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.[2]
| Gelatinase biosynthesis activating pheromone | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | fsrD | ||||||
| UniProt | G8ADN7 | ||||||
| |||||||
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]
References edit
- ^ Teixeira N, Santos S, Marujo P, Yokohata R, Iyer VS, Nakayama J, Hancock LE, Serror P, Silva Lopes Mde F (2012). "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. doi:10.1099/mic.0.055574-0. PMC 4083509. PMID 22117005.
- ^ a b Nishiguchi K, Nagata K, Tanokura M, Sonomoto K, Nakayama J (2009). "Structure-activity relationship of gelatinase biosynthesis-activating pheromone of Enterococcus faecalis". J. Bacteriol. 191 (2): 641–50. doi:10.1128/JB.01029-08. PMC 2620804. PMID 18996993.