title: Chemical synthesis and biological activity of the gelatinase biosynthesis-activating pheromone of Enterococcus faecalis and its analogs.
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.
authors.affiliation: Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Japan. ajiro@mail.ecc.u-tokyo.ac.jp
authors.forename: J
authors.initials: J
authors.lastname: Nakayama
authors.forename: Y
authors.initials: Y
authors.lastname: Cao
authors.forename: T
authors.initials: T
authors.lastname: Horii
authors.forename: S
authors.initials: S
authors.lastname: Sakuda
authors.forename: H
authors.initials: H
authors.lastname: Nagasawa
mesh_terms: D000595:Amino Acid Sequence; D013293:Enterococcus faecalis / Q000378:metabolism*; D007783:Lactones / Q000138:chemical synthesis* / Q000494:pharmacology*; D010456:Peptides, Cyclic / Q000138:chemical synthesis* / Q000494:pharmacology*; D010675:Pheromones / Q000138:chemical synthesis* / Q000494:pharmacology*; D013329:Structure-Activity Relationship
chemical_list: D007783:Lactones; D010456:Peptides, Cyclic; D010675:Pheromones; C438382:gelatinase biosynthesis-activating pheromone