Molecular Characterization of a Novel Lytic Enzyme LysC from <i>Clostridium intestinale</i> URNW and Its Antibacterial Activity Mediated by Positively Charged <i>N</i>-Terminal Extension

Molecular Characterization of a Novel Lytic Enzyme LysC from <i>Clostridium intestinale</i> URNW and Its Antibacterial Activity Mediated by Positively Charged <i>N</i>-Terminal Extension

Peptidoglycan hydrolytic enzymes are considered to be a promising alternative to conventional antibiotics in combating bacterial infections. To identify novel hydrolytic enzymes, we performed a database search with the sequences of two thermostable endolysins with high bactericidal activity, studied...

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Bibliographic Details
Main Authors: Magdalena Plotka, Monika Szadkowska, Maria Håkansson, Rebeka Kovačič, Salam Al-Karadaghi, Björn Walse, Olesia Werbowy, Anna-Karina Kaczorowska, Tadeusz Kaczorowski
Format: Article
Language:English
Published: MDPI AG 2020-07-01
Series:International Journal of Molecular Sciences
Subjects:
bacteriophage
endolysin
autolysin
antimicrobial peptide
peptidoglycan
<i>Staphylococcus aureus</i>
Online Access:https://www.mdpi.com/1422-0067/21/14/4894

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