Structural and Functional Characterization of β−lytic Protease from <i>Lysobacter capsici</i> VKM B−2533<sup>T</sup>

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...

Full description

Bibliographic Details
Main Authors: Alexey Afoshin, Svetlana Tishchenko, Azat Gabdulkhakov, Irina Kudryakova, Inna Galemina, Dmitry Zelenov, Elena Leontyevskaya, Sofia Saharova, Natalya Leontyevskaya (Vasilyeva)
Format: Article
Language:English
Published: MDPI AG 2022-12-01
Series:International Journal of Molecular Sciences
Subjects:
β−lytic protease
<i>Lysobacter capsici</i>
bacteriolytic enzymes
Blp crystal structure
LasA
MRSA
Online Access:https://www.mdpi.com/1422-0067/23/24/16100

Similar Items

Similar Items