Abstract
An 11-residue peptide lactone, termed the gelatinase biosynthesis-activating pheromone (GBAP), triggers the production of the pathogenicit)-related extracellular proteases, gelatinase and serine protease, in Enterococcus faecalis. In this study, we synthesized GBAP and its analogs and examined their gelatinase biosynthesis-inducing activity. This study on the structure-activity relationship shows that a lactone ring was indispensable for the activity.
| Original language | English |
|---|---|
| Pages (from-to) | 2322-2325 |
| Number of pages | 4 |
| Journal | Bioscience, Biotechnology and Biochemistry |
| Volume | 65 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - Oct 1 2001 |
All Science Journal Classification (ASJC) codes
- Food Science
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biotechnology
- Chemistry (miscellaneous)
- Applied Microbiology and Biotechnology
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Cite this
Nakayama, J., Cao, Y., Horii, T., Sakuda, S., & Nagasawa, H. (2001). Chemical synthesis and biological activity of the gelatinase biosynthesis-activating pheromone of enterococcus faecalis and its analogs. Bioscience, Biotechnology and Biochemistry, 65(10), 2322-2325. https://doi.org/10.1271/bbb.65.2322