Chemical Synthesis and Biological Activity of The Gelatinase Biosynthesis-Activating Pheromone of Enterococcus faecalis and Its Analogs
| Autor: | Yong Cao, Hiromichi Nagasawa, Shohei Sakuda, Jiro Nakayama, Takaaki Horii |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Proteases
Peptides Cyclic Applied Microbiology and Biotechnology Biochemistry Pheromones Enterococcus faecalis Analytical Chemistry Microbiology Lactones Structure-Activity Relationship chemistry.chemical_compound Biosynthesis Gelatinase biosynthesis-activating pheromone Gelatinase Amino Acid Sequence Molecular Biology chemistry.chemical_classification Serine protease biology Organic Chemistry Biological activity General Medicine biology.organism_classification Enzyme chemistry biology.protein Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 65:2322-2325 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1271/bbb.65.2322 |
| Popis: | An 11-residue peptide lactone, termed the gelatinase biosynthesis-activating pheromone (GBAP), triggers the production of the pathogenicity-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. |
| Databáze: | OpenAIRE |
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