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Begunova, E. A.; Stepnaya, O. A.; Lysanskaya, V. Ya.; Kulaev, I. S.

doi:10.1023/a:1025074714910

Biochemistry (Moscow)

2003

DOI: 10.1023/a:1025074714910

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E. A. Begunova

O. A. Stepnaya

V. Ya. Lysanskaya

et al.

Abstract: Specificity of Staphylococcus aureus 209P cell wall hydrolysis by the L1 and L2-bacteriolytic enzymes from lysoamidase lytic complex was studied. L1-peptidase was shown to display both glycyl-glycine endopeptidase and N-acetylmuramyl-L-alanine amidase enzymatic activities on the S. aureus peptidoglycan molecule, whereas L2-peptidase acts as N-acetylmuramyl-L-alanine amidase.

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Cited by 14 publications

(2 citation statements)

References 6 publications

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Investigations of bacteriolytic enzymes destroying bacterial cell walls are important since these enzymes are necessary for the vital functions of the bacterial cell itself and for the interaction of the organisms in natural ecosys tems. One of the proteases (L 1 ), being an endopeptidase according to the classification of the bacteriolytic enzymes [4], also exhibits N acetyl muramoyl L alanine amidase activity [5,6], and the other (L 2 ) is N acetyl muramoyl L alanine amidase [6 8]. In addition, bacteriolytic enzymes can be used as medications against pathogenic bacteria that cause different infectious diseases [1].

Extracellular bacteriolytic enzymes of Lysobacter sp.

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confidence: 99%

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Isolation and Characterization of a New Extracellular Bacteriolytic Endopeptidase of Lysobacter sp. XL1

Stepnaya

Tsfasman

Logvina

et al. 2005

Biochemistry (Moscow)

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The previously unstudied bacteriolytic enzyme L(4) was isolated from the culture liquid of the bacterium Lysobacter sp. XL1 in electrophoretically homogeneous state. The enzyme L(4) is a diaminopimelinoyl-alanine endopeptidase relative to peptidoglycan of Lysobacter sp. XL1. The enzyme is an alkaline protein of approximately 21 kD. The N-terminal amino acid sequence of the enzyme has been determined - A V V N G V N Y V Gx T T A ... The maximal activity of the enzyme was observed in 0.05 M Tris-HCl at pH 8.0 and 50-55 degrees C. The half-inactivation temperature of the enzyme is 52 degrees C. The endopeptidase L(4) is not a metalloenzyme since it is not affected by EDTA. The enzyme is inhibited by p-chloromercuribenzoic acid by 72% and by phenylmethylsulfonyl fluoride by 43%, which indicates the involvement of serine and thiol groups in its functioning.

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“…

Extracellular bacteriolytic enzymes of Lysobacter sp.

…”

mentioning

confidence: 99%

“…One of the proteases (L 1 ), being an endopeptidase according to the classification of the bacteriolytic enzymes [4], also exhibits N acetyl muramoyl L alanine amidase activity [5,6], and the other (L 2 ) is N acetyl muramoyl L alanine amidase [6 8]. XL1 are the main components of the antibacterial prepa ration lysoamidase [2].…”

mentioning

confidence: 99%

Isolation and Characterization of a New Extracellular Bacteriolytic Endopeptidase of Lysobacter sp. XL1

Stepnaya

Tsfasman

Logvina

et al. 2005

Biochemistry (Moscow)

Self Cite

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Outer membrane vesicles of Lysobacter sp. XL1: biogenesis, functions, and applied prospects

Kudryakova

Shishkova

Vasilyeva

2016

Appl Microbiol Biotechnol

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Outer membrane vesicles (OMVs) produced by Gram-negative bacteria have been intensively investigated in recent times. Vesicle formation models have been proposed, some factors affecting the process were established, and important roles vesicles play in vital activities of their producing cells were determined. Studies of pathogenic bacterial vesicles contribute to understanding the causes of acute infection and developing drugs on their basis. Despite intensive research, issues associated with the understanding of vesicle biogenesis, the mechanisms of bacterium-bacterium and pathogen-host interactions with participation of vesicles, still remain unresolved. This review discusses some results obtained in the research into OMVs of Lysobacter sp. XL1 VKM B-1576. This bacterium secretes into the environment a spectrum of bacteriolytic enzymes that hydrolyze peptidoglycan of competing bacteria, thus leading to their lysis. One of these enzymes, lytic endopeptidase L5, has been shown not only to be secreted by means of vesicles but also to be involved in their formation. As part of vesicles, the antimicrobial potential of L5 enzyme has been found to be considerably expanded. Vesicles have been shown to have a therapeutic effect in respect of anthrax infection and staphylococcal sepsis modelled in mice. The scientific basis for constructing liposomal antimicrobial preparations from vesicle phospholipids and recombinant bacteriolytic enzyme L5 has been formed.

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Structural and functional properties of antimicrobial protein L5 of Lysоbacter sp. XL1

Kudryakova

Габдулхаков

Tishchenko

et al. 2018

Appl Microbiol Biotechnol

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The Gram-negative bacterium Lysobacter sp. XL1 secretes into the extracellular space five bacteriolytic enzymes that lyse the cell walls of competing microorganisms. Of special interest are homologous lytic proteases L1 and L5. This work found protein L5 to possess Gly-Gly endopeptidase and N-acetylmuramoyl-L-Ala amidase activities with respect to staphylococcal peptidoglycan. Protein L5 was found to be capable of aggregating into amyloid-like fibril structures. The crystal structure of protein L5 was determined at a 1.60-Å resolution. Protein L5 was shown to have a rather high structural identity with bacteriolytic protease L1 of Lysobacter sp. XL1 and α-lytic protease of Lysobacter enzymogenes at a rather low identity of their amino acid sequences. Still, the structure of protein L5 was revealed to have regions that differed from their equivalents in the homologs. The revealed structural distinctions in L5 are suggested to be of importance in exhibiting its unique properties.

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Untitled

Cited by 14 publications

References 6 publications

Isolation and Characterization of a New Extracellular Bacteriolytic Endopeptidase of Lysobacter sp. XL1

Isolation and Characterization of a New Extracellular Bacteriolytic Endopeptidase of Lysobacter sp. XL1

Outer membrane vesicles of Lysobacter sp. XL1: biogenesis, functions, and applied prospects

Structural and functional properties of antimicrobial protein L5 of Lysоbacter sp. XL1

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