., Zavalova, L.L. Polyfunctionality of lysozyme destabilase from the medicinal leech. Russ J Bioorg Chem 34, 304–309 (2008). https://doi.org/10.1134/S1068162008030096

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  • DOI: https://doi.org/10.1134/S1068162008030096

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