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

Jiro Nakayama, Yong Cao, Takaaki Horii, Shohei Sakuda, Hiromichi Nagasawa

Research output: Contribution to journalArticle

43 Citations (Scopus)

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 languageEnglish
Pages (from-to)2322-2325
Number of pages4
JournalBioscience, Biotechnology and Biochemistry
Volume65
Issue number10
DOIs
Publication statusPublished - Oct 1 2001

Fingerprint

Gelatinases
Enterococcus faecalis
Lactones
Bioactivity
pheromones
bioactive properties
biosynthesis
lactones
synthesis
Biosynthesis
Serine Proteases
Structure-Activity Relationship
Peptide Hydrolases
serine proteinases
structure-activity relationships
Peptides
proteinases
peptides
gelatinase biosynthesis-activating pheromone

All Science Journal Classification (ASJC) codes

  • Food Science
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biotechnology
  • Chemistry (miscellaneous)
  • Applied Microbiology and Biotechnology

Cite this

Chemical synthesis and biological activity of the gelatinase biosynthesis-activating pheromone of enterococcus faecalis and its analogs. / Nakayama, Jiro; Cao, Yong; Horii, Takaaki; Sakuda, Shohei; Nagasawa, Hiromichi.

In: Bioscience, Biotechnology and Biochemistry, Vol. 65, No. 10, 01.10.2001, p. 2322-2325.

Research output: Contribution to journalArticle

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