Structural and Functional Characterization of β−lytic Protease from <i>Lysobacter capsici</i> VKM B−2533<sup>T</sup>
The crystal structure of the <i>Lysobacter capsici</i> VKM B−2533<sup>T</sup> 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 acti...
| Main Authors: | , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2022-12-01
|
| Series: | International Journal of Molecular Sciences |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1422-0067/23/24/16100 |
| Summary: | The crystal structure of the <i>Lysobacter capsici</i> VKM B−2533<sup>T</sup> 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 <i>Pseudomonas aeruginosa</i>, 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. |
|---|---|
| ISSN: | 1661-6596 1422-0067 |