Latency, thermal stability, and identification of an inhibitory compound of mirolysin, a secretory protease of the human periodontopathogen Tannerella forsythia

Latency, thermal stability, and identification of an inhibitory compound of mirolysin, a secretory protease of the human periodontopathogen Tannerella forsythia

Mirolysin is a secretory protease of Tannerella forsythia, a member of the dysbiotic oral microbiota responsible for periodontitis. In this study, we show that mirolysin latency is achieved by a “cysteine-switch” mechanism exerted by Cys23 in the N-terminal profragment. Mutation of Cys23 shortened t...

Full description

Bibliographic Details
Main Authors: Krzysztof M. Zak, Mark J. Bostock, Irena Waligorska, Ida B. Thøgersen, Jan J. Enghild, Grzegorz M. Popowicz, Przemyslaw Grudnik, Jan Potempa, Miroslaw Ksiazek
Format: Article
Language:English
Published: Taylor & Francis Group 2021-01-01
Series:Journal of Enzyme Inhibition and Medicinal Chemistry
Subjects:
periodontitis
proteolysis
tannerella forsythia
nmr-based fragment screening
protease inhibitors
Online Access:http://dx.doi.org/10.1080/14756366.2021.1937619

Internet

http://dx.doi.org/10.1080/14756366.2021.1937619

Similar Items