Gelatinase biosynthesis-activating pheromone explained
Gelatinase biosynthesis activating pheromone |
Organism: | Enterococcus faecalis |
Taxid: | 1351 |
Symbol: | fsrD |
Uniprot: | G8ADN7 |
Gelatinase biosynthesis-activating pheromone abbreviated as GBAP is a cyclic peptide produced by pathogenic bacteria such as Enterococcus faecalis.[1] GAP is part of the quorum sensing system of certain bacteria where it positively regulates the expression of gelatinase and serine proteases that are under the control of the gelE-sprE operon.
GBAP is an 11-amino-acid-residue cyclic peptide containing a lactone linkage between the C-terminal carboxylic acid group and a serine side chain hydroxyl group.[2]
Notes and References
- Teixeira N, Santos S, Marujo P, Yokohata R, Iyer VS, Nakayama J, Hancock LE, Serror P, Silva Lopes Mde F . The incongruent gelatinase genotype and phenotype in Enterococcus faecalis are due to shutting off the ability to respond to the gelatinase biosynthesis-activating pheromone (GBAP) quorum-sensing signal . Microbiology . 158 . Pt 2 . 519–28 . 2012 . 22117005 . 10.1099/mic.0.055574-0 . 4083509.
- Nishiguchi K, Nagata K, Tanokura M, Sonomoto K, Nakayama J . Structure-activity relationship of gelatinase biosynthesis-activating pheromone of Enterococcus faecalis . J. Bacteriol. . 191 . 2 . 641–50 . 2009 . 18996993 . 2620804 . 10.1128/JB.01029-08 .