« Previous AbstractMolecular mechanism of peptide-specific pheromone signaling in Enterococcus faecalis: functions of pheromone receptor TraA and pheromone-binding protein TraC encoded by plasmid pPD1    Next AbstractGelatinase biosynthesis-activating pheromone: a peptide lactone that mediates a quorum sensing in Enterococcus faecalis »

Biosci Biotechnol Biochem

Title:		Chemical synthesis and biological activity of the gelatinase biosynthesis-activating pheromone of Enterococcus faecalis and its analogs
Author(s):		Nakayama J; Cao Y; Horii T; Sakuda S; Nagasawa H;
Address:		"Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Japan. ajiro@mail.ecc.u-tokyo.ac.jp"
Journal Title:		Biosci Biotechnol Biochem
Year:		2001
Volume:		65
Issue:		10
Page Number:		2322 - 2325
DOI:		10.1271/bbb.65.2322
ISSN/ISBN:		0916-8451 (Print) 0916-8451 (Linking)
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"
Keywords:		"Amino Acid Sequence Enterococcus faecalis/*metabolism Lactones/*chemical synthesis/*pharmacology Peptides, Cyclic/*chemical synthesis/*pharmacology Pheromones/*chemical synthesis/*pharmacology Structure-Activity Relationship;"
Notes:		"MedlineNakayama, J Cao, Y Horii, T Sakuda, S Nagasawa, H eng England 2002/01/05 Biosci Biotechnol Biochem. 2001 Oct; 65(10):2322-5. doi: 10.1271/bbb.65.2322"