ArticleApplied microbiology and biotechnology2018
Structural and functional properties of antimicrobial protein L5 of Lysоbacter sp. XL1.
Article in Applied microbiology and biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 8 citations in OpenAlex.
- Substrate Specificity and Peptide Motif Preferences of β-Lytic and L5 Proteases fromInternational journal of molecular sciences · 2025Article
- A new bacteriolytic amidase Ami of Lysobacter capsici XL1.Scientific reports · 2025Article
- Development of Efficient Expression Systems for Bacteriolytic Proteases L1 and L5 ofInternational journal of molecular sciences · 2025Article
- Transcriptomic Analysis Followed by the Isolation of Extracellular Bacteriolytic Proteases fromInternational journal of molecular sciences · 2023Article
- The First Homologous Expression System for the β-Lytic Protease ofInternational journal of molecular sciences · 2022Article
- Deletion ofFrontiers in microbiology · 2021Article
- β-Lytic Protease ofAntibiotics (Basel, Switzerland) · 2020Article
- Lytic potential of Lysobacter capsici VKM B-2533Scientific reports · 2020Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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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