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Biosci Biotechnol Biochem. 2001 Oct;65(10):2322-5.

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

Author information

1
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Japan. ajiro@mail.ecc.u-tokyo.ac.jp

Abstract

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.

PMID:
11758932
DOI:
10.1271/bbb.65.2322
[Indexed for MEDLINE]
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