A new bacteriolytic amidase Ami of Lysobacter capsici XL1.

One of the most pressing issues in modern biomedicine is the search for new antimicrobial agents - antibiotics, peptides, bacteriolytic enzymes. This study, using transcriptomic and proteomic approaches, identified a new extracellular bacteriolytic enzyme of Lysobacter capsici XL1 - the amidase Ami. The enzyme was isolated and characterized. Ami was found to hydrolyze the amide bond between the carbohydrate and peptide fragments in bacterial peptidoglycans of chemotypes A1γ, A3α, and A4α. Ami lysed live target cells of opportunistic bacteria Micrococcus luteus Ac-2230(T), Bacillus cereus 217, Staphylococcus aureus 209P, Enterococcus faecium FS86, phytopathogenic bacteria Bacillus megaterium MS941, Curtobacterium flaccumfaciens pv. flaccumfaciens, and pathogenic bacteria of various strains of B. anthracis, including plasmid strains 71/12 and ΔAmes, as well as strains of B. cereus with hemolytic, lecithinase, and phosphatase activities. Thus, the bacteriolytic amidase Ami is a promising candidate for the development of next-generation antimicrobial drugs.