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

被引：39

作者：

Nakayama, J ^{[1
]}

Cao, Y ^{[1
]}

Horii, T ^{[1
]}

Sakuda, S ^{[1
]}

Nagasawa, H ^{[1
]}

机构：

[1] Univ Tokyo, Grad Sch Agr & Life Sci, Dept Appl Biol Chem, Bunkyo Ku, Tokyo, Japan

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2001年 / 65卷 / 10期

关键词：

gelatinase biosynthesis-activating pheromone; Enterococcus faecalis; peptide lactone; peptide pheromone; quorum sensing;

D O I：

10.1271/bbb.65.2322

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：2322 / 2325

页数：4

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