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...

Täydet tiedot

Tallennettuna:
Bibliografiset tiedot
Julkaisussa:J Enzyme Inhib Med Chem
Päätekijät: Zak, Krzysztof M., Bostock, Mark J., Waligorska, Irena, Thøgersen, Ida B., Enghild, Jan J., Popowicz, Grzegorz M., Grudnik, Przemyslaw, Potempa, Jan, Ksiazek, Miroslaw
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: Taylor & Francis 2021
Aiheet:
Original Article
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC8259862/
https://ncbi.nlm.nih.gov/pubmed/34210221
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1080/14756366.2021.1937619
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