Destabilase-lysozyme of medicinal leech. Multifunctionality of recombinant protein

作者：Zavalova L L; Lazarev V N; Levitsky S A; Yudina T G; Baskova I P^*

来源：Biochemistry-Moscow, 2010, 75(9): 1173-1181.

DOI：10.1134/S0006297910090129

• endo-epsilon-(gamma-Glu)-Lys- and exo-epsilon-(gamma-Glu)-Lys-isopeptidolysis
• specific glycosidase activity
• 4-methylumbelliferyl-N-acetyl-beta-chitotetraoxide
• muramidase activity
• antibacterial activity
• Methanosarcina barkeri

Preparation and purification of a recombinant protein are described along with characteristics of its specific (for E >-(gamma-Glu)-Lys and D-dimer substrates) and nonspecific (for L-gamma-Glu-pNA) isopeptidase activities; the absence of peptidase function for alpha-(alpha-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-methylum-belliferyl-tetra-N-acetyl-beta-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.

• 出版日期2010-9