Chemical synthesis and biological activity of the gelatinase biosynthesis-activating pheromone of Enterococcus faecalis and its analogs.
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.
Nakayama
J
J
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Japan. ajiro@mail.ecc.u-tokyo.ac.jp
Cao
Y
Y
Horii
T
T
Sakuda
S
S
Nagasawa
H
H
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
D007783:Lactones; D010456:Peptides, Cyclic; D010675:Pheromones; C438382:gelatinase biosynthesis-activating pheromone