Chemical synthesis and biological activity of the gelatinase biosynthesis-activating pheromone of enterococcus faecalis and its analogs

Article abstract of DOI:10.1271/bbb.65.2322

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.

Full text of DOI:10.1271/bbb.65.2322

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Chemical Synthesis and Biological Activity of The
Gelatinase Biosynthesis-Activating Pheromone of
Enterococcus faecalis and Its Analogs
Jiro NAKAYAMAab, Yong CAOa, Takaaki HORIIa, Shohei SAKUDAa & Hiromichi NAGASAWAa
a Department of Applied Biological Chemistry, Graduate School of Agricultural and Life
Sciences, The University of Tokyo
b Present affiliation: Department of Bioscience and Biotechnology, Faculty of
Agriculture, Kyushu University
Published online: 22 May 2014.
To cite this article: Jiro NAKAYAMA, Yong CAO, Takaaki HORII, Shohei SAKUDA & Hiromichi NAGASAWA (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, DOI: 10.1271/bbb.65.2322
To link to this article: http://dx.doi.org/10.1271/bbb.65.2322
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