학술논문
Structural and Functional Characterization of β−lytic Protease from Lysobacter capsici VKM B−2533T
Document Type
article
Author
Source
International Journal of Molecular Sciences, Vol 23, Iss 24, p 16100 (2022)
Subject
Language
English
ISSN
1422-0067
1661-6596
1661-6596
Abstract
The crystal structure of the Lysobacter capsici VKM B−2533T β-lytic protease (Blp), a medicinally promising antimicrobial enzyme, was first solved. Blp was established to possess a folding characteristic of the M23 protease family. The groove of the Blp active site, as compared with that of the LasA structural homologue from Pseudomonas aeruginosa, was found to have amino acid differences. Biochemical analysis revealed no differences in the optimal reaction conditions for manifesting Blp and LasA bacteriolytic activities. At the same time, Blp had a broader range of action against living and autoclaved target cells. The results suggest that the distinction in the geometry of the active site and the charge of amino acid residues that form the active site groove can be important for the hydrolysis of different peptidoglycan types in target cells.