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A substitution at His-120 in the LasA protease of Pseudomonas aeruginosa blocks enzymatic activity without affecting propeptide processing or extracellular secretion.
The LasA protease of Pseudomonas aeruginosa can degrade elastin and is an important contributor to the pathogenesis of this organism. LasA (20 kDa) is a member of the beta-lytic endopeptidase family of extracellular bacterial proteases, and it shows high-level staphylolytic activity. We sequenced th...
Sparad:
| Huvudupphovsmän: | , , |
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| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
1996
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC178548/ https://ncbi.nlm.nih.gov/pubmed/8932318 |
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