Destabilase-lysozyme of medicinal leech. Multifunctionality of recombinant protein

Preparation and purification of a recombinant protein are described along with characteristics of its specific (for ε-(γ-Glu)-Lys and D-dimer substrates) and nonspecific (for L-γ-Glu-pNA) isopeptidase activities; the absence of peptidase function for α-(α-Glu)-Lys substrate is noted. It is shown that the protein exhibits muramidase (cell walls of Micrococcus lysodeikticus) and specific glycosidase activities. The latter was determined towards the fluorogenic substrate 4-methylumbelliferyl-tetra-N-acetyl-β-chitotetraoxide. Antimicrobial activity of recombinant destabilase-lysozyme protein (recDest-Lys) and its 11-membered amphipathic peptide was revealed towards cells of the strict anaerobic Archaean Methanosarcina barkeri, whose cell walls contain no murein. Possible mechanisms of the effect of recDest-Lys on these cells are discussed.

Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.

Recombinant destabilase-lysozyme exhibits muramidase, isopeptidase and antimicrobial activity against M. barkeri.

Leech-derived molecules this paper discusses, each with a full profile in the ASH compound registry:

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